SERPIND1 Human

Serpin Peptidase Inhibitor, Clade D Member 1 Human Recombinant
Cat. No.
BT24621
Source
Escherichia Coli.
Synonyms

Serpin Family D Member 1, Cysteine Proteinase Inhibitor Clade D Member 1, Serpin Peptidase Inhibitor Clade D Member 1, Protease Inhibitor Leuserpin-2, Serpin D1, HCF2, HLS2, Leuserpin 2, D22S673, THPH10, HC-II, HCII, HC2, LS2.

Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85% as determined by SDS-PAGE.
Usage
THE BioTek'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

SERPIND1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 465 amino acids (58-499) and having a molecular mass of 53.3kDa.
SERPIND1 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction

Serpin Peptidase Inhibitor, Clade D Member 1 (SERPIND1), also known as heparin cofactor II, is a protein that in humans is encoded by the SERPIND1 gene. This gene belongs to the serpin superfamily whose members are the most important inhibitors of serine proteases in human plasma. SERPIND1 is a potent inhibitor of thrombin, a key enzyme in the coagulation cascade. The inhibitory activity of SERPIND1 is significantly enhanced in the presence of glycosaminoglycans such as dermatan sulfate and heparin. SERPIND1 is primarily synthesized in the liver and circulates in the bloodstream. Mutations in this gene are associated with SERPIND1 deficiency, a rare bleeding disorder characterized by a reduced ability to control blood clotting.

Description
Recombinant SERPIND1 protein expressed in E.coli is a monomeric, non-glycosylated polypeptide consisting of 465 amino acid residues (58-499) and having a molecular weight of 53.3 kDa. This protein includes a 23 amino acid His-tag sequence linked to the N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless, and sterile-filtered solution.
Formulation
SERPIND1 is supplied as a 1 mg/ml solution in a buffer containing 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 0.4 M urea.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 85% as assessed by SDS-PAGE analysis.
Synonyms

Serpin Family D Member 1, Cysteine Proteinase Inhibitor Clade D Member 1, Serpin Peptidase Inhibitor Clade D Member 1, Protease Inhibitor Leuserpin-2, Serpin D1, HCF2, HLS2, Leuserpin 2, D22S673, THPH10, HC-II, HCII, HC2, LS2.

Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDFHKENT VTNDWIPEGE EDDDYLDLEK IFSEDDDYID IVDSLSVSPT DSDVSAGNIL QLFHGKSRIQ RLNILNAKFA FNLYRVLKDQ VNTFDNIFIA PVGISTAMGM ISLGLKGETH EQVHSILHFK DFVNASSKYE ITTIHNLFRK LTHRLFRRNF GYTLRSVNDL YIQKQFPILL DFKTKVREYY FAEAQIADFS DPAFISKTNN HIMKLTKGLI KDALENIDPA TQMMILNCIY FKGSWVNKFP VEMTHNHNFR LNEREVVKVS MMQTKGNFLA ANDQELDCDI LQLEYVGGIS MLIVVPHKMS GMKTLEAQLT PRVVERWQKS MTNRTREVLL PKFKLEKNYN LVESLKLMGI RMLFDKNGNM AGISDQRIAI DLFKHQGTIT VNEEGTQATT VTTVGFMPLS TQVRFTVDRP FLFLIYEHRT SCLLFMGRVA NPSRS.

Product Science Overview

Gene and Protein Structure

The SERPIND1 gene encodes a plasma serine protease that functions primarily as a thrombin and chymotrypsin inhibitor . The protein is activated by heparin, dermatan sulfate, and glycosaminoglycans . Members of the serpin family have highly conserved secondary structures with a reactive center loop that interacts with the protease active site to inhibit protease activity .

Function and Mechanism

SERPIND1 is known for its role as a thrombin inhibitor. In the presence of glycosaminoglycans like heparin or dermatan sulfate, Heparin Cofactor II (HC-II), which is encoded by the SERPIND1 gene, becomes the predominant thrombin inhibitor, replacing antithrombin III (AT-III) . This mechanism is essential for regulating blood coagulation and preventing excessive clot formation .

Clinical Significance

Mutations or deficiencies in the SERPIND1 gene are associated with Heparin Cofactor II deficiency, a condition that can lead to an increased risk of thrombosis . Additionally, variations in this gene have been linked to autosomal recessive nonsyndromic deafness 116 .

Research and Applications

Human recombinant SERPIND1 is used in various research applications to study its role in blood coagulation and its potential therapeutic uses. Understanding the function and regulation of this protein can provide insights into developing treatments for coagulation disorders and other related conditions .

For more detailed information, you can refer to resources like GeneCards and the Early Detection Research Network.

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