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results support a model for induction of contact activation in which activity intrinsic to single-chain FXII initiates alphaFXIIa and alpha-kallikrein (zeige KLK4 Proteine) formation on a surface. alphaFXIIa, with support from alpha-kallikrein (zeige KLK4 Proteine), subsequently accelerates contact activation and is responsible for the full procoagulant activity of FXII.
The XPNPEP2 c-2399A and the ACE insertion/deletion polymorphisms analyzed in a population of patients with hereditary angioedema with F12 mutation were not a major determinant of disease expression.
in the presence of platelet polyphosphate and the downstream substrate fibrin, alphaFXIIa is a highly efficient and favorable plasminogen (zeige PLG Proteine) activator.
inhibition of FXI (zeige F11 Proteine) and FXII distinctly alter the biophysical properties of fibrin.
6 different mutations, including 3 missense mutations (Gly341Arg, Glu502Lys and Gly542 Ser), 1 insertion (7142insertC) and 2 deletions (5741-5742 delCA and 6753-6755delACA), were identixFB01;ed on the F12 gene. Three of them (Gly341Arg, 5741-5742delCA and 6753-6755delACA) are reported here for the first time.
The present findings therefore suggest that homozygous FXII-HAE mutation status leads to a severe phenotype in females and males, and to an increased risk of manifest symptoms in the latter.
As the factor XII pathway specifically contributes to thrombosis but not to hemostasis, interference with this pathway provides a unique opportunity for safe anticoagulation that is not associated with excess bleeding. The review summarizes current knowledge on factor XII functions, activators and inhibitors.
It is concluded that F12-46C/T carriage acts as an independent modifier of hereditary angioedema due to C1-INH (zeige SERPING1 Proteine) deficiency severity.
Active neutrophil extracellular traps formation can induce factor XII-mediated coagulation activation in patients with disseminated intravascular coagulation with poor prognosis.
findings suggest that the three mutations in the F12 gene are the causing reasons for the cross-reactive material-negative FXII deficiencies
FXI (zeige F11 Proteine) attenuates part of the allergic response to repeated administration of house dust mite in the airways by a mechanism that is independent of activation via FXII
onset and severity of the thrombotic phenotype are dependent on the presence of platelets but not circulating neutrophils. Unexpectedly, FXII has a protective effect.
Wild type mice developed carotid artery occlusion when the vessel was exposed to a 3.5% solution of ferric chloride (FeCl3). FXII-deficient mice were resistant to occlusion at 5% FeCl3 and partially resistant at 10% FeCl3.
the results of this study characterize the mechanism of HAEIII and establish FXII inhibition as a potential therapeutic strategy to interfere with excessive vascular leakage in HAEIII
Inhibiting factor XIIa with rHA-Infestin-4 may present a safe and effective treatment to decrease the morbidity of silent brain ischemia.
PKK (zeige RIPK4 Proteine) or fXII deficiency reduced thrombus formation in both arterial and venous thrombosis models, without an apparent effect on hemostasis.
fXI (zeige F11 Proteine) and fXII contribute to thrombus formation even when factor VIIa/tissue factor (zeige F3 Proteine) initiates thrombosis.
F12 KNOCKOUT MICE, generated to elucidate the biological role(s) of FXII, had a markedly prolonged APTT. Deficiency of murine FXII does not cause thrombophilia or impaired fibrinolysis or affect hemostasis.
FXII-mediated fibrin formation is crucial for pathological arterial thrombosis but not for hemostasis
This gene encodes coagulation factor XII which circulates in blood as a zymogen. This single chain zymogen is converted to a two-chain serine protease with an heavy chain (alpha-factor XIIa) and a light chain. The heavy chain contains two fibronectin-type domains, two epidermal growth factor (EGF)-like domains, a kringle domain and a proline-rich domain, whereas the light chain contains only a catalytic domain. On activation, further cleavages takes place in the heavy chain, resulting in the production of beta-factor XIIa light chain and the alpha-factor XIIa light chain becomes beta-factor XIIa heavy chain. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then to beta-factor XIIa. The active factor XIIa participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. It activates coagulation factors VII and XI. Defects in this gene do not cause any clinical symptoms and the sole effect is that whole-blood clotting time is prolonged.
, beta-factor XIIa part 1
, beta-factor XIIa part 2
, coagulation factor XII
, coagulation factor XIIa heavy chain
, coagulation factor XIIa light chain
, factor XII
, hageman factor