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616371 Aprotinin, Bovine, Recombinant, Nicotiana sp., Animal-Free - CAS 9087-70-1 - Calbiochem

Descripción

Replacement Information

Tabla espec. clave

CAS #Empirical Formula
9087-70-1C₂₈₄H₄₃₂N₈₄O₇₉S₇

Precios y disponibilidad

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616371-1MG
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      616371-25MG
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          616371-5MG
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              Description
              OverviewRecombinant, bovine aprotinin supplied without animal-derived components. Aprotinin is a competitive, reversible inhibitor of proteolytic and esterolytic activity. A relatively heat- and acid-stable serine protease inhibitor. Forms a tight complex, blocking the active site of the enzyme. Effective at concentrations equimolar with protease. Inhibits several proteases, including coagulation factors in the prephase of blood clotting, tissue and leukocytic proteinases, chymotrypsin, trypsin (Kd = 5 x 10-14 M), plasmin (Kd = 2.3 x 10-10 M), and kallikrein (Kd = 1 x 10-7 M). Proteases not inhibited by aprotinin include Factor Xa, thrombin, pepsin, papain, and carboxypeptidases A and B. Useful for protein purification and for extending the life of cells in culture by preventing proteolytic damage.
              Catalogue Number616371
              Brand Family Calbiochem®
              SynonymsPancreatic Trypsin Inhibitor, Trypsin-Kallikrein Inhibitor, Kallikrein-Trypsin Inactivator, Antikrein, Basic Pancreatic Trypsin Inhibitor
              References
              ReferencesDeutscher, M.P., 1990. Methods Enzymol. 182, 83.
              Product Information
              CAS number9087-70-1
              Unit of DefinitionOne TIU (Trypsin Inhibitory Unit) will decrease the activity of two trypsin units by 50% where one trypsin unit will hydrolyze 1.0 µmole of Nα-benzoyl-L-Arginine-p-Nitroanilide (L-BAPNA) per minute at pH 7.8 at 25°C.
              ATP CompetitiveN
              EC number2329949
              FormWhite to off-white powder
              FormulationContains no animal-derived components.
              Hill FormulaC₂₈₄H₄₃₂N₈₄O₇₉S₇
              Chemical formulaC₂₈₄H₄₃₂N₈₄O₇₉S₇
              ReversibleY
              Quality LevelMQ200
              Applications
              Biological Information
              Primary Targetchymotrypsin
              Primary Target IC<sub>50</sub>Kd = 5 x 10-14 M, 2.3 x 10-10 M, 1 x 10-7 M against trypsin, plasmin, and kallikrein, respectively
              Purity≥98% by SDS-PAGE
              Specific Activity≥5.0 EPU/mg protein
              Concentration Label Please refer to vial label for lot-specific concentration
              Physicochemical Information
              Cell permeableN
              Dimensions
              Materials Information
              Toxicological Information
              Safety Information according to GHS
              RTECSYN5080000
              Safety Information
              Product Usage Statements
              Storage and Shipping Information
              Ship Code Blue Ice Only
              Toxicity Standard Handling
              Storage +2°C to +8°C
              Do not freeze Ok to freeze
              Packaging Information
              Transport Information
              Supplemental Information
              Specifications
              Global Trade Item Number
              Número de referencia GTIN
              616371-1MG 04055977262919
              616371-25MG 04055977262926
              616371-5MG 04055977262933

              Documentation

              Aprotinin, Bovine, Recombinant, Nicotiana sp., Animal-Free - CAS 9087-70-1 - Calbiochem Ficha datos de seguridad (MSDS)

              Título

              Ficha técnica de seguridad del material (MSDS) 

              Aprotinin, Bovine, Recombinant, Nicotiana sp., Animal-Free - CAS 9087-70-1 - Calbiochem Certificados de análisis

              CargoNúmero de lote
              616371

              Referencias bibliográficas

              Visión general referencias
              Deutscher, M.P., 1990. Methods Enzymol. 182, 83.
              Ficha técnica

              Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

              Revision08-August-2024 JSW
              SynonymsPancreatic Trypsin Inhibitor, Trypsin-Kallikrein Inhibitor, Kallikrein-Trypsin Inactivator, Antikrein, Basic Pancreatic Trypsin Inhibitor
              DescriptionRecombinant, bovine aprotinin supplied without animal-derived components. Aprotinin is a competitive, reversible inhibitor of proteolytic and esterolytic activity. A relatively heat- and acid-stable serine protease inhibitor. Forms a tight complex, blocking the active site of the enzyme. Effective at concentrations equimolar with protease. Inhibits several proteases, including coagulation factors in the prephase of blood clotting, tissue and leukocytic proteinases, chymotrypsin, trypsin (Kd = 5 x 10-14 M), plasmin (Kd = 2.3 x 10-10 M), and kallikrein (Kd = 1 x 10-7 M). Proteases not inhibited by aprotinin include Factor Xa, thrombin, pepsin, papain, and carboxypeptidases A and B. Useful for protein purification and for extending the life of cells in culture by preventing proteolytic damage.
              FormWhite to off-white powder
              FormulationContains no animal-derived components.
              Concentration Label Please refer to vial label for lot-specific concentration
              CAS number9087-70-1
              RTECSYN5080000
              EC number2329949
              Chemical formulaC₂₈₄H₄₃₂N₈₄O₇₉S₇
              Purity≥98% by SDS-PAGE
              Specific activity≥5.0 EPU/mg protein
              Unit definitionOne TIU (Trypsin Inhibitory Unit) will decrease the activity of two trypsin units by 50% where one trypsin unit will hydrolyze 1.0 µmole of Nα-benzoyl-L-Arginine-p-Nitroanilide (L-BAPNA) per minute at pH 7.8 at 25°C.
              Storage +2°C to +8°C
              Do Not Freeze Ok to freeze
              Toxicity Standard Handling
              Merck USA index14, 757
              ReferencesDeutscher, M.P., 1990. Methods Enzymol. 182, 83.