Browse result page of ThPDB2
This is the result page of the browse module of ThPDB2. This page gives the information about the query submitted by the user as per the browse category. Further details of the entries can be seen by clicking on the ID or THPP_ID. Further the user can sort the entries on the basis of various fields by clicking on the respective headers. The user can also download the results in various formats.
Tabular representation:
| ID | THPP_ID | Therapeutic Name | Sequence | Molecular Weight | Chemical Formula | Isoelectric Point | Hydrophobicity | Melting Point | Half Life | Description | Disease/Indication | Pharmacodynamics | Mechanism of Action | Toxicity | Metabolism | Absorption | Volume of Distribution | Clearance | Categories | Patent Number | Date of Issue | Date of Expiry | Drug Interaction | Target | Brand Name | Company | Brand Description | Prescribed for | Chemical Name | Formulation | Physical Appearance | Route of Administation | Recommended Dosage | Contraindication | Side Effects | Useful Links 1 | Useful Links 2 | Remarks |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| 10470 | Th1084 | Becaplermin | >Th1084_Becaplermin SLGSLTIAEPAMIAECKTRTEVFEISRRLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQCRPTQVQLRPVQVRKIEIVRKKPIFKKATVTLEDHLACKCETVAAARPVT | 12294.4 | C532H892N162O153S9 | 9.38 | -0.16 | NA | NA | Recombinant platelet derived growth factor (PDGF), the gene for B chain, produced in yeast by cloning and expression of, Saccharomyces cerevisiae. Molecular weight ~25 KD is the homodimer composed of two identical polypeptide chains linked by disulfide bonds. | For topical treatment of skin ulcers (from diabetes) | Used for the topical treatment of skin ulcers, Regranex has a biological activity similar to that of endogenous platelet-derived growth factor, which includes promoting the chemotactic recruitment and proliferation of cells involved in wound repair and enhancing the formation of granulation tissue. | Binds to the beta platelet-derived growth factor (PDGF) receptor, a tyrosine kinase receptor. PDGF is known to exist as a dimer, and activates its signaling pathway by a ligand induced receptor dimerization and autophosphorylation. PDGF receptors also contain many auto-phosphorylation sites, which serve to mediate binding of SH2 sites and subsequently signal corresponding pathways. There are five different isoforms of PDGF that activate through two different receptors (alpha and beta). | NA | NA | very little systemic absorption. 15% of patients experienced complete healing within 8 weeks, while for 25% of patients, it was at 10 weeks. | NA | NA | Acids,Acids, Noncarboxylic,Alimentary Tract and Metabolism,Amino Acids, Peptides, and Proteins,Angiogenesis Inducing Agents,Angiogenesis Modulating Agents,Anions,Biological Factors,Blood Proteins,Cicatrizants,Dermatologicals,DNA-Binding Proteins,Electrolytes,Growth Substances,Hematologic Agents,Human Platelet-derived Growth Factor,Intercellular Signaling Peptides and Proteins,Ions,Neoplasm Proteins,Oncogene Proteins,Peptides,Phosphoric Acids,Phosphorus Acids,Phosphorus Compounds,Platelet-Derived Growth Factor,Preparations for Treatment of Wounds and Ulcers,Proteins,Proto-Oncogene Proteins,Proto-Oncogene Proteins c-sis,Stomatological Preparations | CA1340846 | 7-Dec-1999 | 7-Oct-2005 | NA | Platelet-derived growth factor receptor beta,Platelet-derived growth factor receptor alpha,Alpha-2-macroglobulin | REGRANEX | OMJ Pharmaceuticals, Inc. San German, Puerto Rico | OMJ Pharmaceuticals, Inc. San German, Puerto Rico | for the treatment of lower extremity diabetic neuropathic ulcers that extend into the subcutaneous tissue or beyond and have an adequate blood supply, when used as an adjunct to, and not a substitute for, good ulcer care practices including initial sharp debridement, pressure relief and infection control. | NA | 0.01 % clear to straw-colored gel | Gel: 0.01 %; clear, colorless to straw-colored gel | For topical use; not for oral, ophthalmic or intra | Gel to be applied will vary depending upon the size of the ulcer area. | A very serious allergic reaction to this drug is rare. However, seek immediate medical attention if you notice any symptoms of a serious allergic reaction, including: rash, itching/swelling (especially of the face/tongue/throat), severe dizziness, trouble breathing. | hives; difficulty breathing; swelling of your face, lips, tongue, or throat. | Link | NA | NA |
| 13160 | Th1388 | Bovine type I collagen | >Th1388_Bovine_type_I_collagen MFSFVDLRLLLLLAATALLTHGQEEGQEEGQEEDIPPVTCVQNGLRYHDRDVWKPVPCQICVCDNGNVLCDDVICDELKDCPNAKVPTDECCPVCPEGQESPTDQETTGVEGPKGDTGPRGPRGPAGPPGRDGIPGQPGLPGPPGPPGPPGPPGLGGNFAPQLSYGYDEKSTGISVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAPGPAGARGNDGATGAAGPPGPTGPAGPPGFPGAVGAKGEGGPQGPRGSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPSGPPGPKGNSGEPGAPGSKGDTGAKGEPGPTGIQGPPGPAGEEGKRGARGEPGPAGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGAPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMGFPGPKGAAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGPPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGANGAPGNDGAKGDAGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGAPGKDGVRGLTGPIGPPGPAGAPGDKGEAGPSGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDAGAKGDAGPPGPAGPAGPPGPIGNVGAPGPKGARGSAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPAGKEGSKGPRGETGPAGRPGEVGPPGPPGPAGEKGAPGADGPAGAPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKSGDRGETGPAGPAGPIGPVGARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPPGPPGSPGEQGPSGASGPAGPRGPPGSAGSPGKDGLNGLPGPIGPPGPRGRTGDAGPAGPPGPPGPPGPPGPPSGGYDLSFLPQPPQEKAHDGGRYYRADDANVVRDRDLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSVAQKNWYISKNPKEKRHVWYGESMTGGFQFEYGGQGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKALLLQGSNEIEIRAEGNSRFTYSVTYDGCTSHTGAWGKTVIEYKTTKTSRLPIIDVAPLDVGAPDQEFGFDVGPACFL | NA | NA | NA | NA | NA | NA | Bovine collagen alpha-1 is a naturally occurring extracellular matrix protein which is found in tendons and other connective tissues. It plays a vital role in cell growth, differentiation, attachment, and migration [L2481]. Often combined with other ingredients, such as fibroblasts and keratinocytes, it allows for accelerated and effective wound healing [L2427], [L2450]. Excellagen, a topical gel of bovine type I collagen, is used in the management of wounds including: partial and full- thickness wounds, pressure ulcers, venous ulcers, diabetic ulcers, chronic vascular ulcers, tunneled/undermined wounds, surgical wounds (donor sites/graft, post-Moh’s surgery, post-laser surgery, podiatric, wound dehiscence), trauma wounds (abrasions, lacerations, second-degree burns and skin tears) and draining wounds [L2500]. Bovine type I collagen is also used as a health supplement for bones and joints [A32698]. Interestingly, bovine type I collagen has been studied as a possible endovascular stent material, and has demonstrated promising results in rabbits [A32696]. | For the management of wounds including: partial and full- thickness wounds, pressure ulcers, venous ulcers, diabetic ulcers, chronic vascular ulcers, tunneled/undermined wounds, surgical wounds (donor sites/graft, post-Moh’s dermatological surgery, post-laser surgery, podiatric, wound dehiscence), trauma wounds (abrasions, lacerations, second-degree burns and skin tears) and draining wounds [L2500]. Gintuit (Allogeneic Cultured Keratinocytes and Fibroblasts in Bovine Collagen) is an allogeneic cellularized scaffold product indicated for topical (non-submerged) application to a surgically created vascular wound bed in the treatment of mucogingival conditions in adults. It uses bovine collagen as a matrix to support the growth of keratinocytes and fibroblasts in wound healing [L2450]. Other products using bovine type 1 collagen include PriMatrix, Integra, Orcel and Matriderm [L2490]. Orcel is a bilayered cellular matrix in which normal human allogeneic skin cells (both epidermal keratinocytes and dermal fibroblasts) are cultured in two separate layers into a Type I bovine collagen sponge, indicated in venous leg ulcers and diabetic foot. Type I bovine collagen acts as a matrix for the growth and proliferation of fibroblasts and keratinocytes, offering structure and support [L2427]. In the laboratory, bovine Collagen Type I purified protein standard is used as a control for SDS-PAGE, Western Blot, ELISA, immunoprecipitation, and for other immunological assays [L2488]. | Collagen-based ingredients are very important for tissue engineering and regenerative medicine because of its superior human biocompatibility and low immunogenicity [L2492]. Bovine Collagen Type I belongs to a family of proteins found particularly in the flesh and connective tissues of mammals (approximately 1/3 of the body's total protein). More than two dozen types of collagen have been discovered; Type I is the most abundant form in the body. This type of collagen is found in scar tissue, tendons, the skin, arterial wall, the cornea, muscles, cartilage, and in certain parts of bones and teeth. Bovine Collagen Type I is ideal for investigators studying in extracellular matrix proteins and osteoporosis [L2488]. Type I collagen is the primary organic component of the extracellular matrix in the bone and can play an imperative role in bone tissue engineering. Type I collagen (bovine) is the basis of several laboratory and pharmaceutical products including Collapat II, Healos, Collagraft, and Biostite, among others [L2489]. | Collagen is a fibrillar protein that forms the conjunctive and connective tissues in the human body, including the skin, joints, and bones. This molecule is one of the most predominant in many living organisms, owing to its connective role in biological structures [L2492]. Collagen as a general substance is the most abundant structural protein in the human body that provides support to numerous tissues such as tendons, skin, and teeth (collagen joined to mineral crystals). All proteins that have a structure based on three helix structured polypeptidic chains [L2492]. Bovine collagen is used most frequently out of naturally-sourced collagen, due to its biocompatibility with human beings [L2492]. When applied to a wound surface, bovine type I collagen absorbs wound fluid and maintains a moist wound environment, which is optimal for healing [L2485]. Numerous studies have demonstrated that the use of type I collagen matrices is capable of promoting osteogenic differentiation and mineralization of marrow stromal cells as well as human adipose stem cells. Another study demonstrated that a collagen scaffold (Gingistat) is appropriate for supporting the distribution of cells to form bone tissue [L2489]. | Elevated anti-collagen antibody levels have been detected in patients treated with clinical doses of injectable collagen, even in the absence of adverse cutaneous reactions [A32697]. Antibodies to both native type I bovine and human collagen can lead to a variety of symptoms including joint inflammation, edema at the injection site of bovine collagen implant and fever, as late as 6 months after injection [A32702], [A32703]. Products derived from bovine tissues, especially gelatine, tallow and dicalcium phosphate have been studied in relation to bovine spongiform encephalopathy (BSE) and Creutzfeld-Jacob disease (CJD) [A32698]. The risk of BSE and CJD is dependent on many factors, including the country of origin of the bovine collagen, the health of the cattle from which the collagen is obtained, and practices during processing. Denaturation temperature is a particularly important parameter, depending on the collagen origin and hydration level [A32699]. According to the World Health Organization (WHO), prolonged alkaline treatment, filtration, and heat sterilization (= 138o C for = 4 sec) or an equivalent process on gelatin is a safe practice in preventing BSE [L2497]. The collagen manufacturing process may have some steps in common with the manufacture of gelatin such as alkaline and sodium sulfate treatment, calcium hydroxide and sodium hydroxide treatments or enzyme treatment. These common steps can, however, differ in duration and pH condition which can result in significant differences in their prion inactivation capacity. Manufacturers should at least conduct a process evaluation based on the similarities of the collagen processing steps, as compared to known inactivation steps in the manufacture of gelatin, to support the safety of the product. Outside of the processing steps, differences also exist in the final use of the material and, as a result, in their risk assessment, while gelatin is widely used for oral administration, many collagen applications are in the form of implants. This should be considered in the final risk assessment of type I bovine collagen products [L2498]. According to the EMA (European medicines agency), collagen produced from tissues such as hides, skins, tendons, and sinews do not usually present a measurable TSE risk provided that contamination with potentially infected materials, for example, spillage of blood and/or central nervous tissues, is avoided during procurement. Hides represent a safer raw material for human implants derived from collagen. However, cross-contamination with brain material released during the slaughtering process, possibly dried on the surface of hides is difficult to eliminate. This is another aspect to consider in the evaluation of the safety of bovine type I collagen [L2497]. | NA | NA | NA | NA | Allogeneic Cultured Cell Scaffold | NA | NA | NA | NA | NA | Gintuit | Organogenesis | Organogenesis | Topical | NA | NA | The most common adverse reactions observed in the clinical trials (≥1%) included sinusitis, nasopharyngitis, respiratory tract infections, aphthous stomatitis, and the local effects of oral surgery. | Gintuit, Allogeneic Cultured Keratinocytes and Fibroblasts in Bovine Collagen, is a cellular sheet that contains allogeneic human cells, human extracellular matrix proteins, and bovine collagen for topical application in the oral cavity. Gintuit appears off-white in color and is comprised of two main layers: an upper cornified layer formed by keratinocytes, and a lower layer constructed of bovine-derived collagen, human extracellular matrix proteins, and dermal fibroblasts. These components interact and produce the final bilayered structure. Gintuit does not contain Langerhans cells, melanocytes, macrophages, lymphocytes, blood vessels, or hair follicles. | Gintuit (Allogeneic Cultured Keratinocytes and Fibroblasts in Bovine Collagen) is an allogeneic cellularized scaffold product indicated for topical (non-submerged) application to a surgically created vascular wound bed in the treatment of mucogingival conditions in adults. | NA | NA | Link | Link | NA |
| 13361 | Th1398 | Thrombin alfa | >Th1398_Thrombin_alfa MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE | NA | NA | NA | NA | NA | Following intravenous administration, thrombin alfa exhibited an initial half-life of 0.17 hours (10.2 min) [L2079]. Following either intravenous or subcutaneous administration, the agent demonstrated a terminal half-life of about 15 hours [L2079]. This data follows administration of thrombin alfa to cynomolgus monkeys. | Thrombin Alfa is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. Thrombin Alfa is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. Thrombin Alfa precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. The cell line used to manufacture Thrombin Alfa has been tested and shown to be free of known infectious agents. The cell culture process used in the manufacture of Thrombin Alfa employs no additives of human or animal origin. The purification process includes solvent-detergent treatment and nano-filtration steps dedicated to viral clearance. The thrombin alfa product ultimate comes from recombinant human prethrombin-1 [L2079]. Nevertheless, because the incidence of hemostasis within a timely manner is relatively comparable between the use of thrombin alfa and the placebo treatment in patient subjects, thrombin alfa is not currently approved by certain organizations like the European Medicines Agency [L2079]. | Indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age [FDA Label]. Additionally, thrombin alfa can be used in conjunction with an absorbable gelatin sponge, USP [FDA Label]. | As thrombin alfa, a recombinant thrombin, is considered to be identical in amino acid sequence and structural similarity to naturally occurring human thrombin, it is believed that thrombin alfa shares the same pharmacodynamics as endogenous or natural human thrombin coagulation factor [L2079]. In the natural blood coagulation pathway of the human body, thrombin functions as a coagulation factor that converts clotting factor XI to XIa, factor VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa [A32408]. Specifically, clotting factor XIIIa is a transglutaminase that catalyzes the formation of covalent bonds between the lysine and glutamine residues found in fibrin. These covalent bonds assist in increasing the stability of the fibrin clot [A32408]. Additionally, thrombin also promotes the activation and aggregation of platelets by way of activating protease-activated receptors on the cell membranes of platelets [A32408]. | Specifically, thrombin alfa is a human serine protease that promotes hemostasis and acts locally when applied topically to a site of bleeding [FDA Label]. In particular, thrombin alfa activates platelets and cleaves fibrinogen to fibrin, leading directly to clot formation. It also activates clotting factor XIII, leading to fibrin cross-linking and clot stability [FDA Label, L2079]. The ability of thrombin alfa to bypass the initial enzymatic steps of the coagulation pathway provides a clear rationale as to why thrombin alfa may be used as a topical haemostatic agent [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Data regarding overdosage are not available. The predominant adverse reaction associated with thrombin alfa is the possibility of thrombosis or other thromboembolic events occurring [FDA Label]. | Much like endogenous thrombin, thrombin alfa does not circulate in the blood as a free, active molecule for very long [FDA Label]. After performing its function it is rapidly inactivated after formation of complexes with various circulating endogenous plasma inhibitors (like antithrombin III) [FDA Label, L2079]. This rapid inactivation prevents the active agent from diffusing into the general circulation. The complexes formed are then generally cleared and eliminated by the liver [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Nevertheless, observations of a subcutaneous administration of 350 U rhThrombin/kg resulted in a bioavailability of approximately 95% in male cynomolgus monkeys [L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Volume of distribution data is subsequently not readily available. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Regardless, thrombin alfa, like natural thrombin, is known to be rapidly neutralized by naturally circulating plasma inhibitors limiting its duration of action and preventing the active form from diffusing into the general circulation [L2079]. | Amino Acids, Peptides, and Proteins | NA | NA | NA | NA | Coagulation factor V,Coagulation factor VIII,Fibrinogen alpha chain,Fibrinogen beta chain,Fibrinogen gamma chain | Recothrom | The Medicines Company | The Medicines Company | Topical | 1000 [iU]/1mL | Do not inject directly into the circulatory system. Do not use for the treatment of massive or brisk arterial bleeding. Do not administer to patients with a history of hypersensitivity to RECOTHROM or any components of RECOTHROM. Do not use in patients with known hypersensitivity to hamster proteins. | blood clots detaching from their point of origin and moving through the bloodstream (thromboembolic events), and antibody formation. | RECOTHROM, Thrombin topical (Recombinant), is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. RECOTHROM is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. RECOTHROM precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. | RECOTHROM®, Thrombin topical (Recombinant), is a topical thrombin indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age. | NA | NA | Link | Link | NA |
| 13362 | Th1398 | Thrombin alfa | >Th1398_Thrombin_alfa MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE | NA | NA | NA | NA | NA | Following intravenous administration, thrombin alfa exhibited an initial half-life of 0.17 hours (10.2 min) [L2079]. Following either intravenous or subcutaneous administration, the agent demonstrated a terminal half-life of about 15 hours [L2079]. This data follows administration of thrombin alfa to cynomolgus monkeys. | Thrombin Alfa is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. Thrombin Alfa is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. Thrombin Alfa precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. The cell line used to manufacture Thrombin Alfa has been tested and shown to be free of known infectious agents. The cell culture process used in the manufacture of Thrombin Alfa employs no additives of human or animal origin. The purification process includes solvent-detergent treatment and nano-filtration steps dedicated to viral clearance. The thrombin alfa product ultimate comes from recombinant human prethrombin-1 [L2079]. Nevertheless, because the incidence of hemostasis within a timely manner is relatively comparable between the use of thrombin alfa and the placebo treatment in patient subjects, thrombin alfa is not currently approved by certain organizations like the European Medicines Agency [L2079]. | Indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age [FDA Label]. Additionally, thrombin alfa can be used in conjunction with an absorbable gelatin sponge, USP [FDA Label]. | As thrombin alfa, a recombinant thrombin, is considered to be identical in amino acid sequence and structural similarity to naturally occurring human thrombin, it is believed that thrombin alfa shares the same pharmacodynamics as endogenous or natural human thrombin coagulation factor [L2079]. In the natural blood coagulation pathway of the human body, thrombin functions as a coagulation factor that converts clotting factor XI to XIa, factor VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa [A32408]. Specifically, clotting factor XIIIa is a transglutaminase that catalyzes the formation of covalent bonds between the lysine and glutamine residues found in fibrin. These covalent bonds assist in increasing the stability of the fibrin clot [A32408]. Additionally, thrombin also promotes the activation and aggregation of platelets by way of activating protease-activated receptors on the cell membranes of platelets [A32408]. | Specifically, thrombin alfa is a human serine protease that promotes hemostasis and acts locally when applied topically to a site of bleeding [FDA Label]. In particular, thrombin alfa activates platelets and cleaves fibrinogen to fibrin, leading directly to clot formation. It also activates clotting factor XIII, leading to fibrin cross-linking and clot stability [FDA Label, L2079]. The ability of thrombin alfa to bypass the initial enzymatic steps of the coagulation pathway provides a clear rationale as to why thrombin alfa may be used as a topical haemostatic agent [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Data regarding overdosage are not available. The predominant adverse reaction associated with thrombin alfa is the possibility of thrombosis or other thromboembolic events occurring [FDA Label]. | Much like endogenous thrombin, thrombin alfa does not circulate in the blood as a free, active molecule for very long [FDA Label]. After performing its function it is rapidly inactivated after formation of complexes with various circulating endogenous plasma inhibitors (like antithrombin III) [FDA Label, L2079]. This rapid inactivation prevents the active agent from diffusing into the general circulation. The complexes formed are then generally cleared and eliminated by the liver [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Nevertheless, observations of a subcutaneous administration of 350 U rhThrombin/kg resulted in a bioavailability of approximately 95% in male cynomolgus monkeys [L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Volume of distribution data is subsequently not readily available. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Regardless, thrombin alfa, like natural thrombin, is known to be rapidly neutralized by naturally circulating plasma inhibitors limiting its duration of action and preventing the active form from diffusing into the general circulation [L2079]. | Biological Factors | NA | NA | NA | NA | Coagulation factor V,Coagulation factor VIII,Fibrinogen alpha chain,Fibrinogen beta chain,Fibrinogen gamma chain | Recothrom | Zymo Genetics | Zymo Genetics | Topical | 1000 [iU]/1mL | Do not inject directly into the circulatory system. Do not use for the treatment of massive or brisk arterial bleeding. Do not administer to patients with a history of hypersensitivity to RECOTHROM or any components of RECOTHROM. Do not use in patients with known hypersensitivity to hamster proteins. | blood clots detaching from their point of origin and moving through the bloodstream (thromboembolic events), and antibody formation. | RECOTHROM, Thrombin topical (Recombinant), is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. RECOTHROM is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. RECOTHROM precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. | RECOTHROM®, Thrombin topical (Recombinant), is a topical thrombin indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age. | NA | NA | Link | Link | NA |
| 13363 | Th1398 | Thrombin alfa | >Th1398_Thrombin_alfa MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE | NA | NA | NA | NA | NA | Following intravenous administration, thrombin alfa exhibited an initial half-life of 0.17 hours (10.2 min) [L2079]. Following either intravenous or subcutaneous administration, the agent demonstrated a terminal half-life of about 15 hours [L2079]. This data follows administration of thrombin alfa to cynomolgus monkeys. | Thrombin Alfa is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. Thrombin Alfa is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. Thrombin Alfa precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. The cell line used to manufacture Thrombin Alfa has been tested and shown to be free of known infectious agents. The cell culture process used in the manufacture of Thrombin Alfa employs no additives of human or animal origin. The purification process includes solvent-detergent treatment and nano-filtration steps dedicated to viral clearance. The thrombin alfa product ultimate comes from recombinant human prethrombin-1 [L2079]. Nevertheless, because the incidence of hemostasis within a timely manner is relatively comparable between the use of thrombin alfa and the placebo treatment in patient subjects, thrombin alfa is not currently approved by certain organizations like the European Medicines Agency [L2079]. | Indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age [FDA Label]. Additionally, thrombin alfa can be used in conjunction with an absorbable gelatin sponge, USP [FDA Label]. | As thrombin alfa, a recombinant thrombin, is considered to be identical in amino acid sequence and structural similarity to naturally occurring human thrombin, it is believed that thrombin alfa shares the same pharmacodynamics as endogenous or natural human thrombin coagulation factor [L2079]. In the natural blood coagulation pathway of the human body, thrombin functions as a coagulation factor that converts clotting factor XI to XIa, factor VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa [A32408]. Specifically, clotting factor XIIIa is a transglutaminase that catalyzes the formation of covalent bonds between the lysine and glutamine residues found in fibrin. These covalent bonds assist in increasing the stability of the fibrin clot [A32408]. Additionally, thrombin also promotes the activation and aggregation of platelets by way of activating protease-activated receptors on the cell membranes of platelets [A32408]. | Specifically, thrombin alfa is a human serine protease that promotes hemostasis and acts locally when applied topically to a site of bleeding [FDA Label]. In particular, thrombin alfa activates platelets and cleaves fibrinogen to fibrin, leading directly to clot formation. It also activates clotting factor XIII, leading to fibrin cross-linking and clot stability [FDA Label, L2079]. The ability of thrombin alfa to bypass the initial enzymatic steps of the coagulation pathway provides a clear rationale as to why thrombin alfa may be used as a topical haemostatic agent [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Data regarding overdosage are not available. The predominant adverse reaction associated with thrombin alfa is the possibility of thrombosis or other thromboembolic events occurring [FDA Label]. | Much like endogenous thrombin, thrombin alfa does not circulate in the blood as a free, active molecule for very long [FDA Label]. After performing its function it is rapidly inactivated after formation of complexes with various circulating endogenous plasma inhibitors (like antithrombin III) [FDA Label, L2079]. This rapid inactivation prevents the active agent from diffusing into the general circulation. The complexes formed are then generally cleared and eliminated by the liver [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Nevertheless, observations of a subcutaneous administration of 350 U rhThrombin/kg resulted in a bioavailability of approximately 95% in male cynomolgus monkeys [L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Volume of distribution data is subsequently not readily available. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Regardless, thrombin alfa, like natural thrombin, is known to be rapidly neutralized by naturally circulating plasma inhibitors limiting its duration of action and preventing the active form from diffusing into the general circulation [L2079]. | Blood Coagulation Factors | NA | NA | NA | NA | Coagulation factor V,Coagulation factor VIII,Fibrinogen alpha chain,Fibrinogen beta chain,Fibrinogen gamma chain | Recothrom | Baxter Healthcare Corporation | Baxter Healthcare Corporation | Topical | 1000 [iU]/1mL | Do not inject directly into the circulatory system. Do not use for the treatment of massive or brisk arterial bleeding. Do not administer to patients with a history of hypersensitivity to RECOTHROM or any components of RECOTHROM. Do not use in patients with known hypersensitivity to hamster proteins. | blood clots detaching from their point of origin and moving through the bloodstream (thromboembolic events), and antibody formation. | RECOTHROM, Thrombin topical (Recombinant), is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. RECOTHROM is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. RECOTHROM precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. | RECOTHROM®, Thrombin topical (Recombinant), is a topical thrombin indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age. | NA | NA | Link | Link | NA |
| 13364 | Th1398 | Thrombin alfa | >Th1398_Thrombin_alfa MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE | NA | NA | NA | NA | NA | Following intravenous administration, thrombin alfa exhibited an initial half-life of 0.17 hours (10.2 min) [L2079]. Following either intravenous or subcutaneous administration, the agent demonstrated a terminal half-life of about 15 hours [L2079]. This data follows administration of thrombin alfa to cynomolgus monkeys. | Thrombin Alfa is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. Thrombin Alfa is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. Thrombin Alfa precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. The cell line used to manufacture Thrombin Alfa has been tested and shown to be free of known infectious agents. The cell culture process used in the manufacture of Thrombin Alfa employs no additives of human or animal origin. The purification process includes solvent-detergent treatment and nano-filtration steps dedicated to viral clearance. The thrombin alfa product ultimate comes from recombinant human prethrombin-1 [L2079]. Nevertheless, because the incidence of hemostasis within a timely manner is relatively comparable between the use of thrombin alfa and the placebo treatment in patient subjects, thrombin alfa is not currently approved by certain organizations like the European Medicines Agency [L2079]. | Indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age [FDA Label]. Additionally, thrombin alfa can be used in conjunction with an absorbable gelatin sponge, USP [FDA Label]. | As thrombin alfa, a recombinant thrombin, is considered to be identical in amino acid sequence and structural similarity to naturally occurring human thrombin, it is believed that thrombin alfa shares the same pharmacodynamics as endogenous or natural human thrombin coagulation factor [L2079]. In the natural blood coagulation pathway of the human body, thrombin functions as a coagulation factor that converts clotting factor XI to XIa, factor VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa [A32408]. Specifically, clotting factor XIIIa is a transglutaminase that catalyzes the formation of covalent bonds between the lysine and glutamine residues found in fibrin. These covalent bonds assist in increasing the stability of the fibrin clot [A32408]. Additionally, thrombin also promotes the activation and aggregation of platelets by way of activating protease-activated receptors on the cell membranes of platelets [A32408]. | Specifically, thrombin alfa is a human serine protease that promotes hemostasis and acts locally when applied topically to a site of bleeding [FDA Label]. In particular, thrombin alfa activates platelets and cleaves fibrinogen to fibrin, leading directly to clot formation. It also activates clotting factor XIII, leading to fibrin cross-linking and clot stability [FDA Label, L2079]. The ability of thrombin alfa to bypass the initial enzymatic steps of the coagulation pathway provides a clear rationale as to why thrombin alfa may be used as a topical haemostatic agent [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Data regarding overdosage are not available. The predominant adverse reaction associated with thrombin alfa is the possibility of thrombosis or other thromboembolic events occurring [FDA Label]. | Much like endogenous thrombin, thrombin alfa does not circulate in the blood as a free, active molecule for very long [FDA Label]. After performing its function it is rapidly inactivated after formation of complexes with various circulating endogenous plasma inhibitors (like antithrombin III) [FDA Label, L2079]. This rapid inactivation prevents the active agent from diffusing into the general circulation. The complexes formed are then generally cleared and eliminated by the liver [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Nevertheless, observations of a subcutaneous administration of 350 U rhThrombin/kg resulted in a bioavailability of approximately 95% in male cynomolgus monkeys [L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Volume of distribution data is subsequently not readily available. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Regardless, thrombin alfa, like natural thrombin, is known to be rapidly neutralized by naturally circulating plasma inhibitors limiting its duration of action and preventing the active form from diffusing into the general circulation [L2079]. | Blood Proteins | NA | NA | NA | NA | Coagulation factor V,Coagulation factor VIII,Fibrinogen alpha chain,Fibrinogen beta chain,Fibrinogen gamma chain | Recothrom | Mallinckrodt Hospital Products Inc. | Mallinckrodt Hospital Products Inc. | Topical | 1000 [iU]/1mL | Do not inject directly into the circulatory system. Do not use for the treatment of massive or brisk arterial bleeding. Do not administer to patients with a history of hypersensitivity to RECOTHROM or any components of RECOTHROM. Do not use in patients with known hypersensitivity to hamster proteins. | blood clots detaching from their point of origin and moving through the bloodstream (thromboembolic events), and antibody formation. | RECOTHROM, Thrombin topical (Recombinant), is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. RECOTHROM is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. RECOTHROM precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. | RECOTHROM®, Thrombin topical (Recombinant), is a topical thrombin indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age. | NA | NA | Link | Link | NA |
| 13365 | Th1398 | Thrombin alfa | >Th1398_Thrombin_alfa MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE | NA | NA | NA | NA | NA | Following intravenous administration, thrombin alfa exhibited an initial half-life of 0.17 hours (10.2 min) [L2079]. Following either intravenous or subcutaneous administration, the agent demonstrated a terminal half-life of about 15 hours [L2079]. This data follows administration of thrombin alfa to cynomolgus monkeys. | Thrombin Alfa is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. Thrombin Alfa is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. Thrombin Alfa precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. The cell line used to manufacture Thrombin Alfa has been tested and shown to be free of known infectious agents. The cell culture process used in the manufacture of Thrombin Alfa employs no additives of human or animal origin. The purification process includes solvent-detergent treatment and nano-filtration steps dedicated to viral clearance. The thrombin alfa product ultimate comes from recombinant human prethrombin-1 [L2079]. Nevertheless, because the incidence of hemostasis within a timely manner is relatively comparable between the use of thrombin alfa and the placebo treatment in patient subjects, thrombin alfa is not currently approved by certain organizations like the European Medicines Agency [L2079]. | Indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age [FDA Label]. Additionally, thrombin alfa can be used in conjunction with an absorbable gelatin sponge, USP [FDA Label]. | As thrombin alfa, a recombinant thrombin, is considered to be identical in amino acid sequence and structural similarity to naturally occurring human thrombin, it is believed that thrombin alfa shares the same pharmacodynamics as endogenous or natural human thrombin coagulation factor [L2079]. In the natural blood coagulation pathway of the human body, thrombin functions as a coagulation factor that converts clotting factor XI to XIa, factor VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa [A32408]. Specifically, clotting factor XIIIa is a transglutaminase that catalyzes the formation of covalent bonds between the lysine and glutamine residues found in fibrin. These covalent bonds assist in increasing the stability of the fibrin clot [A32408]. Additionally, thrombin also promotes the activation and aggregation of platelets by way of activating protease-activated receptors on the cell membranes of platelets [A32408]. | Specifically, thrombin alfa is a human serine protease that promotes hemostasis and acts locally when applied topically to a site of bleeding [FDA Label]. In particular, thrombin alfa activates platelets and cleaves fibrinogen to fibrin, leading directly to clot formation. It also activates clotting factor XIII, leading to fibrin cross-linking and clot stability [FDA Label, L2079]. The ability of thrombin alfa to bypass the initial enzymatic steps of the coagulation pathway provides a clear rationale as to why thrombin alfa may be used as a topical haemostatic agent [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Data regarding overdosage are not available. The predominant adverse reaction associated with thrombin alfa is the possibility of thrombosis or other thromboembolic events occurring [FDA Label]. | Much like endogenous thrombin, thrombin alfa does not circulate in the blood as a free, active molecule for very long [FDA Label]. After performing its function it is rapidly inactivated after formation of complexes with various circulating endogenous plasma inhibitors (like antithrombin III) [FDA Label, L2079]. This rapid inactivation prevents the active agent from diffusing into the general circulation. The complexes formed are then generally cleared and eliminated by the liver [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Nevertheless, observations of a subcutaneous administration of 350 U rhThrombin/kg resulted in a bioavailability of approximately 95% in male cynomolgus monkeys [L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Volume of distribution data is subsequently not readily available. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Regardless, thrombin alfa, like natural thrombin, is known to be rapidly neutralized by naturally circulating plasma inhibitors limiting its duration of action and preventing the active form from diffusing into the general circulation [L2079]. | Endopeptidases | NA | NA | NA | NA | Coagulation factor V,Coagulation factor VIII,Fibrinogen alpha chain,Fibrinogen beta chain,Fibrinogen gamma chain | Recothrom | Baxter Laboratories | Baxter Laboratories | Topical | 24000 unit / vial | Do not inject directly into the circulatory system. Do not use for the treatment of massive or brisk arterial bleeding. Do not administer to patients with a history of hypersensitivity to RECOTHROM or any components of RECOTHROM. Do not use in patients with known hypersensitivity to hamster proteins. | blood clots detaching from their point of origin and moving through the bloodstream (thromboembolic events), and antibody formation. | RECOTHROM, Thrombin topical (Recombinant), is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. RECOTHROM is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. RECOTHROM precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. | RECOTHROM®, Thrombin topical (Recombinant), is a topical thrombin indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age. | NA | NA | Link | Link | NA |
| 13366 | Th1398 | Thrombin alfa | >Th1398_Thrombin_alfa MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLERECVEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHVNITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQECSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASAQAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETGDGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFYTHVFRLKKWIQKVIDQFGE | NA | NA | NA | NA | NA | Following intravenous administration, thrombin alfa exhibited an initial half-life of 0.17 hours (10.2 min) [L2079]. Following either intravenous or subcutaneous administration, the agent demonstrated a terminal half-life of about 15 hours [L2079]. This data follows administration of thrombin alfa to cynomolgus monkeys. | Thrombin Alfa is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. Thrombin Alfa is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. Thrombin Alfa precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. The cell line used to manufacture Thrombin Alfa has been tested and shown to be free of known infectious agents. The cell culture process used in the manufacture of Thrombin Alfa employs no additives of human or animal origin. The purification process includes solvent-detergent treatment and nano-filtration steps dedicated to viral clearance. The thrombin alfa product ultimate comes from recombinant human prethrombin-1 [L2079]. Nevertheless, because the incidence of hemostasis within a timely manner is relatively comparable between the use of thrombin alfa and the placebo treatment in patient subjects, thrombin alfa is not currently approved by certain organizations like the European Medicines Agency [L2079]. | Indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age [FDA Label]. Additionally, thrombin alfa can be used in conjunction with an absorbable gelatin sponge, USP [FDA Label]. | As thrombin alfa, a recombinant thrombin, is considered to be identical in amino acid sequence and structural similarity to naturally occurring human thrombin, it is believed that thrombin alfa shares the same pharmacodynamics as endogenous or natural human thrombin coagulation factor [L2079]. In the natural blood coagulation pathway of the human body, thrombin functions as a coagulation factor that converts clotting factor XI to XIa, factor VIII to VIIIa, V to Va, fibrinogen to fibrin, and XIII to XIIIa [A32408]. Specifically, clotting factor XIIIa is a transglutaminase that catalyzes the formation of covalent bonds between the lysine and glutamine residues found in fibrin. These covalent bonds assist in increasing the stability of the fibrin clot [A32408]. Additionally, thrombin also promotes the activation and aggregation of platelets by way of activating protease-activated receptors on the cell membranes of platelets [A32408]. | Specifically, thrombin alfa is a human serine protease that promotes hemostasis and acts locally when applied topically to a site of bleeding [FDA Label]. In particular, thrombin alfa activates platelets and cleaves fibrinogen to fibrin, leading directly to clot formation. It also activates clotting factor XIII, leading to fibrin cross-linking and clot stability [FDA Label, L2079]. The ability of thrombin alfa to bypass the initial enzymatic steps of the coagulation pathway provides a clear rationale as to why thrombin alfa may be used as a topical haemostatic agent [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Data regarding overdosage are not available. The predominant adverse reaction associated with thrombin alfa is the possibility of thrombosis or other thromboembolic events occurring [FDA Label]. | Much like endogenous thrombin, thrombin alfa does not circulate in the blood as a free, active molecule for very long [FDA Label]. After performing its function it is rapidly inactivated after formation of complexes with various circulating endogenous plasma inhibitors (like antithrombin III) [FDA Label, L2079]. This rapid inactivation prevents the active agent from diffusing into the general circulation. The complexes formed are then generally cleared and eliminated by the liver [FDA Label, L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Nevertheless, observations of a subcutaneous administration of 350 U rhThrombin/kg resulted in a bioavailability of approximately 95% in male cynomolgus monkeys [L2079]. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Volume of distribution data is subsequently not readily available. | Traditional absorption, distribution, metabolism, and excretion studies were not/have not been performed for thrombin alfa [L2079]. Regardless, thrombin alfa, like natural thrombin, is known to be rapidly neutralized by naturally circulating plasma inhibitors limiting its duration of action and preventing the active form from diffusing into the general circulation [L2079]. | Enzymes | NA | NA | NA | NA | Coagulation factor V,Coagulation factor VIII,Fibrinogen alpha chain,Fibrinogen beta chain,Fibrinogen gamma chain | Recothrom | Baxter Laboratories | Baxter Laboratories | Topical | 6000 unit / vial | Do not inject directly into the circulatory system. Do not use for the treatment of massive or brisk arterial bleeding. Do not administer to patients with a history of hypersensitivity to RECOTHROM or any components of RECOTHROM. Do not use in patients with known hypersensitivity to hamster proteins. | blood clots detaching from their point of origin and moving through the bloodstream (thromboembolic events), and antibody formation. | RECOTHROM, Thrombin topical (Recombinant), is a human coagulation protein produced via recombinant DNA technology from a genetically modified CHO cell line. RECOTHROM is identical in amino acid sequence and structurally similar to naturally occurring human thrombin. RECOTHROM precursor is secreted to culture medium as single chain form that is proteolytically converted to a two-chain active form (using a protein derived from snakes) and is purified by a chromatographic process that yields a product having hemostatic activities similar to native human thrombin. | RECOTHROM®, Thrombin topical (Recombinant), is a topical thrombin indicated to aid hemostasis whenever oozing blood and minor bleeding from capillaries and small venules is accessible and control of bleeding by standard surgical techniques (such as suture, ligature, or cautery) is ineffective or impractical in adults and pediatric populations greater than or equal to one month of age. | NA | NA | Link | Link | NA |