SerpinC1 / AntithrombinIII / ATIII Recombinant Protein | ATIII recombinant protein

Recombinant Human SerpinC1 / AntithrombinIII / ATIII Protein (His tag)

Cat. Num. AAA2546489

• Gene Names: SERPINC1; AT3; AT3D; ATIII; THPH7
• Purity: > 95 % as determined by SDS-PAGE
• Synonyms: SerpinC1 / AntithrombinIII / ATIII; Recombinant Human SerpinC1 / AntithrombinIII / ATIII Protein (His tag); SerpinC1; AT3; ATIII; MGC22579; ATIII recombinant protein

• Host: Human Cells
• Purity/Purification: > 95 % as determined by SDS-PAGE
• Form/Format: Lyophilized from sterile PBS, pH 7.4
• Sequence Length: 464

• Application Notes: The recombinant human SerpinC1 consists of 443 amino acids and has a predicted molecular mass of 50.5 kDa. In SDS-PAGE, the apparent molecular mass of rhSerpinC1 is approximately 55-60 kDa due to glycosylation.
• Predicted N Terminal: His 33
• Endotoxin: < 1.0 EU per mug of the protein as determined by the LAL method
• Preparation and Storage: Samples are stable for up to twelve months from date of receipt at -70 degree C

SDS-PAGE

Related Product Information for ATIII recombinant protein

Background: SerpinC1, also known as antithrombin III (AT III), is a member of the serpin superfamily of serine protease inhibitors, and has been found to be a marker for disseminated intravascular coagulation (DIC) and to be of prognostic significance in septic patients. SerpinC1 synthesized in the liver is the principal plasma serpin of blood coagulation proteases and inhibits thrombin and other factors such as Xa by the formation of covalently linked complexes. Thus it is one of the most important coagulation inhibitors and the fundamental enzyme for the therapeutical action of heparin. In common with SerpinA5 and D1, the inhibitory activity of SerpinC1 undergoes a dramatic increase in the presence of heparin and other glycosaminoglycans. ATIII mediates the promotion of prostaglandin release, an inhibitor of leucocyte activation and downregulator of many proinflammatory cytokines. Antithrombin III exerts anti-inflammatory properties in addition to its anti-coagulative mechanisms. In animal models of sepsis, ATIII affected cytokine plasma concentrations with a decrease of pro-inflammatory cytokines. The deficiency or functional abnormality of ATIII may result in an increased risk of thromboembolic disease, such as deep vein thrombosis and pulmonary embolism. In addition, it has been reported that SerpinC1 can alter or influence inflammatory processes via inhibition of NF-kappaB activation or actin polymerization.

Description: A DNA sequence encoding the human SerpinC1 (NP_000479.1) (Met 1-Lys 464) was expressed with a C-terminal polyhistidine tag.

NCBI and Uniprot Product Information

• NCBI GI #: 4502261
• NCBI GeneID: 462
• NCBI Accession #: NP_000479.1
• NCBI GenBank Nucleotide #: NM_000488.3
• Molecular Weight: 52,602 Da
• NCBI Official Full Name: antithrombin-III
• NCBI Official Synonym Full Names: serpin family C member 1
• NCBI Official Symbol: SERPINC1
• NCBI Official Synonym Symbols: AT3; AT3D; ATIII; THPH7
• NCBI Protein Information: antithrombin-III
• UniProt Protein Name: Antithrombin-III
• UniProt Gene Name: SERPINC1
• UniProt Synonym Gene Names: AT3; ATIII

NCBI Description

The protein encoded by this gene is a plasma protease inhibitor and a member of the serpin superfamily. This protein inhibits thrombin as well as other activated serine proteases of the coagulation system, and it regulates the blood coagulation cascade. The protein includes two functional domains: the heparin binding-domain at the N-terminus of the mature protein, and the reactive site domain at the C-terminus. The inhibitory activity is enhanced by the presence of heparin. More than 120 mutations have been identified for this gene, many of which are known to cause antithrombin-III deficiency. [provided by RefSeq, Jul 2009]

Uniprot Description

Most important serine protease inhibitor in plasma that regulates the blood coagulation cascade. AT-III inhibits thrombin, matriptase-3/TMPRSS7, as well as factors IXa, Xa and XIa. Its inhibitory activity is greatly enhanced in the presence of heparin.