Analytical Data
-
Gene name
Heparinase III
-
简介
Heparinase III Protein is the unique member of the heparinase family of heparin-degrading lyases that recognizes the ubiquitous cell-surface heparan sulfate proteoglycans as its primary substrate. Heparinase III functions in cleaving metazoan heparan sulfate and providing carbon, nitrogen and sulfate sources for microorganisms. Furthermore, Heparinase III is cardioprotective in a dose-dependent manner, preserves endothelial function and attenuates PMN adherence to the coronary vascular endothelium. Heparinase III Protein, P. heparinus (His) is the recombinant Heparinase III protein, expressed by E. coli , with N-6*His labeled tag.
- Application
-
Alternative Names
Heparin-sulfate lyase; hepC; Heparin-sulfate eliminase; Heparinase III; HepIII; Heparitin-sulfate lyase
-
Species
Others
-
Source
E. coli
-
Tag
N-6*His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
AAB18278
-
Expression Region
Q25-P659
-
AA Sequence
QSSSITRKDFDHINLEYSGLEKVNKAVAAGNYDDAAKALLAYYREKSKAREPDFSNAEKPADIRQPIDKVTREMADKALVHQFQPHKGYGYFDYGKDINWQMWPVKDNEVRWQLHRVKWWQAMALVYHATGDEKYAREWVYQYSDWARKNPLGLSQDNDKFVWRPLEVSDRVQSLPPTFSLFVNSPAFTPAFLMEFLNSYHQQADYLSTHYAEQGNHRLFEAQRNLFAGVSFPEFKDSPRWRQTGISVLNTEIKKQVYADGMQFELSPIYHVAAIDIFLKAYGSAKRVNLEKEFPQSYVQTVENMIMALISISLPDYNTPMFGDSWITDKNFRMAQFASWARVFPANQAIKYFATDGKQGKAPNFLSKALSNAGFYTFRSGWDKNATVMVLKASPPGEFHAQPDNGTFELFIKGRNFTPDAGVFVYSGDEAIMKLRNWYRQTRIHSTLTLDNQNMVITKARQNKWETGNNLDVLTYTNPSYPNLDHQRSVLFINKKYFLVIDRAIGEATGNLGVHWQLKEDSNPVFDKTKNRVYTTYRDGNNLMIQSLNADRTSLNEEEGKVSYVYNKELKRPAFVFEKPKKNAGTQNFVSIVYPYDGQKAPEISIRENKGNDFEKGKLNLTLTINGKQQLVLVP
-
Protein Length
Full Length of Mature Protein
-
Molecular Weight
74 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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 III is an important enzyme involved in the degradation of heparan sulfate and heparin, two glycosaminoglycans that play significant roles in various biological processes, including cell signaling, coagulation, and inflammation. The enzyme is produced by certain bacteria and has gained attention due to its potential therapeutic applications, particularly in the treatment of anticoagulant conditions and in cancer therapy, where modulation of the tumor microenvironment can enhance drug delivery and effectiveness. Studies have shown that Heparinase III can effectively enhance drug bioavailability by disrupting heparan sulfate-protein interactions, potentially improving the outcomes of existing treatments. Furthermore, its ability to modify extracellular matrix components has implications in tissue engineering and regenerative medicine. The production of recombinant Heparinase III allows for more controlled studies and application in therapeutic contexts, overcoming the limitations of extracting the enzyme from natural sources. As research progresses, understanding the structure-function relationship of this enzyme through recombinant methods can yield insights into its catalytic mechanisms, optimal conditions for activity, and interaction partners, further elucidating its role in physiological and pathological processes. Additionally, advancements in recombinant technology open up avenues for engineering Heparinase III variants with enhanced activity or specificity, paving the way for novel biomedical applications. Overall, the study of recombinant Heparinase III presents significant opportunities for therapeutic innovation and a deeper understanding of glycosaminoglycan biology.
