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IDPMIDYEARSequenceNameLengthN-ter MODC-ter MODLinear/CyclicChiralityChem-MODOriginNatureIncubation TimeConcentrationHalf LifeUnits Half LifeProteaseAssayTest SampleVivo/VitroReferencePatent No.Activity
2080
90672971996
YGGFLRRl
E-2078 [N-methyl-Tyr1, N-methyl-Arg7-D-Leu8] Dyn A (1 €“8) ethylamide]N.A.MethylationEthylamideLinearMixMethylation on Arg7 and Tyr1Dynorphin A (1 €“ 8) analogAnalgesicNot reported10 mg/kg44Monkey blood proteasesMALDI-MSRhesus monkey blood plasma (Intravenous)in vivo7479294NoneNot available
4019
387372832024
LAEAKVLANRELDKYGVSDFYKRLINKAKTVEGVEALKLHILAALP-FRRG-(E5C3)-(GN)
ABD035-immunoGNN.A.P1h3His-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)
immunoGNN.A.P1h3His-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-immunoGNN.A.P1h3His-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
N.A.
BI-XN.A.N.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
N.A.
BI-XN.A.N.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
N.A.
BI-XN.A.N.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
N.A.
(89Zr, Mn)-WPMNsN.A.FreeFreeLinearLMn 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
N.A.
(89Zr, Mn)-WPMNsN.A.FreeFreeLinearLMn 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
N.A.
DAE Rum55N.A.N.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
N.A.
E268R-EKL16N.A.N.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
N.A.
Xyn10-HBN.A.N.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
N.A.
Trx1PN.A.N.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
N.A.
Trx1ThpN.A.N.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
N.A.
IL-15-Cy7N.A.FreeFreeLinearLCy7Derived 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
N.A.
biNV-IL-15-Cy7N.A.FreeFreeLinearLCy7Derived 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
N.A.
KAN-101N.A.N.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
N.A.
S-20-1N.A.N.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
N.A.
S-20-1N.A.N.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
4719
N.A.2022
N.A.
Test 1N.A.N.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
N.A.2022
N.A.
Test 2N.A.N.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
N.A.2022
N.A.
Test 3N.A.N.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
N.A.2022
N.A.
Test 4N.A.N.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
N.A.
BA17N.A.FreeFreeLinearLNoneIsolated from B. licheniformisSerine protease50°CN.A.90 (Enzyme Activity)N.A.ZymographyN.A.In VitroNoneNoneN.A.
4756
359102762022
N.A.
BA17N.A.FreeFreeLinearLNoneIsolated from B. licheniformisSerine protease60 °CN.A.12 (Enzyme Activity)N.A.ZymographyN.A.In VitroNoneNoneN.A.
4763
354883382022
N.A.
FRAP-smTGN.A.Frap (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
N.A.
FRAP-TGm1N.A.Frap (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
N.A.
FRAPD-TGm1N.A.Frap (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
N.A.
E187A N.A.FreeFreeLinearLResidue 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
5229
320342892020
VL-GGGGSGGGGSGGGGS-VH-GGGGS-KPLPEVTDEY
α-GD2 scFv TMN.A.Radiolabelled 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
N.A.
Uox-WTN.A.N.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
N.A.
Uox-HSAN.A.N.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
N.A.
PEG-PAEU + Uox-HSAN.A.N.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
N.A.
PEG-PAEU-ABP + Uox-HSAN.A.N.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
N.A.
Pept. AN.A.FreeFreeCyclicLN.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
N.A.
Pept. AN.A.FreeFreeCyclicLN.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
N.A.
ASNN.A.N.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
N.A.
ASNN.A.N.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
N.A.
ASNN.A.N.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
N.A.
ASNN.A.N.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
N.A.
FITC-AAR029bN.A.Fluorescein 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
N.A.
FITC-AAR029b in LiposomeN.A.Fluorescein 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
N.A.
PAK2N.A.N.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
N.A.
PAK2N.A.N.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.
5885
292823032018
SIINFEKL
SCRAP-mCherryN.A.DDmCherryN.A.LNoneSyntheticAffects Antigen PresentationN.A.N.A.41 ± 5 El4 cells proteaseBD cytoflex flow cytometryEL4 cells after Shield-1 removalN.A.NoneNoneN.A.
5916
296336132018
N.A.
ThXylCN.A.FreeFreeLinearLNoneObtained 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
N.A.
ThXylC-ELKN.A.FreeELK16 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
N.A.
fibrinolytic enzymeN.A.N.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
N.A.
fibrinolytic enzymeN.A.N.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 inhibitorN.A.Tag-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 inhibitorN.A.Tag-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
5981
287144752017
XCFRLPCRQLRC
FXIIa inhibitorN.A.Fluorescein (F) AmidationBi-Cyclic(C2-7, C7-C12 Disulfide Bond In Fxiia Inhibitor)LNoneSyntheticFXIIa InhibitorN.A.3.7 mg/kg0.21 ± 0.04 (T1/2b)Rabbit plasma proteaseA single quadrupole liquid chromatography mass spectrometer Rabbit plasmaIn VivoNoneNoneKi FXIIa = 4±0.9 nM in presence of albumin
6047
280686642017
N.A.
scFv57RN.A.FreeFreeLinearLNoneSyntheticAntiviral (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
6048
280686642017
DPDNEAYEMPSEEGYQDYEPEA
scFv57R-ATSN.A.Free(ATS) was fused to the C-terminus of the anti-RV scFv57RLinearLNonescFv57R-ATS fusion proteinAntiviral (against Rabies Virus)37o C for 0-72 hours 0.5 mg/ml33.9N.A.ELISAPBSIn VitroNoneNoneNeutralizing potency (IU/ml) = 2.9 ± 0.5 for polymer
6049
280686642017
DPDNEAYEMPSEEGYQDYEPEA
scFv57R-ATSN.A.Free(ATS) was fused to the C-terminus of the anti-RV scFv57RLinearLNonescFv57R-ATS fusion proteinAntiviral (against Rabies Virus)37o C 0.5 mg/ml15.6Mouse serum proteaseELISAMouse serumIn VitroNoneNoneNeutralizing potency (IU/ml) = 2.9 ± 0.5 for polymer
6078
276894062017
N.A.
X1N.A.N.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
N.A.
X2N.A.N.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
N.A.
X3N.A.N.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.