Mouse monoclonal primary
SERPINC1 Mouse Monoclonal Antibody [15F1] (EM1901-11)
Synthetic peptide within human aa 100-400.
HL-60 cell lysates, HepG2 cell lysate, SiHa cell lysate, U937 cell lysate, zebrafish tissue lysates, rat testis tissue, human lung carcinoma tissue, human liver tissue, mouse kidney tissue, HCT116.
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
ANT3_HUMAN antibody; Antithrombin antibody; Antithrombin III antibody; Antithrombin-III antibody; AntithrombinIII antibody; AT 3 antibody; AT III antibody; AT3 antibody; AT3D antibody; ATIII antibody; Heparin cofactor I antibody; MGC22579 antibody; Serine (or cysteine) proteinase inhibitor clade C (antithrombin) member 1 antibody; Serine cysteine proteinase inhibitor clade C member 1 antibody; Serine proteinase inhibitor clade C member 1 antibody; Serpin C1 antibody; Serpin family C member 1 antibody; Serpin peptidase inhibitor clade C (antithrombin) member 1 antibody; SERPINC1 antibody; THPH7 antibody
Belongs to the serpin family.
Found in plasma.
Phosphorylated by FAM20C in the extracellular medium.
Extracellular space or secreted.
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. 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.