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  • 产品名称：serpinPeptidaseInhibitor,CladeD(HeparinCofactor),Member1(SERPIND1)(AA20-499)(Ac

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  • 产品厂商：ACROBiosystems
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简单介绍：
serpinPeptidaseInhibitor,CladeD(HeparinCofactor),Member1(SERPIND1)(AA20-499)(Active)protein(Histag)
详情介绍：
Characteristics This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 55.7 kDa. The protein migrates as 65-70 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Purity >95 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
ProductDetails: Biological Activity Comment Biological Activity: Measured by its ability to inhibit Recombinant Human Coagulation Factor II/Thrombin cleavage of a fluorogenic peptide substrate Boc-VPR-AMC. The IC50 value is <1.8 nm.="" <="" td="">
Background Serpin D1 is also known as Heparin cofactor 2 (HCF2), Protease inhibitor leuserpin-2 (HLS2), Heparin cofactor II (HC-II), which belongs to the serpin family. HCF2 is expressed predominantly in liver. Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, SerpinD1 / HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). In a glycosaminoglycan-independent manner, serpinD1 / HC-II also inhibits chymotrypsin. Peptides at the N-terminal of HC-II have chemotactic activity for both monocytes and neutrophils.
Molecular Weight 55.7 kDa
UniProt P05546
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer 50 mM Tris, 150 mM NaCl, pH 7.5
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Supplier Images
SDS-PAGE (SDS) image for serpin Peptidase Inhibitor, Clade D (Heparin Cofactor), Member 1 (SERPIND1) (AA 20-499) (Active) protein (His tag) (ABIN2181748) Human Serpin D1, His Tag on SDS-PAGE under reducing (R) condition. The gel was staine...
Background publications Van Deerlin, Tollefsen: "The N-terminal acidic domain of heparin cofactor II mediates the inhibition of alpha-thrombin in the presence of glycosaminoglycans." in: The Journal of biological chemistry, Vol. 266, Issue 30, pp. 20223-31, 1991 (PubMed).