Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
The protein encoded by SERPINC1 is a plasma protease inhibitor and a member of the serpin superfamily. Zusätzlich bieten wir Ihnen Serine (Or Cysteine) Peptidase Inhibitor, Clade C (Antithrombin), Member 1 Antikörper (289) und Serine (Or Cysteine) Peptidase Inhibitor, Clade C (Antithrombin), Member 1 Kits (66) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 34 products:
Human SERPINC1 Protein expressed in Human - ABIN3119645
Tafaleng, Chakraborty, Han, Hale, Wu, Soto-Gutierrez, Feghali-Bostwick, Wilson, Kotton, Nagaya, Strom, Roy-Chowdhury, Stolz, Perlmutter, Fox: Induced pluripotent stem cells model personalized variations in liver disease resulting from α1-antitrypsin deficiency. in Hepatology (Baltimore, Md.) 2015
Show all 2 Pubmed References
Human SERPINC1 Protein expressed in Human - ABIN491621
Gardell, Krueger, Antrilli, Elokdah, Mayer, Orcutt, Crandall, Vlasuk: Neutralization of plasminogen activator inhibitor I (PAI-1) by the synthetic antagonist PAI-749 via a dual mechanism of action. in Molecular pharmacology 2007
The results this study reveal several novel mutations to the already growing list of SERPINC1 mutations, thereby adding to our knowledge of the molecular background of antithrombin deficiency.
Data indicate that all patients suffered from homozygous antithrombin (AT) deficiency caused by the mutation p.Leu131Phe in the AT gene (SERPINC1).
Studies indicate that antithrombin III (ATIII) and its gene SerpinC1 may be related to many diseases, including hypertension and kidney diseases.
The odds ratio of developing idiopathic fatal pulmonary embolism as a variant carrier for SERPINC1 is 144.2 (95% CI, 26.3-779.4; P = 1.7 x 10- 7).
In Hungary, the founder mutation, ATBp3, is the most common Antithrombin deficiency
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.
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.
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 peptidase inhibitor, clade C (antithrombin), member 1
, anti-thrombin 3
, serpin C1
, serpin peptidase inhibitor, clade C, member 1
, antithrombin III
, serine (or cysteine) peptidase inhibitor, clade C (antithrombin), member 1