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human α thrombin  (Yeasen Biotechnology)

 
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    Yeasen Biotechnology human α thrombin
    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+%CE%B1+thrombin/human+thrombin+%CE%B1/pm40812128-53-13-20
    Average 86 stars, based on 1 article reviews
    human α thrombin - by Bioz Stars, 2026-10
    86/100 stars

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    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+%CE%B1+thrombin/human+thrombin+%CE%B1/pmc13116384-152-0-6
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    human α thrombin native protein  (Thermo Fisher)
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    Thermo Fisher human α thrombin native protein
    ( 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 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
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    human α thrombin  (Sysmex Corporation)
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    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+%CE%B1+thrombin/human+thrombin+%CE%B1/pmc12859844-92-13-17
    Average 86 stars, based on 1 article reviews
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    human α thrombin  (Yeasen Biotechnology)
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    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+%CE%B1+thrombin/human+thrombin+%CE%B1/pm40812128-53-13-20
    Average 86 stars, based on 1 article reviews
    human α thrombin - by Bioz Stars, 2026-10
    86/100 stars
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    human α-thrombin  (Prolytix)
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    ( 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+%CE%B1+thrombin/human+%CE%B1+thrombin/pmc11909436__BLOODA_ADV___2024___013810___mmc1-1-39-44
    Average 90 stars, based on 1 article reviews
    human α-thrombin - by Bioz Stars, 2026-10
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    enzyme human α-thrombin  (Biopharm GmbH)
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    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+%CE%B1+thrombin/bovine+thrombin/us12351648-2087-12-15
    Average 90 stars, based on 1 article reviews
    enzyme human α-thrombin - by Bioz Stars, 2026-10
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    human α thrombin  (Thermo Fisher)
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    Thermo Fisher 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 Thermo Fisher, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/human+%CE%B1+thrombin/Thrombin+Human/pmc11607481-327-10-12
    Average 94 stars, based on 1 article reviews
    human α thrombin - by Bioz Stars, 2026-10
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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+%CE%B1+thrombin/human+%CE%B1+thrombin+ht+1002a/pm40499720-58-0-6
    Average 90 stars, based on 1 article reviews
    human α-thrombin ht 1002a - by Bioz Stars, 2026-10
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    ( 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