Detailed description page of ThPDB2
This page displays user query in tabular form. |
Th1047 details |
Primary information | |
---|---|
ID | 10331 |
Therapeutic ID | Th1047 |
Protein Name | Alpha-1-proteinase inhibitor |
Sequence | >Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK |
Molecular Weight | 44324.5 |
Chemical Formula | C2001H3130N514O601S10 |
Isoelectric Point | 5.37 |
Hydrophobicity | -0.302 |
Melting point | 59 |
Half-life | NA |
Description | Human alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation. |
Indication/Disease | For treatment of panacinar emphysema. |
Pharmacodynamics | Prevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema. |
Mechanism of Action | Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. |
Toxicity | NA |
Metabolism | NA |
Absorption | NA |
5632 ± 2006 mL [ARALAST NP] | |
Clearance | 940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg] |
Categories | Acute-Phase Proteins, Alpha-Globulins, Amino Acids, Peptides, and Proteins, Antifibrinolytic Agents, Blood and Blood Forming Organs, Blood Proteins, Enzyme Inhibitors, Enzymes, Enzymes and Coenzymes, Globulins, Glycoproteins, Hemostatics, Human alpha-1 Proteinase Inhibitor, Peptides, Protease Inhibitors, Proteinase Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Serum Globulins, Trypsin Inhibitors |
Patents Number | NA |
Date of Issue | NA |
Date of Expiry | NA |
Drug Interaction | NA |
Target | Neutrophil elastase |
Brand Name | Aralast |
Company | Baxter |
Brand Description | Baxter |
Prescribed For | Its used to treat lung problems (emphysema) caused by a certain inherited disease (alpha-1-proteinase inhibitor deficiency). In people with this condition, lung damage is caused by elastase, a natural substance that the body needs to kill bacteria in the |
Chemical Name | NA |
Formulation | ARALAST NP is available as a lyophilized powder in single dose vials containing 0.5 gram or 1 gram of functional Alpha 1 -Protenase inhibitor |
Physical Appearance | Lyophilized powder |
Route of Administration | Intravenous infusion |
Recommended Dosage | Recommended dose is 60 mg/kg of body weight, administered once in a week. |
Contraindication | ARALAST NP is contraindicated in immunoglobulin A deficient patients with antibodies against IgA, due to the risk of severe hypersensitivity. |
Side Effects | Fever, chills, body aches, flu symptoms, sores in your mouth and throat; pain or burning when you urinate; wheezing, chest pain or tightness, trouble breathing; or vision changes. |
Useful Link 1 | Link |
Useful Link 2 | NA |
Remarks | NA |
Primary information | |
---|---|
ID | 10332 |
Therapeutic ID | Th1047 |
Protein Name | Alpha-1-proteinase inhibitor |
Sequence | >Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK |
Molecular Weight | 44324.5 |
Chemical Formula | C2001H3130N514O601S10 |
Isoelectric Point | 5.37 |
Hydrophobicity | -0.302 |
Melting point | 59 |
Half-life | NA |
Description | Human alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation. |
Indication/Disease | For treatment of panacinar emphysema. |
Pharmacodynamics | Prevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema. |
Mechanism of Action | Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. |
Toxicity | NA |
Metabolism | NA |
Absorption | NA |
5618 ± 1618 mL [Aralast] | |
Clearance | 940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg] |
Categories | Acute-Phase Proteins, Alpha-Globulins, Amino Acids, Peptides, and Proteins, Antifibrinolytic Agents, Blood and Blood Forming Organs, Blood Proteins, Enzyme Inhibitors, Enzymes, Enzymes and Coenzymes, Globulins, Glycoproteins, Hemostatics, Human alpha-1 Proteinase Inhibitor, Peptides, Protease Inhibitors, Proteinase Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Serum Globulins, Trypsin Inhibitors |
Patents Number | NA |
Date of Issue | NA |
Date of Expiry | NA |
Drug Interaction | NA |
Target | NA |
Brand Name | Glassia |
Company | Takeda, Baxalta US Inc. |
Brand Description | Takeda, Baxalta US Inc. |
Prescribed For | treat the symptoms of Alpha-1 Antitrypsin Deficiency. |
Chemical Name | NA |
Formulation | GLASSIA is prepared from human plasma obtained from US-licensed plasma collection centers by a modified version of the cold ethanol fractionation process and the Alpha1 -PI is then purified using chromatographic methods. |
Physical Appearance | sterile, ready to use, liquid preparation of purified human alpha1 -proteinase inhibitor |
Route of Administration | intravenous |
Recommended Dosage | Administer 60 mg/kg body weight of GLASSIA once weekly by intravenous infusion. |
Contraindication | GLASSIA is contraindicated in: immunoglobulin A (IgA) deficient patients with antibodies against IgA. individuals with a history of anaphylaxis or other severe systemic reaction to Alpha11-PI products. |
Side Effects | hives, difficulty breathing, swelling of your face, lips, tongue, or throat, hives, wheezing, lightheadedness, fever, chills, body aches, flu symptoms, sores in your mouth and throat, pain or burning when you urinate, chest pain or tightness, and vision changes |
Useful Link 1 | Link |
Useful Link 2 | NA |
Remarks | NA |
Primary information | |
---|---|
ID | 10333 |
Therapeutic ID | Th1047 |
Protein Name | Alpha-1-proteinase inhibitor |
Sequence | >Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK |
Molecular Weight | 44324.5 |
Chemical Formula | C2001H3130N514O601S10 |
Isoelectric Point | 5.37 |
Hydrophobicity | -0.302 |
Melting point | 59 |
Half-life | NA |
Description | Human alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation. |
Indication/Disease | For treatment of panacinar emphysema. |
Pharmacodynamics | Prevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema. |
Mechanism of Action | Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. |
Toxicity | NA |
Metabolism | NA |
Absorption | NA |
NA | |
Clearance | 940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg] |
Categories | Acute-Phase Proteins, Alpha-Globulins, Amino Acids, Peptides, and Proteins, Antifibrinolytic Agents, Blood and Blood Forming Organs, Blood Proteins, Enzyme Inhibitors, Enzymes, Enzymes and Coenzymes, Globulins, Glycoproteins, Hemostatics, Human alpha-1 Proteinase Inhibitor, Peptides, Protease Inhibitors, Proteinase Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Serum Globulins, Trypsin Inhibitors |
Patents Number | NA |
Date of Issue | NA |
Date of Expiry | NA |
Drug Interaction | NA |
Target | NA |
Brand Name | Respreeza |
Company | Csl Behring |
Brand Description | Csl Behring |
Prescribed For | NA |
Chemical Name | NA |
Formulation | NA |
Physical Appearance | NA |
Route of Administration | NA |
Recommended Dosage | NA |
Contraindication | NA |
Side Effects | NA |
Useful Link 1 | Link |
Useful Link 2 | NA |
Remarks | NA |
Primary information | |
---|---|
ID | 10334 |
Therapeutic ID | Th1047 |
Protein Name | Alpha-1-proteinase inhibitor |
Sequence | >Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK |
Molecular Weight | 44324.5 |
Chemical Formula | C2001H3130N514O601S10 |
Isoelectric Point | 5.37 |
Hydrophobicity | -0.302 |
Melting point | 59 |
Half-life | NA |
Description | Human alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation. |
Indication/Disease | For treatment of panacinar emphysema. |
Pharmacodynamics | Prevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema. |
Mechanism of Action | Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. |
Toxicity | NA |
Metabolism | NA |
Absorption | NA |
NA | |
Clearance | 940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg] |
Categories | Acute-Phase Proteins, Alpha-Globulins, Amino Acids, Peptides, and Proteins, Antifibrinolytic Agents, Blood and Blood Forming Organs, Blood Proteins, Enzyme Inhibitors, Enzymes, Enzymes and Coenzymes, Globulins, Glycoproteins, Hemostatics, Human alpha-1 Proteinase Inhibitor, Peptides, Protease Inhibitors, Proteinase Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Serum Globulins, Trypsin Inhibitors |
Patents Number | NA |
Date of Issue | NA |
Date of Expiry | NA |
Drug Interaction | NA |
Target | NA |
Brand Name | Prolastin |
Company | Talecris Biotherapeutics C formerly Bayer |
Brand Description | Talecris Biotherapeutics C formerly Bayer |
Prescribed For | It is used to treat alpha 1-antitrypsin deficiency in people who have symptoms of emphysema. |
Chemical Name | NA |
Formulation | The specific activity of Prolastin is _ 0.35 mg functional alpha1-PI/mg protein and when reconstituted as directed, the concentration of alpha1-PI is _ 20 mg/mL. When reconstituted, Prolastin (alpha) has a pH of 6.6_7.4, a sodium content of 100_210 mEq/L, |
Physical Appearance | Lyophilized powder |
Route of Administration | Intravenous infusion |
Recommended Dosage | Prolastin (alpha) may be given at a rate of 0.08 mL/kg/min or greater and must be administered intravenously. The recommended dosage of 60 mg/kg takes approximately 30 minutes to infuse. |
Contraindication | Individuals with selective IgA deficiencies who have known antibody against IgA (anti-IgA antibody) should not receive Alpha1-Proteinase Inhibitor (Human), Prolastin (alpha) , since these patients may experience severe reactions, including anaphylaxis, to IgA which may be present. |
Side Effects | Fever, chills, body aches, flu symptoms, sores in your mouth and throat; pain or burning when you urinate; wheezing, chest pain or tightness, trouble breathing; or vision changes. |
Useful Link 1 | Link |
Useful Link 2 | NA |
Remarks | NA |
Primary information | |
---|---|
ID | 10335 |
Therapeutic ID | Th1047 |
Protein Name | Alpha-1-proteinase inhibitor |
Sequence | >Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK |
Molecular Weight | 44324.5 |
Chemical Formula | C2001H3130N514O601S10 |
Isoelectric Point | 5.37 |
Hydrophobicity | -0.302 |
Melting point | 59 |
Half-life | NA |
Description | Human alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation. |
Indication/Disease | For treatment of panacinar emphysema. |
Pharmacodynamics | Prevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema. |
Mechanism of Action | Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. |
Toxicity | NA |
Metabolism | NA |
Absorption | NA |
NA | |
Clearance | 940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg] |
Categories | Acute-Phase Proteins, Alpha-Globulins, Amino Acids, Peptides, and Proteins, Antifibrinolytic Agents, Blood and Blood Forming Organs, Blood Proteins, Enzyme Inhibitors, Enzymes, Enzymes and Coenzymes, Globulins, Glycoproteins, Hemostatics, Human alpha-1 Proteinase Inhibitor, Peptides, Protease Inhibitors, Proteinase Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Serum Globulins, Trypsin Inhibitors |
Patents Number | NA |
Date of Issue | NA |
Date of Expiry | NA |
Drug Interaction | NA |
Target | NA |
Brand Name | Zemaira |
Company | Csl Behring |
Brand Description | Csl Behring |
Prescribed For | to treat alpha 1-antitrypsin deficiency in people who have symptoms of emphysema. |
Chemical Name | NA |
Formulation | Zemaira is manufactured from large pools of human plasma by cold ethanol fractionation according to a modified Cohn process followed by additional purification steps. The manufacturing process includes two virus clearance steps: heat treatment at 60°C for 10 hours in an aqueous solution with stabilizers; and nanofiltration. These virus clearance steps have been validated in a series of in vitro experiments for their capacity to inactivate/ remove both enveloped and non-enveloped viruses. |
Physical Appearance | sterile, white, lyophilized preparation of purified Alpha1-Proteinase Inhibitor |
Route of Administration | intravenous |
Recommended Dosage | The recommended dose of ZEMAIRA is 60 mg/kg body weight administered once weekly. |
Contraindication | ZEMAIRA is contraindicated in patients with a history of anaphylaxis or severe systemic reactions to ZEMAIRA or A1-PI protein. ZEMAIRA is contraindicated in immunoglobulin A (IgA)-deficient patients with antibodies against IgA, due to the risk of severe hypersensitivity |
Side Effects | Nausea, bloating; headache, dizziness, drowsiness; feeling tired; back pain, joint or muscle pain; swelling in your hands or feet; flushing (warmth, redness, or tingly feeling); cold symptoms such as stuffy nose, sneezing, sore throat, cough; or mild itching. |
Useful Link 1 | Link |
Useful Link 2 | NA |
Remarks | NA |
Primary information | |
---|---|
ID | 10336 |
Therapeutic ID | Th1047 |
Protein Name | Alpha-1-proteinase inhibitor |
Sequence | >Th1047_Alpha-1-proteinase_inhibitor EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATAFAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFLSEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDTVFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVLLMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLKSVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSIPPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK |
Molecular Weight | 44324.5 |
Chemical Formula | C2001H3130N514O601S10 |
Isoelectric Point | 5.37 |
Hydrophobicity | -0.302 |
Melting point | 59 |
Half-life | NA |
Description | Human alpha-1 proteinase inhibitor or alpha-1-antitrypsin, prepared from human plasma via Cohn alcohol fractionation followed by PEG and zinc chloride fractionation. |
Indication/Disease | For treatment of panacinar emphysema. |
Pharmacodynamics | Prevents excessive accumulation of active neutrophil elastase and consequent proteolysis of elastin tissues in alveolar lung structures. This prevents the development of emphysema. |
Mechanism of Action | Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) in the lungs. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable. |
Toxicity | NA |
Metabolism | NA |
Absorption | NA |
NA | |
Clearance | 940 ± 275 mL/day [Patients with congenital deficiency with single IV infusion of 60mg/kg] |
Categories | Acute-Phase Proteins, Alpha-Globulins, Amino Acids, Peptides, and Proteins, Antifibrinolytic Agents, Blood and Blood Forming Organs, Blood Proteins, Enzyme Inhibitors, Enzymes, Enzymes and Coenzymes, Globulins, Glycoproteins, Hemostatics, Human alpha-1 Proteinase Inhibitor, Peptides, Protease Inhibitors, Proteinase Inhibitors, Proteins, Serine Protease Inhibitors, Serpins, Serum Globulins, Trypsin Inhibitors |
Patents Number | NA |
Date of Issue | NA |
Date of Expiry | NA |
Drug Interaction | NA |
Target | NA |
Brand Name | NA |
Company | NA |
Brand Description | NA |
Prescribed For | NA |
Chemical Name | NA |
Formulation | NA |
Physical Appearance | NA |
Route of Administration | NA |
Recommended Dosage | NA |
Contraindication | NA |
Side Effects | NA |
Useful Link 1 | Link |
Useful Link 2 | NA |
Remarks | NA |