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human α thrombin native protein  (Thermo Fisher)
96
Thermo Fisher human α thrombin native protein
Human α Thrombin Native Protein, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+alpha+thrombin/bio_rxiv__64898__2026__03__30__714774-149-14-28?v=Thermo+Fisher
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human α thrombin native protein - by Bioz Stars, 2026-06
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human alpha thrombin  (Enzyme Research Laboratories)
86
Enzyme Research Laboratories human alpha thrombin
( a ) Kinetic profiles of the cold-induced reversible gelation of 0.25% agar at 25 °C (absorbance changes at 350 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters of agar are A = 0.132, B = 12.087, C = 1.731, m = 0.00044, and q = −0.009. Derived kinetical parameters for agar gelation are Abs Max = 0.132, V Max = 0.007 Abs/min, t VMax = 5.9 min, and t AbsMax/2 = 11.9 min. Considering the crucial timings t 0 , t lag , t VMax , t AbsMax/2 and t AbsMax , five phases can be identified: I (lag phase), IIa (increase up to maximum rate), IIb (approximately constant-rate increase), IIIa (decelerating increase), and IIIb (plateau with a slight asymptotic drift); see main text for further details; ( b ) Kinetic profiles of the enzymatic assay of 8 μM S–2238 catalyzed by 0.15 nM human <t>alpha</t> <t>thrombin</t> at 25 °C (absorbance changes at 405 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters for S–2238 are A = 0.139, B = 15.048, C = 1.742, m = −0.000027, and q = 0.005. Derived kinetical parameters for S–2238 enzymatic assay are Abs Max = 0.136, V Max = 0.006 Abs/min, t VMax = 7.2 min, and t AbsMax/2 = 14.9 min. Contrariwise, for the enzymatic reaction only IIa, IIb, IIIa and IIIb phases can be distinguished.
Human Alpha Thrombin, supplied by Enzyme Research Laboratories, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+alpha+thrombin/pmc13116384-152-0-6?v=Enzyme+Research+Laboratories
Average 86 stars, based on 1 article reviews
human alpha thrombin - by Bioz Stars, 2026-06
86/100 stars
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human α thrombin  (Sysmex Corporation)
86
Sysmex Corporation human α thrombin
( a ) Kinetic profiles of the cold-induced reversible gelation of 0.25% agar at 25 °C (absorbance changes at 350 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters of agar are A = 0.132, B = 12.087, C = 1.731, m = 0.00044, and q = −0.009. Derived kinetical parameters for agar gelation are Abs Max = 0.132, V Max = 0.007 Abs/min, t VMax = 5.9 min, and t AbsMax/2 = 11.9 min. Considering the crucial timings t 0 , t lag , t VMax , t AbsMax/2 and t AbsMax , five phases can be identified: I (lag phase), IIa (increase up to maximum rate), IIb (approximately constant-rate increase), IIIa (decelerating increase), and IIIb (plateau with a slight asymptotic drift); see main text for further details; ( b ) Kinetic profiles of the enzymatic assay of 8 μM S–2238 catalyzed by 0.15 nM human <t>alpha</t> <t>thrombin</t> at 25 °C (absorbance changes at 405 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters for S–2238 are A = 0.139, B = 15.048, C = 1.742, m = −0.000027, and q = 0.005. Derived kinetical parameters for S–2238 enzymatic assay are Abs Max = 0.136, V Max = 0.006 Abs/min, t VMax = 7.2 min, and t AbsMax/2 = 14.9 min. Contrariwise, for the enzymatic reaction only IIa, IIb, IIIa and IIIb phases can be distinguished.
Human α Thrombin, supplied by Sysmex Corporation, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+alpha+thrombin/pmc12859844-92-13-17?v=Sysmex+Corporation
Average 86 stars, based on 1 article reviews
human α thrombin - by Bioz Stars, 2026-06
86/100 stars
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human α thrombin  (Yeasen Biotechnology)
86
Yeasen Biotechnology human α thrombin
( a ) Kinetic profiles of the cold-induced reversible gelation of 0.25% agar at 25 °C (absorbance changes at 350 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters of agar are A = 0.132, B = 12.087, C = 1.731, m = 0.00044, and q = −0.009. Derived kinetical parameters for agar gelation are Abs Max = 0.132, V Max = 0.007 Abs/min, t VMax = 5.9 min, and t AbsMax/2 = 11.9 min. Considering the crucial timings t 0 , t lag , t VMax , t AbsMax/2 and t AbsMax , five phases can be identified: I (lag phase), IIa (increase up to maximum rate), IIb (approximately constant-rate increase), IIIa (decelerating increase), and IIIb (plateau with a slight asymptotic drift); see main text for further details; ( b ) Kinetic profiles of the enzymatic assay of 8 μM S–2238 catalyzed by 0.15 nM human <t>alpha</t> <t>thrombin</t> at 25 °C (absorbance changes at 405 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters for S–2238 are A = 0.139, B = 15.048, C = 1.742, m = −0.000027, and q = 0.005. Derived kinetical parameters for S–2238 enzymatic assay are Abs Max = 0.136, V Max = 0.006 Abs/min, t VMax = 7.2 min, and t AbsMax/2 = 14.9 min. Contrariwise, for the enzymatic reaction only IIa, IIb, IIIa and IIIb phases can be distinguished.
Human α Thrombin, supplied by Yeasen Biotechnology, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+alpha+thrombin/pm40812128-53-13-20?v=Yeasen+Biotechnology
Average 86 stars, based on 1 article reviews
human α thrombin - by Bioz Stars, 2026-06
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human α-thrombin  (Prolytix)
90
Prolytix human α-thrombin
( a ) Kinetic profiles of the cold-induced reversible gelation of 0.25% agar at 25 °C (absorbance changes at 350 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters of agar are A = 0.132, B = 12.087, C = 1.731, m = 0.00044, and q = −0.009. Derived kinetical parameters for agar gelation are Abs Max = 0.132, V Max = 0.007 Abs/min, t VMax = 5.9 min, and t AbsMax/2 = 11.9 min. Considering the crucial timings t 0 , t lag , t VMax , t AbsMax/2 and t AbsMax , five phases can be identified: I (lag phase), IIa (increase up to maximum rate), IIb (approximately constant-rate increase), IIIa (decelerating increase), and IIIb (plateau with a slight asymptotic drift); see main text for further details; ( b ) Kinetic profiles of the enzymatic assay of 8 μM S–2238 catalyzed by 0.15 nM human <t>alpha</t> <t>thrombin</t> at 25 °C (absorbance changes at 405 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters for S–2238 are A = 0.139, B = 15.048, C = 1.742, m = −0.000027, and q = 0.005. Derived kinetical parameters for S–2238 enzymatic assay are Abs Max = 0.136, V Max = 0.006 Abs/min, t VMax = 7.2 min, and t AbsMax/2 = 14.9 min. Contrariwise, for the enzymatic reaction only IIa, IIb, IIIa and IIIb phases can be distinguished.
Human α Thrombin, supplied by Prolytix, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+alpha+thrombin/pmc11909436__BLOODA_ADV___2024___013810___mmc1-1-39-44?v=Prolytix
Average 90 stars, based on 1 article reviews
human α-thrombin - by Bioz Stars, 2026-06
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enzyme human α-thrombin  (Biopharm GmbH)
90
Biopharm GmbH enzyme human α-thrombin
( a ) Kinetic profiles of the cold-induced reversible gelation of 0.25% agar at 25 °C (absorbance changes at 350 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters of agar are A = 0.132, B = 12.087, C = 1.731, m = 0.00044, and q = −0.009. Derived kinetical parameters for agar gelation are Abs Max = 0.132, V Max = 0.007 Abs/min, t VMax = 5.9 min, and t AbsMax/2 = 11.9 min. Considering the crucial timings t 0 , t lag , t VMax , t AbsMax/2 and t AbsMax , five phases can be identified: I (lag phase), IIa (increase up to maximum rate), IIb (approximately constant-rate increase), IIIa (decelerating increase), and IIIb (plateau with a slight asymptotic drift); see main text for further details; ( b ) Kinetic profiles of the enzymatic assay of 8 μM S–2238 catalyzed by 0.15 nM human <t>alpha</t> <t>thrombin</t> at 25 °C (absorbance changes at 405 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters for S–2238 are A = 0.139, B = 15.048, C = 1.742, m = −0.000027, and q = 0.005. Derived kinetical parameters for S–2238 enzymatic assay are Abs Max = 0.136, V Max = 0.006 Abs/min, t VMax = 7.2 min, and t AbsMax/2 = 14.9 min. Contrariwise, for the enzymatic reaction only IIa, IIb, IIIa and IIIb phases can be distinguished.
Enzyme Human α Thrombin, supplied by Biopharm GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+alpha+thrombin/us12351648-2087-12-15?v=Biopharm+GmbH
Average 90 stars, based on 1 article reviews
enzyme human α-thrombin - by Bioz Stars, 2026-06
90/100 stars
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human α-thrombin ht 1002a  (Enzyme Research Laboratories)
90
Enzyme Research Laboratories human α-thrombin ht 1002a
( a ) Kinetic profiles of the cold-induced reversible gelation of 0.25% agar at 25 °C (absorbance changes at 350 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters of agar are A = 0.132, B = 12.087, C = 1.731, m = 0.00044, and q = −0.009. Derived kinetical parameters for agar gelation are Abs Max = 0.132, V Max = 0.007 Abs/min, t VMax = 5.9 min, and t AbsMax/2 = 11.9 min. Considering the crucial timings t 0 , t lag , t VMax , t AbsMax/2 and t AbsMax , five phases can be identified: I (lag phase), IIa (increase up to maximum rate), IIb (approximately constant-rate increase), IIIa (decelerating increase), and IIIb (plateau with a slight asymptotic drift); see main text for further details; ( b ) Kinetic profiles of the enzymatic assay of 8 μM S–2238 catalyzed by 0.15 nM human <t>alpha</t> <t>thrombin</t> at 25 °C (absorbance changes at 405 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters for S–2238 are A = 0.139, B = 15.048, C = 1.742, m = −0.000027, and q = 0.005. Derived kinetical parameters for S–2238 enzymatic assay are Abs Max = 0.136, V Max = 0.006 Abs/min, t VMax = 7.2 min, and t AbsMax/2 = 14.9 min. Contrariwise, for the enzymatic reaction only IIa, IIb, IIIa and IIIb phases can be distinguished.
Human α Thrombin Ht 1002a, supplied by Enzyme Research Laboratories, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/human+alpha+thrombin/pm40499720-58-0-6?v=Enzyme+Research+Laboratories
Average 90 stars, based on 1 article reviews
human α-thrombin ht 1002a - by Bioz Stars, 2026-06
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Image Search Results


( a ) Kinetic profiles of the cold-induced reversible gelation of 0.25% agar at 25 °C (absorbance changes at 350 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters of agar are A = 0.132, B = 12.087, C = 1.731, m = 0.00044, and q = −0.009. Derived kinetical parameters for agar gelation are Abs Max = 0.132, V Max = 0.007 Abs/min, t VMax = 5.9 min, and t AbsMax/2 = 11.9 min. Considering the crucial timings t 0 , t lag , t VMax , t AbsMax/2 and t AbsMax , five phases can be identified: I (lag phase), IIa (increase up to maximum rate), IIb (approximately constant-rate increase), IIIa (decelerating increase), and IIIb (plateau with a slight asymptotic drift); see main text for further details; ( b ) Kinetic profiles of the enzymatic assay of 8 μM S–2238 catalyzed by 0.15 nM human alpha thrombin at 25 °C (absorbance changes at 405 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters for S–2238 are A = 0.139, B = 15.048, C = 1.742, m = −0.000027, and q = 0.005. Derived kinetical parameters for S–2238 enzymatic assay are Abs Max = 0.136, V Max = 0.006 Abs/min, t VMax = 7.2 min, and t AbsMax/2 = 14.9 min. Contrariwise, for the enzymatic reaction only IIa, IIb, IIIa and IIIb phases can be distinguished.

Journal: Gels

Article Title: Origin of the High Variability in Sol–Gel Phase Transitions: The Agar Gelation Model

doi: 10.3390/gels12040304

Figure Lengend Snippet: ( a ) Kinetic profiles of the cold-induced reversible gelation of 0.25% agar at 25 °C (absorbance changes at 350 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters of agar are A = 0.132, B = 12.087, C = 1.731, m = 0.00044, and q = −0.009. Derived kinetical parameters for agar gelation are Abs Max = 0.132, V Max = 0.007 Abs/min, t VMax = 5.9 min, and t AbsMax/2 = 11.9 min. Considering the crucial timings t 0 , t lag , t VMax , t AbsMax/2 and t AbsMax , five phases can be identified: I (lag phase), IIa (increase up to maximum rate), IIb (approximately constant-rate increase), IIIa (decelerating increase), and IIIb (plateau with a slight asymptotic drift); see main text for further details; ( b ) Kinetic profiles of the enzymatic assay of 8 μM S–2238 catalyzed by 0.15 nM human alpha thrombin at 25 °C (absorbance changes at 405 nm plotted vs. time) and their corresponding fitted curves (continuous line, ―). According to Equation (3), the fitting parameters for S–2238 are A = 0.139, B = 15.048, C = 1.742, m = −0.000027, and q = 0.005. Derived kinetical parameters for S–2238 enzymatic assay are Abs Max = 0.136, V Max = 0.006 Abs/min, t VMax = 7.2 min, and t AbsMax/2 = 14.9 min. Contrariwise, for the enzymatic reaction only IIa, IIb, IIIa and IIIb phases can be distinguished.

Article Snippet: Human alpha thrombin was purchased by Enzyme Research Laboratories (South Bend, IN, USA).

Techniques: Derivative Assay, Enzymatic Assay