Streptokinase

Streptokinase Recombinant
Cat. No.
BT14880
Source
Escherichia Coli.
Synonyms
Streptokinase, SK.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

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.

Product Specs

Introduction
Streptokinase is a medication used to dissolve blood clots. It is produced by the bacteria Streptococcus and works by activating plasminogen, which is a protein involved in the breakdown of clots.
Description
This is a recombinant Streptokinase protein produced in E. coli. It is a non-glycosylated polypeptide chain with a molecular weight of 47.3 kDa, purified using chromatographic techniques.
Physical Appearance
Sterile, white, lyophilized powder.
Formulation
Lyophilized from a 0.2 µm filtered solution at a concentration of 1 mg/ml in phosphate-buffered saline (PBS) at pH 7.4.
Solubility
Reconstitute the lyophilized Streptokinase in sterile 18 M-cm H₂O to a concentration of at least 100 µg/ml. This solution can be further diluted in other aqueous solutions.
Stability
Lyophilized Streptokinase is stable at room temperature for 3 weeks but should be stored desiccated below -18°C. After reconstitution, store at 4°C for 2-7 days. For long-term storage, freeze below -18°C. Avoid repeated freeze-thaw cycles.
Purity
Purity greater than 97.0% as determined by: (a) Reverse-phase high-performance liquid chromatography (RP-HPLC) and (b) Sodium dodecyl-sulfate polyacrylamide gel electrophoresis (SDS-PAGE).
Biological Activity
The specific biological activity, measured by the ability to lyse fibrin in an agarose plate assay, was found to be 80000 IU/mg.
Synonyms
Streptokinase, SK.
Source
Escherichia Coli.
Amino Acid Sequence
IAGPEWLLDR PSVNNSQLVV SVAGTVEGTN QDISLKFFEI DLTSRPAHGG KTEQGLSPKS KLFATDSGAM PHKLEKADLL KAIQEQLIAN VHSNDDYFEV IDFASDATIT DRNGKVYFAD KDGSVTLPIQ PVQEFLLKGH VRVRPYKEKP VQNQAKSVDV EYTVQFTPLN PDDDFRPALK DTKLLKTLAI GDTITSQELL AQAQSILNKN HPGYTIYERD SSIVTHDNDI FRTILPMDQE FTYHVKNREQ AYRINKKSGL NEEINNTDLI SEKYYVLKKG EKPYDPFDRS HLKLFTIKYV DVNTNELLKS EQLLTASERN LDFRDLYDPR DKAKLLYNNL DAFGIMDYTL TGKVEDNHDD TNRIITVYMG KRPEGENASY HLAYDKDRYT EEEREVYSYL RYTGTPIPDN PNDK.

Product Science Overview

Introduction

Streptokinase is a potent plasminogen activator widely used as a thrombolytic agent in clinical settings. It is naturally secreted by several strains of beta-hemolytic streptococci, particularly Streptococcus equisimilis . Streptokinase works by converting plasminogen to plasmin, which then breaks down fibrin clots, making it an essential treatment for conditions such as myocardial infarction, pulmonary embolism, and deep vein thrombosis .

Recombinant Production

The natural production of streptokinase has several limitations, including low yields and the pathogenic nature of its native host. To overcome these challenges, recombinant DNA technology has been employed to produce streptokinase in various host organisms. One notable example is the expression of streptokinase in the Gram-positive bacterium Streptomyces lividans .

In this process, the structural gene encoding streptokinase is fused to signal sequences that facilitate its secretion. For instance, the Streptomyces venezuelae CBS762.70 subtilisin inhibitor (vsi) signal sequence or the Streptomyces lividans xylanase C (xlnC) signal sequence can be used . The recombinant production in Streptomyces lividans has shown higher yields when the Sec-dependent signal peptide mediates the translocation of streptokinase .

Advantages of Recombinant Streptokinase

Recombinant streptokinase offers several advantages over its naturally produced counterpart:

  1. Higher Yields: Recombinant production methods can significantly increase the yield of streptokinase, making it more cost-effective .
  2. Reduced Pathogenicity: By using non-pathogenic host organisms, the risks associated with the pathogenic nature of the native host are eliminated .
  3. Enhanced Specificity: Recombinant techniques allow for the modification of streptokinase to enhance its specificity and reduce potential side effects .
Applications

Streptokinase is primarily used as a thrombolytic agent to dissolve blood clots in patients suffering from acute myocardial infarction, pulmonary embolism, and other thrombotic conditions . Its ability to activate plasminogen and subsequently degrade fibrin clots makes it a critical component in emergency medicine.

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