SERPINC1 Human

Serpin Peptidase Inhibitor, Clade C Member 1 Human Recombinant
Cat. No.
BT15297
Source
Escherichia Coli.
Synonyms
AT3, AT3D, ATIII, THPH7, Antithrombin-III, Serpin C1, SERPINC1.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85.0% 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

SERPINC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 455 amino acids (33-464 a.a) and having a molecular mass of 51.4kDa.
SERPINC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction

Belonging to the serpin superfamily, Serpin Peptidase Inhibitor, Clade C Member 1 (SERPINC1) functions as a plasma protease inhibitor. SERPINC1 plays a crucial role in regulating the blood coagulation cascade by inhibiting thrombin, along with other activated serine proteases involved in this pathway. Specifically, SERPINC1 inhibits Thrombin and Factors IXa, Xa, and XIa. Deficiencies in SERPINC1 can lead to antithrombin III (ATIII) deficiency, an autosomal dominant disorder that may result in hereditary thrombophilia, a condition characterized by an increased tendency for blood clotting.

Description
Recombinant human SERPINC1, expressed in E. coli, is a single, non-glycosylated polypeptide chain consisting of 455 amino acids (residues 33-464). With a molecular weight of 51.4 kDa, SERPINC1 is fused to a 23-amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
A clear, sterile-filtered solution.
Formulation
The SERPINC1 protein solution is provided at a concentration of 0.5 mg/ml and contains 20 mM Tris-HCl buffer (pH 8.0), 0.4 M Urea, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Repeated freezing and thawing should be avoided.
Purity
SDS-PAGE analysis indicates a purity greater than 85.0%.
Synonyms
AT3, AT3D, ATIII, THPH7, Antithrombin-III, Serpin C1, SERPINC1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHGSPVDI CTAKPRDIPM NPMCIYRSPE KKATEDEGSE QKIPEATNRR VWELSKANSR FATTFYQHLA DSKNDNDNIF LSPLSISTAF AMTKLGACND TLQQLMEVFK FDTISEKTSD QIHFFFAKLN CRLYRKANKS SKLVSANRLF GDKSLTFNET YQDISELVYG AKLQPLDFKE NAEQSRAAIN KWVSNKTEGR ITDVIPSEAI NELTVLVLVN TIYFKGLWKS KFSPENTRKE LFYKADGESC SASMMYQEGK FRYRRVAEGT QVLELPFKGD DITMVLILPK PEKSLAKVEK ELTPEVLQEW LDELEEMMLV VHMPRFRIED GFSLKEQLQD MGLVDLFSPE KSKLPGIVAE GRDDLYVSDA FHKAFLEVNE EGSEAAASTA VVIAGRSLNP NRVTFKANRP FLVFIREVPL NTIIFMGRVA NPCVK.

Product Science Overview

Introduction

Serpin Peptidase Inhibitor, Clade C Member 1, also known as Antithrombin III (ATIII), is a crucial protein in the regulation of blood coagulation. It belongs to the serine protease inhibitor (serpin) superfamily, which includes proteins that inhibit proteases by trapping them in a stable complex. This article delves into the background, structure, function, and clinical significance of this important protein.

Gene and Protein Structure

The gene encoding Serpin Peptidase Inhibitor, Clade C Member 1, is located on chromosome 1q25.1 . The protein is synthesized in the liver and secreted into the bloodstream. It consists of 432 amino acids, including six cysteines that form three disulfide bonds . The protein has four glycosylation sites, which are crucial for its stability and function .

The protein contains two important functional domains:

  1. Reactive Center: Located near the C-terminus, this domain includes the proteinase target cleavage site at arginine 393 and serine 394 .
  2. Glycosaminoglycan-Binding Site: Located in the N-terminus, this domain interacts with heparin and certain endothelial cell surface heparan sulfate proteoglycans .
Function

Antithrombin III is the most important inhibitor of thrombin and other coagulation proteinases . It regulates clot formation by inhibiting thrombin activity directly and interfering with earlier stages of the clotting cascade . The heparin-antithrombin mechanism is one of the principal natural anticoagulant systems that exert damping effects on various steps of the coagulation cascade .

Clinical Significance

Inherited antithrombin III deficiency is a risk factor for the early development of venous thromboembolism . This condition, known as Thrombophilia 7, can lead to severe complications if not managed properly . Additionally, recent studies have shown that Serpin Peptidase Inhibitor, Clade C Member 1, acts as a tumor suppressor in hepatocellular carcinoma by inducing apoptosis and blocking macrophage polarization .

Recombinant Production

Human recombinant Antithrombin III is produced using recombinant DNA technology. This involves inserting the gene encoding the protein into a suitable expression system, such as bacteria or mammalian cells, to produce the protein in large quantities. Recombinant Antithrombin III is used in clinical settings to treat patients with hereditary antithrombin deficiency and to prevent thromboembolic events during surgeries and childbirth.

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