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The protein encoded by SERPINC1 is a plasma protease inhibitor and a member of the serpin superfamily. Additionally we are shipping Serine (Or Cysteine) Peptidase Inhibitor, Clade C (Antithrombin), Member 1 Kits (48) and Serine (Or Cysteine) Peptidase Inhibitor, Clade C (Antithrombin), Member 1 Proteins (31) and many more products for this protein.
Showing 10 out of 270 products:
Mouse (Murine) Polyclonal SERPINC1 Primary Antibody for WB - ABIN610759
Cool, Normant, Shen, Chen, Pannell, Zhang, Loh: Carboxypeptidase E is a regulated secretory pathway sorting receptor: genetic obliteration leads to endocrine disorders in Cpe(fat) mice. in Cell 1997
Show all 4 references for ABIN610759
Human Polyclonal SERPINC1 Primary Antibody for EIA, WB - ABIN453366
REIF, POTTER: Oxidative pathways insensitive to antimycin A. in Archives of biochemistry and biophysics 1954
Show all 2 references for ABIN453366
Human Polyclonal SERPINC1 Primary Antibody for IHC, WB - ABIN2776790
Lee, Kim, Kim, Schuit, Kim: Detection of large deletion mutations in the SERPINC1 gene causing hereditary antithrombin deficiency by multiplex ligation-dependent probe amplification (MLPA). in Journal of thrombosis and haemostasis : JTH 2008
RNA interference of Serpinc1 and/or Proc allows for evaluation of the function of these genes in vivo and provides a novel, controlled mouse model for spontaneous venous thrombosis.
Our studies of ATIII in-cell folding reveal a surprising, biased order of disulfide bond formation, with early formation of the C-terminal disulfide, before formation of the N-terminal disulfides, critical for folding to the active, metastable state
Describe antibody specifically targeting a unique conformational epitope on antithrombin III beta conformation that blocks anticoagulation.
This is the first case of pregnancy related stroke, associated with type-II heparin binding site antithrombin deficiency (c. 391C > T, p.Leu131Phe), that has been reported so far. A genetic analysis of the AT gene (SERPINC1) was performed.
Elevated levels of circulating microparticles can play a role in carriers of mild and severe inherited thrombophilia resulting from antithrombin deficiency.
The relevance of the vitamin D pathway on the regulation of SERPINC1 was confirmed in a cell model.
The increased SERPINC1 SNP frequency among Han patients receiving heart surgery might contribute to the differences in their perioperative sensitivity to heparin
Patients with low antithrombin III activities presented a higher risk of developing acute kidney injury after cardiac surgery.
Letter/Case Report: novel antithrombin mutation resulting in antithrombin deficiency and arterial/venous thrombosis.
This suggests that allosteric information propagation pathways are present even in the non-activated native form of antithrombin.
analysis of mutations in SERPINC1 with a role in Hereditary antithrombin (AT) deficiency
ATIII may be protective in HIV-1 disease by inhibiting HIV-1 replication
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.
, serine (or cysteine) proteinase inhibitor, clade C (antithrombin), member 1
, serpin C1
, serpin peptidase inhibitor, clade C, member 1
, serpin peptidase inhibitor, clade C (antithrombin), member 1
, antithrombin III
, serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1