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233526 Coagulation Factor Xa, Human Plasma

Coagulation Factor Xa, Human Plasma, CAS 9002-05-5, is a native coagulation factor Xa prepared from Factor X by activation with Russel's viper venom. The venom is removed after activation.

Coagulation Factor Xa, Human Plasma: のSDS（安全データシート）、CoA（試験成績書）およびCoQ（品質証明書）、カタログなど製品関連の技術資料を入手いただけます。
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233526
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概要

Replacement Information

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233526-10UCN
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      Description
      OverviewNative coagulation factor Xa from human plasma prepared from homogeneous Factor X by activation with Russel’s viper venom. The venom is removed after activation. During coagulation, in the presence of Ca2+ and membrane phospholipids, a complex of Factor Xa and Factor Va (the prothrombinase complex) activates prothrombin to thrombin. Inhibitors include AEBSF (Cat. No. 101500), DFP (Cat. No. 30967), PMSF (Cat. No. 52332), and Soybean Trypsin Inhibitor (Cat. No. 650357). Sold on the basis of plasma equivalent units of Factor X. 100 plasma equivalent units are equal to 800 µg of Factor X.
      Catalogue Number233526
      Brand Family Calbiochem®
      References
      ReferencesHeeb, M.J., et al. 1994. Proc. Natl. Acad. Sci. USA 91, 2728.
      Lindhout, T., et al. 1994. Biochem. J. 297, 131.
      Morishita, H., et al. 1994. Thrombosis Res. 73, 193.
      Lupu, C., et al. 1993. Thrombosis Haemostasis 70, 579.
      Jordan, S.P., et al. 1992. Biochemistry 31, 5374.
      Schoen, P., et al. 1992. Br. J. Haemotol. 81, 255.
      Tracy, P.B., et al. 1992. Methods Enzymol. 215, 329.
      Lawson, J.H., and Mann, K.G. 1991. J. Biol. Chem. 226, 11317.
      Tans, G., et al. 1991. J. Biol. Chem. 266, 21864.
      Owen, W.G., et al. 1974. J. Biol. Chem. 249, 594.
      Product Information
      CAS number9002-05-5
      Unit of DefinitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol CHROMOZYM<sup>®</sup> X substrate per min at 25°C.
      EC number3.4.21.6
      FormLyophilized
      FormulationLyophilized from 700 mM NaCl, 20 mM Tris-HCl, pH 7.4.
      Quality LevelMQ100
      Applications
      Biological Information
      Purityhomogeneous by SDS-PAGE
      SourcePrepared from plasma that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
      Specific Activity≥170 units/mg protein
      Physicochemical Information
      Dimensions
      Materials Information
      Toxicological Information
      Safety Information according to GHS
      Safety Information
      Product Usage Statements
      Storage and Shipping Information
      Ship Code Ambient Temperature Only
      Toxicity Standard Handling
      Storage -20°C
      Do not freeze Ok to freeze
      Special InstructionsFollowing reconstitution, refrigerate (4°C). Stock solutions are stable for up to 6 months at 4°C.
      Packaging Information
      Transport Information
      Supplemental Information
      Specifications
      Global Trade Item Number
      カタログ番号 GTIN
      233526-10UCN 04055977217889

      Documentation

      Coagulation Factor Xa, Human Plasma (M)SDS

      タイトル

      英語版製品安全データシート（(M)SDS） 

      Coagulation Factor Xa, Human Plasma 試験成績書（CoA）

      タイトルロット番号
      233526

      参考資料

      参考資料の概要
      Heeb, M.J., et al. 1994. Proc. Natl. Acad. Sci. USA 91, 2728.
      Lindhout, T., et al. 1994. Biochem. J. 297, 131.
      Morishita, H., et al. 1994. Thrombosis Res. 73, 193.
      Lupu, C., et al. 1993. Thrombosis Haemostasis 70, 579.
      Jordan, S.P., et al. 1992. Biochemistry 31, 5374.
      Schoen, P., et al. 1992. Br. J. Haemotol. 81, 255.
      Tracy, P.B., et al. 1992. Methods Enzymol. 215, 329.
      Lawson, J.H., and Mann, K.G. 1991. J. Biol. Chem. 226, 11317.
      Tans, G., et al. 1991. J. Biol. Chem. 266, 21864.
      Owen, W.G., et al. 1974. J. Biol. Chem. 249, 594.
      データシート

      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.

      Revision19-March-2009 JSW
      DescriptionNative coagulation factor Xa from human plasma prepared from homogeneous Factor X by activation with Russel’s viper venom. Hydrolyzes peptide and ester bonds at the carboxyl group of arginine. Specifically catalyzes the activation of prothrombin to thrombin. Prothrombin activation is accelerated by Factor Va, phospholipids, and Ca2+. Factor Xa was prepared from homogeneous Factor X, using Russels' viper venom (RVV), which was removed after activation. Inhibited by AEBSF (Cat. No. 101500), DFP (Cat. No. 30967), PMSF (Cat. No. 52332), and soybean trypsin inhibitor (Cat. No. 650357). Sold on the basis of plasma equivalent units of Factor X. 100 plasma equivalent units are equal to 800 µg of Factor X.
      FormLyophilized
      FormulationLyophilized from 700 mM NaCl, 20 mM Tris-HCl, pH 7.4.
      SourcePrepared from plasma that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
      CAS number9002-05-5
      EC number3.4.21.6
      Purityhomogeneous by SDS-PAGE
      Specific activity≥170 units/mg protein
      Unit definitionOne unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol CHROMOZYM® X substrate per min at 25°C.
      SolubilityH₂O.
      Storage -20°C
      Do Not Freeze Ok to freeze
      Special InstructionsFollowing reconstitution, refrigerate (4°C). Stock solutions are stable for up to 6 months at 4°C.
      Toxicity Standard Handling
      ReferencesHeeb, M.J., et al. 1994. Proc. Natl. Acad. Sci. USA 91, 2728.
      Lindhout, T., et al. 1994. Biochem. J. 297, 131.
      Morishita, H., et al. 1994. Thrombosis Res. 73, 193.
      Lupu, C., et al. 1993. Thrombosis Haemostasis 70, 579.
      Jordan, S.P., et al. 1992. Biochemistry 31, 5374.
      Schoen, P., et al. 1992. Br. J. Haemotol. 81, 255.
      Tracy, P.B., et al. 1992. Methods Enzymol. 215, 329.
      Lawson, J.H., and Mann, K.G. 1991. J. Biol. Chem. 226, 11317.
      Tans, G., et al. 1991. J. Biol. Chem. 266, 21864.
      Owen, W.G., et al. 1974. J. Biol. Chem. 249, 594.