Analytical Data
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Gene name
Heparinase
- Application
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Alternative Names
heparin-sulfate lyase HepC
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Species
Others
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Source
E. coli
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
WP_041517255.1
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Expression Region
A22-L658
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Protein Length
Partial
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Heparinase is an important glycosidase enzyme that specifically degrades heparin and heparan sulfate, which are sulfated glycosaminoglycans involved in various biological processes, including cell signaling, coagulation, and inflammation. The study of Heparinase, particularly recombinant forms of the enzyme, has gained considerable attention in biomedical research due to its potential therapeutic applications. By producing Heparinase as a recombinant protein, researchers can obtain a more stable, efficient, and pure source of the enzyme for various studies. This is particularly relevant in the context of developing novel anticoagulant therapies or understanding the roles of heparan sulfate in various diseases, such as cancer and cardiovascular disorders. The ability to generate high quantities of recombinant Heparinase opens new avenues for both fundamental research into the mechanisms of glycosaminoglycan interactions and for the practical application of Heparinase in enzyme-based therapies. Furthermore, understanding the structure-function relationships of this enzyme can lead to enhancements in its activity and specificity, paving the way for innovative drug design strategies targeting heparin-related pathways. This research not only aims to elucidate the biochemical properties of Heparinase but also explores its clinical implications, thereby contributing to the broader field of glycobiology and therapeutics.
