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IDPMIDYEARSequenceNameLengthN-ter MODC-ter MODLinear/CyclicChiralityChem-MODOriginNatureIncubation TimeConcentrationHalf LifeUnits Half LifeProteaseAssayTest SampleVivo/VitroReferencePatent No.Activity
4019
387372832024
LAEAKVLANRELDKYGVSDFYKRLINKAKTVEGVEALKLHILAALP-FRRG-(E5C3)-(GN)
ABD035-immunoGNNoneP1h3His-tagLinearLHumanized anti-HER2 scFv P1h3, albumin-binding peptides (ABD035 or dAb7h8), cathepsin B-cleavable peptide B2, endosome-disruptive peptide E5C3 fusion protein, GN= Gasdermin-NSynthetic AntitumorBlood samples were promptly collected at 5, 10, 30, 60, 360, and 720 min0.1 μmol/kg35.22BALB/c mice serum proteaseELISABALB/c mice serumIn VivoNoneNoneCytotoxicity of ABD035-immunoGN in N87 cells reached as high as 62 %, compared to 38 % for immunotBid after 24 h of incubation
4020
387372832024
FRRG-(E5C3)-(GN)
immunoGNNoneP1h3His-tagLinearLHumanized anti-HER2 scFv P1h3, albumin-binding peptides (ABD035 or dAb7h8), cathepsin B-cleavable peptide B2, endosome-disruptive peptide E5C3 fusion protein, GN= Gasdermin-NSynthetic AntitumorBlood samples were promptly collected at 5, 10, 30, 60, 360, and 720 min0.1 μmol/kg4.599BALB/c mice serum proteaseELISABALB/c mice serumIn VivoNoneNoneCytotoxicity of ABD035-immunoGN in N87 cells reached as high as 62 %, compared to 38 % for immunotBid after 24 h of incubation
4021
387372832024
DIQMTQSPSSLSAVGDRVTITCRASQSISSYLNWYQQKPGKAPKLLIYRNSPLQSGVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQQTYRVPPTFGQGTKVEIKR-FRRG-(E5C3)-(GN)
dAb7h8-immunoGNNoneP1h3His-tagLinearLHumanized anti-HER2 scFv P1h3, albumin-binding peptides (ABD035 or dAb7h8), cathepsin B-cleavable peptide B2, endosome-disruptive peptide E5C3 fusion protein, GN= Gasdermin-NSynthetic AntitumorBlood samples were promptly collected at 5, 10, 30, 60, 360, and 720 min0.1 μmol/kg31.25BALB/c mice serum proteaseELISABALB/c mice serumIn VivoNoneNoneCytotoxicity of ABD035-immunoGN in N87 cells reached as high as 62 %, compared to 38 % for immunotBid after 24 h of incubation
4048
383994082024
None
BI-XNoneN.A.N.A.N.A.N.A.N.A.SyntheticTreatment Of Human Ocular Diseaseserial blood samples were taken in EDTA anticoagulant pre-dose and at 1 h, 2 h, 4 h, 24 h, 48 h, 72 h, 96 h, and 168 h and 2, 4, 6, 8, and 10 weeks after dosing or until the last in-life timepoint of the animals.0.25 mg/eye3Cynomolgus Monkeys Plasma ProteaseImmunocapture-LC-MS/MSCynomolgus monkeys plasmaIn VivoNoneNoneAffinity binding site to human albumin (KD = 1.4 nM)
4049
383994082024
None
BI-XNoneN.A.N.A.N.A.N.A.N.A.SyntheticTreatment Of Human Ocular Diseaseserial blood samples were taken in EDTA anticoagulant pre-dose and at 1 h, 2 h, 4 h, 24 h, 48 h, 72 h, 96 h, and 168 h and 2, 4, 6, 8, and 10 weeks after dosing or until the last in-life timepoint of the animals.0.25 mg/eye13.2Cynomolgus Monkeys Plasma ProteaseImmunocapture-LC-MS/MSCynomolgus monkeys plasmaIn VivoNoneNoneAffinity binding site to human albumin (KD = 1.4 nM)
4050
383994082024
None
BI-XNoneN.A.N.A.N.A.N.A.N.A.SyntheticTreatment Of Human Ocular Diseaseserial blood samples were taken in EDTA anticoagulant pre-dose and at 1 h, 2 h, 4 h, 24 h, 48 h, 72 h, 96 h, and 168 h and 2, 4, 6, 8, and 10 weeks after dosing or until the last in-life timepoint of the animals.0.25 mg/eye11.8Cynomolgus Monkeys Plasma ProteaseImmunocapture-LC-MS/MSCynomolgus monkeys plasmaIn VivoNoneNoneAffinity binding site to human albumin (KD = 1.4 nM)
4118
388636462024
None
(89Zr, Mn)-WPMNsNoneFreeFreeLinearLMn and 89Zr labeling, MNPs modified with WL12-SH WL12 derivativeTargets PD-L1Blood samples were collected from orbital vein at 1, 3, 5, 10, 15, 20, 30, 45 min and 1, 1.5, 2, 3, 4, 14, 24, 48, 72, 96 h0.5 mg/ml0.1234 (Fast) (Metabolic Half Life)KM mouse blood proteaseRadioactivity assay using γ-counterKM mouse bloodIn VivoNoneNoneN.A.
4119
388636462024
None
(89Zr, Mn)-WPMNsNoneFreeFreeLinearLMn and 89Zr labeling, MNPs modified with WL12-SH WL12 derivativeTargets PD-L1Blood samples were collected from orbital vein at 1, 3, 5, 10, 15, 20, 30, 45 min and 1, 1.5, 2, 3, 4, 14, 24, 48, 72, 96 h0.5 mg/ml1.554 (Slow) (Distribution Half Life)KM mouse blood proteaseRadioactivity assay using γ-counterKM mouse blood sampleIn VivoNoneNoneN.A.
4120
386974232024
None
DAE Rum55NoneN.A.N.A.N.A.DN.A.Ruminococcus sp. CAG55 Epimerase50 °CN.A.4.5 (Activity Half Life)N.A.N.A.N.A.In VitroNoneNoneD-allulose/D-psicose 3-epimerase (DAE/DPE, EC 5.1.3.30) and D-tagatose 3-epimerase (DTE, EC 5.1.3.31), of which DAE usually exhibits higher catalytic activity
4121
386974232024
None
E268R-EKL16NoneN.A.N.A.N.A.N.A.N.A.Ruminococcus sp. CAG55 derivativeEpimerase50 °CN.A.135.3 (Activity Half Life)N.A.N.A.N.A.In VitroNoneNoneD-allulose/D-psicose 3-epimerase (DAE/DPE, EC 5.1.3.30) and D-tagatose 3-epimerase (DTE, EC 5.1.3.31), of which DAE usually exhibits higher catalytic activity
4122
387530952024
None
Xyn10-HBNoneN.A.N.A.N.A.N.A.N.A.GH10 xylanase from Halalkalibacterium halodurans C-125 GH10 xylanasepH 8.5 and 60 °CN.A.3 (Activity Half Life)N.A.N.A.N.A.In VitroNoneNoneXyn10-HB produced active XOS with antioxidant activity determined by the DPPH radical scavenging method (IC50 of 0.54 mg/mL after 4 h)
4123
381152312024
None
Trx1PNoneN.A.N.A.LinearLN.A.Derived from E. coli thioredoxin (Trx).N.A.N.A.N.A.124 ± 15 (T1/2 Cis-Trans Isomerizations)N.A.N.A.N.A.N.A.NoneNoneN.A.
4124
381152312024
None
Trx1ThpNoneN.A.N.A.LinearLIncorporation of 4-thiaproline (Thp) at position cisPro76Derived from E. coli thioredoxin (Trx).N.A.N.A.N.A.33 ± 3 (T1/2 Cis-Trans Isomerizations)N.A.N.A.N.A.N.A.NoneNoneN.A.
4178
378754812023
None
IL-15-Cy7NoneFreeFreeLinearLCy7Derived from Interleukin-15AntitumorThe blood sample was harvested at timed intervals (2 min, 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, 12 h, and 24 h)N.A.0.69Mice blood proteaseFluorescence spectrophotometryMice bloodIn VivoNoneNoneNot mentioned
4179
378754812023
None
biNV-IL-15-Cy7NoneFreeFreeLinearLCy7Derived from Interleukin-15AntitumorThe blood sample was harvested at timed intervals (2 min, 5 min, 15 min, 30 min, 1 h, 2 h, 4 h, 8 h, 12 h, and 24 h)N.A.5.66Mice blood proteaseFluorescence spectrophotometryMice bloodIn VivoNoneNoneNot mentioned
4388
373299002023
None
KAN-101NoneN.A.N.A.N.A.N.A.Liver-targeting glycosylation signature conjugated to a deaminated gliadin peptideN.A.Liver-Targeted Immune Tolerance TherapyN.A.0·15 mg/kg, 0·3 mg/kg, 0·6 mg/kg, 1·2 mg/kg, 1·5 mg/kg3·72 to 31·72 Human proteaseN.A.HumanIn VivoNoneNoneN.A.
4520
360758992022
None
S-20-1NoneN.A.N.A.CyclicLModified by adding negative chargeSyntheticAntiviral (Against Infection By Sars-Cov-2 )Blood samples were collected at 10 min, 20 min, 30 min, 1 h, 2 h, 4 h, 8 h, 24 h and 48 h50 mg/kg14.53 (Terminal Elimination Half Life)C57Bl/6 mice plasma proteaseLC-MS/MSC57BL/6 mice plasmaIn VivoNoneNoneIC50 (μM) = 0.8 in HUH 7 cells
4521
360758992022
None
S-20-1NoneN.A.N.A.CyclicLModified by adding negative chargeSyntheticAntiviral (Against Infection By Sars-Cov-2 )Blood samples were collected at 10 min, 20 min, 30 min, 1 h, 2 h, 4 h, 8 h, 24 h and 48 h50 mg/kg24.29 (Terminal Elimination Half Life)C57Bl/6 mice plasma proteaseLC-MS/MSC57BL/6 mice plasmaIn VivoNoneNoneIC50 (μM) = 0.8 in HUH 7 cells
4522
360472552022
H-r-Dmt-KF-PEG-DSPE, c(RGD)-PEG-DSPE
MTP/RGD-CAL/TAN NSNoneFreeMTP/RGD comodified with CAL/TAN NS LinearL(cRGD), Mix(MTP)Dmt: 2',6'-dimethyltyrosineSyntheticTreatment of Acute Myocardial Infarction (Ami) Blood samples were obtained at determined times until 72 h after injection and 15 μL of heparin (1000 U/mL) was added to each sample10 mg/kg8.22AMI rats plasma proteaseN.A.AMI rats plasmaIn VivoNoneNoneBlank MTP/RGD NS and RGD-PEG-DSPE groups showed over 85% of cell viability. In contrast, drugs contained formulations exhibited cytotoxicity to some extent
4719
EP 2021080747 W2022
None
Test 1NoneN.A.N.A.N.A.N.A.N.A.GLP-1 analogsAntidiabetesBlood samples (0.8 Ml) were taken via the second catheter at predetermined time points (0-3 weeks)10 nmol/kg100 (Terminal Half Life)Minipigs plasma proteaseLC-MSMinipigs plasmaIn VivoNoneEP 2021080747 WN.A.
4720
EP 2021080747 W2022
None
Test 2NoneN.A.N.A.N.A.N.A.N.A.GLP-1 analogsAntidiabetesBlood samples (0.8 Ml) were taken via the second catheter at predetermined time points (0-3 weeks)10 nmol/kg101 (Terminal Half Life)Minipigs plasma proteaseLC-MSMinipigs plasmaIn VivoNoneEP 2021080747 WN.A.
4721
EP 2021080747 W2022
None
Test 3NoneN.A.N.A.N.A.N.A.N.A.GLP-1 analogsAntidiabetesBlood samples (0.8 Ml) were taken via the second catheter at predetermined time points (0-3 weeks)10 nmol/kg105 (Terminal Half Life)Minipigs plasma proteaseLC-MSMinipigs plasmaIn VivoNoneEP 2021080747 WN.A.
4722
EP 2021080747 W2022
None
Test 4NoneN.A.N.A.N.A.N.A.N.A.GLP-1 analogsAntidiabetesBlood samples (0.8 Ml) were taken via the second catheter at predetermined time points (0-3 weeks)10 nmol/kg109 (Terminal Half Life)Minipigs plasma proteaseLC-MSMinipigs plasmaIn VivoNoneEP 2021080747 WN.A.
4755
359102762022
None
BA17NoneFreeFreeLinearLNoneIsolated from B. licheniformisSerine protease50°CN.A.90 (Enzyme Activity)N.A.ZymographyN.A.In VitroNoneNoneN.A.
4756
359102762022
None
BA17NoneFreeFreeLinearLNoneIsolated from B. licheniformisSerine protease60 °CN.A.12 (Enzyme Activity)N.A.ZymographyN.A.In VitroNoneNoneN.A.
4763
354883382022
None
FRAP-smTGNoneFrap (A Fusion Tag)FreeLinearLNoneTGm1 variant Used to generate protein crosslinking or attachment of small molecules60 ℃0.4 mg/mL < 2 (Activity Half Life)N.A.N.A.N.A.N.A.NoneNoneN.A.
4764
354883382022
None
FRAP-TGm1NoneFrap (A Fusion Tag)FreeLinearLNoneTGm1 variant Used to generate protein crosslinking or attachment of small molecules60 ℃0.4 mg/mL 11.31 (Activity Half Life)N.A.N.A.N.A.N.A.NoneNoneN.A.
4765
354883382022
None
FRAPD-TGm1NoneFrap (A Fusion Tag)FreeLinearLadditional modification (Asp residue)TGm1 variant Used to generate protein crosslinking or attachment of small molecules60 ℃0.4 mg/mL 21.97 (Activity Half Life)N.A.N.A.N.A.N.A.NoneNoneN.A.
4770
351338602022
None
E187A NoneFreeFreeLinearLResidue Glu187 of the Ca1 site in the catalytic domain was replaced by AlaDerived from preTSSCollagenolytic protease 70°CN.A.N.A.N.A.N.A.N.A.In Viro Study NoneNoneWhen the residue Glu187 of the Ca1 site in the catalytic domain was replaced by Ala, the resulting variant E187A was completely inactivated after incubation at 70°C for 3 h
4968
336655012021
Poly(L-glutamic acid)
PLG-PtNoneFreeCisplatin (CDDP) is complexed with the carboxyl groups of the L-glutamic acidLinearLNoneSyntheticAnticancerAt predefined time points 5, 15, and 30 min, and 1, 3, 6, 12, and 24 h, 200.0 μL of blood samples were collected from the orbital cavities of rats3 mg/kg1.9Rats plasma proteaseICP-MSRats plasma In VivoNoneNoneIC50 (μg mL−1) = 4.8 in SKOV3 cells 
4969
336655012021
Poly(L-glutamic acid)
PEG-PLG-PtNonePEGylationCisplatin (CDDP) is complexed with the carboxyl groups of the L-glutamic acidLinearLPEGylationSyntheticAnticancerAt predefined time points 5, 15, and 30 min, and 1, 3, 6, 12, and 24 h, 200.0 μL of blood samples were collected from the orbital cavities of rats3 mg/kg8.8Rats plasma proteaseICP-MSRats plasma In VivoNoneNoneIC50 (μg mL−1) = 11 in SKOV3 cells 
4970
336655012021
Poly(L-glutamic acid)
PEG-pHe-PLG-Pt (pH 7.4) NonePEG-CDMCisplatin (CDDP) is complexed with the carboxyl groups of the L-glutamic acidLinearLPoly(L-glutamic acid) is grafted with methoxy poly(ethylene glycol) (PEG) using a pH-sensitive linker, 2-propionic-3-methylmaleic anhydride = CDMSyntheticAnticancerAt predefined time points 5, 15, and 30 min, and 1, 3, 6, 12, and 24 h, 200.0 μL of blood samples were collected from the orbital cavities of rats3 mg/kg7.9Rats plasma proteaseICP-MSRats plasma In VivoNoneNoneIC50 (μg mL−1) = 8.5 in SKOV3 cells 
4971
336655012021
Poly(L-glutamic acid)
PEG-pHe-PLG-Pt (pH 6.5) NonePEG-CDMCisplatin (CDDP) is complexed with the carboxyl groups of the L-glutamic acidLinearLPoly(L-glutamic acid) is grafted with methoxy poly(ethylene glycol) (PEG) using a pH-sensitive linker, CDM = 2-propionic-3-methylmaleic anhydride SyntheticAnticancerAt predefined time points 5, 15, and 30 min, and 1, 3, 6, 12, and 24 h, 200.0 μL of blood samples were collected from the orbital cavities of rats3 mg/kgN.A.Rats plasma proteaseICP-MSRats plasma In VivoNoneNoneIC50 (μg mL−1) = 5.8 in SKOV3 cells 
4972
336655012021
PLGLAG-Poly(L-glutamic acid)
PEG-MMP-PLG-Pt NonePEGylationCisplatin (CDDP) is complexed with the carboxyl groups of the L-glutamic acidLinearLPEGylation through an MMP-sensitive peptide linker (PLGLAG), CDM = 2-propionic-3-methylmaleic anhydride SyntheticAnticancerAt predefined time points 5, 15, and 30 min, and 1, 3, 6, 12, and 24 h, 200.0 μL of blood samples were collected from the orbital cavities of rats3 mg/kg7.8Rats plasma proteaseICP-MSRats plasma In VivoNoneNoneIC50 (μg mL−1) = 6.9 in SKOV3 cells 
5229
320342892020
VL-GGGGSGGGGSGGGGS-VH-GGGGS-KPLPEVTDEY
α-GD2 scFv TMNoneRadiolabelled with 64CuE5B9LinearLVH and VL joined by linker (GGGGS)3SyntheticAntitumorN.A.N.A.1.6Mice blood proteasePET scanningMice blood sampleIn VivoE5B9 sequence available on this link: https://pmc.ncbi.nlm.nih.gov/articles/PMC6805801/NoneEC50 = 0.7 nM (target cell lysis)
5282
324541202020
None
Uox-WTNoneN.A.N.A.N.A.N.A.N.A.SyntheticTreatment of hyperuricemia Incubated for 4 h at room temperature28 μM1.1 (Enzymatic Activity Half Life)Mice serum proteaseUric acid degradation assayMice serumIn VivoNoneNoneN.A.
5283
324541202020
None
Uox-HSANoneN.A.N.A.N.A.N.A.N.A.SyntheticTreatment of hyperuricemia Incubated for 4 h at room temperature28 μM17.4 (Enzymatic Activity Half Life)Mice serum proteaseUric acid degradation assayMice serumIn VivoNoneNoneN.A.
5284
324541202020
None
PEG-PAEU + Uox-HSANoneN.A.N.A.N.A.N.A.N.A.SyntheticTreatment of hyperuricemia Incubated for 4 h at room temperature28 μM43.6 (Enzymatic Activity Half Life)Mice serum proteaseUric acid degradation assayMice serumIn VivoNoneNoneN.A.
5285
324541202020
None
PEG-PAEU-ABP + Uox-HSANoneN.A.N.A.N.A.N.A.N.A.SyntheticTreatment of hyperuricemia Incubated for 4 h at room temperature28 μM96.3 (Enzymatic Activity Half Life)Mice serum proteaseUric acid degradation assayMice serumIn VivoNoneNoneN.A.
5337
314532572019
None
Pept. ANoneFreeFreeCyclicLN.A.N.A.Therapeutic agent against a CNS-related disorderBlood (100 µl) and CSF (100 µl) aliquots for drug concentration assessment were collected pre-dose, on study day 1 at 0.5, 1.5, 3, 6, and 24 h post first dose, and on study day 2 at 1.5 h post the second dose (corresponding to 25.5 h from study start)4.2 mg/kg3.5 ± 0.7 (Terminal Half Life)Göttingen minipigs plasma proteaseLC-MS/MSGöttingen minipigs plasmaIn VivoNoneNoneN.A.
5338
314532572019
None
Pept. ANoneFreeFreeCyclicLN.A.N.A.Therapeutic agent against a CNS-related disorderBlood (100 µl) and CSF (100 µl) aliquots for drug concentration assessment were collected pre-dose, on study day 1 at 0.5, 1.5, 3, 6, and 24 h post first dose, and on study day 2 at 1.5 h post the second dose (corresponding to 25.5 h from study start)4.2 mg/kg14.3 ± 5.5 (Terminal Half Life)göttingen Minipig Csf Lumbar ProteaseLC-MS/MSGöttingen minipigs CSF lumbarIn VivoNoneNoneN.A.
5601
303440182019
None
ASNNoneN.A.N.A.N.A.N.A.N.A.B. cereus BDRD-ST26 (P43-amyE-BcA)Production of acrylamide-free food 50 CN.A.17.35 (Activity Half Life)N.A.N.A.N.A.N.A.NoneNoneKm = 9.38 mM
5602
303440182019
None
ASNNoneN.A.N.A.N.A.N.A.N.A.B. cereus BDRD-ST26 (P43-BcA)Production of acrylamide-free food 50 CN.A.17.57 (Activity Half Life)N.A.N.A.N.A.N.A.NoneNonekm = 9.41 mM
5603
303440182019
None
ASNNoneN.A.N.A.N.A.N.A.N.A.B. subtilis 168Production of acrylamide-free food 65 CN.A.61 (Activity Half Life)N.A.N.A.N.A.N.A.NoneNonekm = 5.3 mM
5604
303440182019
None
ASNNoneN.A.N.A.N.A.N.A.N.A.T. kodakaraensis 1656Production of acrylamide-free food 85 CN.A.130 (Activity Half Life)N.A.N.A.N.A.N.A.NoneNonekm = 5.5 mM
5631
308099012019
None
FITC-AAR029bNoneFluorescein isothiocynate labeledFreeMacrocyclicLNoneDerived from a class of peptides known as cyclic peptide triazoles (cPTs)AntiviralN.A.0.01 mg/kg 0.029 ± 0.01 (T1/2Α-Distribution Half Life)Rats plasma proteaseFluorescence assayRats plasmaIn VivoNoneNoneEC50(nM) = 210±16 for AAR029b in Bal.01 virus
5632
308099012019
None
FITC-AAR029b in LiposomeNoneFluorescein isothiocynate labeledFreeMacrocyclicLNoneDerived from a class of peptides known as cyclic peptide triazoles (cPTs)AntiviralN.A.0.01 mg/kg 0.032 ± 0.005 (T1/2Α-Distribution Half Life)Rats plasma proteaseFluorescence assayRats plasmaIn VivoNoneNoneEC50(nM) = 210±16 for AAR029b in Bal.01 virus
5875
293355222018
None
PAK2NoneN.A.N.A.N.A.N.A.N.A.SyntheticRole in PDAC cancer invasion and metastasisN.A.N.A.4.5Miapaca-2 cell lysate proteaseWestern blottingMiapaca-2 cells lysate after PKM2 depletion (treated with 20 μg/ml cycloheximide (CHX)) In VitroNoneNoneN.A.
5876
293355222018
None
PAK2NoneN.A.N.A.N.A.N.A.N.A.SyntheticRole in PDAC cancer invasion and metastasisN.A.N.A.>24Miapaca-2 cell lysate proteaseWestern blottingMiapaca-2 cells lysate with PKM2 expression (treated with 20 μg/ml cycloheximide (CHX)) In VitroNoneNoneN.A.
5916
296336132018
None
ThXylCNoneFreeFreeLinearLNoneObtained from the soluble fractions of the recombinant E. coli BL21(DE3) cellsβ-xylosidase65 °CN.A.8.9 (Activity Half Life)N.A.N.A.ThXylCIn VitroNoneNoneN.A.
5917
296336132018
None
ThXylC-ELKNoneFreeELK16 short peptide was introduced to the C-terminus of ThXylCLinearLNoneObtained from the soluble fractions of the recombinant E. coli BL21(DE3) cellsβ-xylosidase65 °CN.A.54.8 (Activity Half Life)N.A.N.A.ThXylC-ELKIn VitroNoneNoneN.A.
5922
293738182018
None
fibrinolytic enzymeNoneN.A.N.A.N.A.N.A.N.A.From the marine Serratia marcescens subsp sakuensisClot lysis37 °CN.A.19 (Activity Half Life)N.A.N.A.N.A.In VitroNoneNoneN.A.
5923
293738182018
None
fibrinolytic enzymeNoneN.A.N.A.N.A.N.A.N.A.From the marine Serratia marcescens subsp sakuensisClot lysis50°CN.A.29 (Activity Half Life)N.A.N.A.N.A.In VitroNoneNoneN.A.
5979
287144752017
EYEK(C14)EYE-(PEG24)3-XCFRLPCRQLRC
tag-3xPEG24-FXIIa inhibitorNoneTag-3xPEG24AmidationBi-Cyclic(C2-7, C7-C12 Disulfide Bond In Fxiia Inhibitor)LNoneSyntheticFXIIa InhibitorN.A.5 mg/kg1.0 ± 0.2 (T1/2a)Rabbit plasma proteaseRP-HPLC using fluorescence detectorRabbit plasmaIn VivoNoneNone(EC5x) at 4.2±0.5 mM
5980
287144752017
EYEK(C14)EYE-(PEG24)3-XCFRLPCRQLRC
tag-3xPEG24-FXIIa inhibitorNoneTag-3xPEG24AmidationBi-Cyclic(C2-7, C7-C12 Disulfide Bond In Fxiia Inhibitor)LNoneSyntheticFXIIa InhibitorN.A.5 mg/kg5.2 ± 0.4 (T1/2b)Rabbit plasma proteaseRP-HPLC using fluorescence detectorRabbit plasmaIn VivoNoneNone(EC5x) at 4.2±0.5 mM
6047
280686642017
None
scFv57RNoneFreeFreeLinearLNoneSyntheticAntiviral (against Rabies Virus)37o C for 0-72 hours 0.5 mg/ml14.1N.A.ELISAPBSIn VitroNoneNoneNeutralizing potency (IU/ml) = 83.8 ± 9.4 for monomer
6078
276894062017
None
X1NoneN.A.N.A.N.A.N.A.N.A.N.A.AntiobesityN.A.N.A.3.9Surgical rats plasma protease (Wistar Rat)RIASurgical rats plasma (Wistar rat)In VivoNoneNoneN.A.
6079
276894062017
None
X2NoneN.A.N.A.N.A.N.A.N.A.N.A.AntiobesityN.A.N.A.16.1Surgical rats plasma protease (Wistar Rat)RIASurgical rats plasma (Wistar rat)In VivoNoneNoneN.A.
6080
276894062017
None
X3NoneN.A.N.A.N.A.N.A.N.A.N.A.AntiobesityN.A.N.A.21.3Surgical rats plasma protease (Wistar Rat)RIASurgical rats plasma (Wistar rat)In VivoNoneNoneN.A.
6259
076-262-596-914-4682016
None
GLP-1 ELP1-120NoneHis7 of GLP1FreeLinearLFusion with ELPpreproglucagonN.A.N.A.10mg/kg12.9Tev proteaseBioassayRatin vivohttps://www.lens.org/lens/patent/076-262-596-914-468US 9,458,218 B2N.A.
6260
076-262-596-914-4682016
None
GLP-1 ELP1-120NoneHis7 of GLP1FreeLinearLFusion with ELPpreproglucagonN.A.N.A.1 mg/kg20Tev proteaseBioassayRabbitin vivohttps://www.lens.org/lens/patent/076-262-596-914-468US 9,458,218 B2N.A.
6267
059-320-765-410-1022016
GS(n-octanoyl-S)FLSPEHQKAQQRKESKKPPAKLQPRC
rGhrelin-carrier conjugateNoneFreecysteineLinearLVitamin D3-PEG-maleimideE. coliTherapeuticNA0.1 mg/kg8NAELISARatsin vivohttps://www.lens.org/lens/patent/059-320-765-410-102US 9,289,507 B2N.A.
6280
179-033-965-606-5982017
None
20K-PEG-insulinNone20K-PEGFreeLinearLNoneHumanNA15 minNAimprovedNAenzyme immunoassayRat Bloodin vivohttps://lens.org/179-033-965-606-599US 9616109 B2EC50 =26.3ng/ml
6281
179-033-965-606-5982017
None
VitD-(25)-PEG2K-insulinNoneVitD-(25)-PEG2KFreeLinearLNoneHumanNA2-16 hoursNAimprovedNAenzyme immunoassayRat Bloodin vivohttps://lens.org/179-033-965-606-600US 9616109 B2EC50 =15.8ng/ml
6282
179-033-965-606-5982017
None
VitD-(3)-PEG1.2K-insulinNoneVitD-(3)-PEG1.2KFreeLinearLNoneHumanNA20 minNADrastically ImprovedNAenzyme immunoassayRat Bloodin vivohttps://lens.org/179-033-965-606-601US 9616109 B2EC50= 282.2ng/ml
6295
034-343-155-162-3022017
None
singly stapled SAH-Ex(A)NoneSAHFreeLinearLNoneNANANANA94chymotrypsinELISANAin vitrohttps://lens.org/034-343-155-162-302US 9695224 B2NA
6296
034-343-155-162-3022017
None
singly stapled SAH-Ex(B)NoneSAHFreeLinearLNoneNANANANA128chymotrypsinELISANAin vitrohttps://lens.org/034-343-155-162-302US 9695224 B2NA
6297
034-343-155-162-3022017
None
doubly stapled SAH-Ex(A, B)NoneSAHFreeLinearLNoneNANANANA295chymotrypsinELISANAin vitrohttps://lens.org/034-343-155-162-302US 9695224 B2NA
6299
034-343-155-162-3022017
None
singly stapled SAH-Ex(A)NoneFreeSAHLinearLNoneNANANANA81pepsinELISANAin vitrohttps://lens.org/034-343-155-162-302US 9695224 B2NA
6300
034-343-155-162-3022017
None
SAH-Ex(A, B)NoneFreeSAHLinearLNoneNANANANA172pepsinELISANAin vitrohttps://lens.org/034-343-155-162-302US 9695224 B2NA