Streptokinase Recombinant Protein

Streptokinase Recombinant Protein

Catalog Number:
P001416278ABE
Mfr. No.:
Abe32-2822
Price:
  • Size:
    750000, IU
    Quantity:
    Add to Cart:
      • Overview
        • Streptokinase Recombinant produced in E. Coli is a non-glycosylated polypeptide chain containing 414 amino acids and having a molecular weight of 47.3kDa. The Streptokinase is purified by proprietary chromatographic techniques. Streptokinase is an extracellular metallo-enzymeproduced by beta-haemolytic streptococcusand is used as an effective and cheap clot-dissolving medicationin some cases of myocardial infarction(heart attack) and pulmonary embolism. It belongs to a group of medications known as fibrinolytics, and works by activating plasminogenthrough cleavage to produce plasmin.

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      • Properties
        • Protein Name
          Streptokinase, SK.
          Source
          E. coli
          Type
          Recombinant Proteins
          Purification
          Greater than 97.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
          Formulation
          Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4.
          Storage
          Lyophilized Streptokinase although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Streptokinase should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
          Activity
          Biological Activity measured by the ability of fibrin lysis in agarose plate was found to be 80000U/mg.

          * For Research Use Only. Not for use in diagnostic/therapeutics procedures.

      • Applications
        • Application Description
          It is recommended to reconstitute the lyophilized Streptokinase in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. The specific biological activity measured by the ability of fibrin lysis in agarose plate was found to be 80000U/mg.

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