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Human Polyclonal F12 Primary Antibody for EIA, IHC (p) - ABIN951608
Houlihan, Davies, Tenesa, Harris, Luciano, Gow, McGhee, Liewald, Porteous, Starr, Lowe, Visscher, Deary: Common variants of large effect in F12, KNG1, and HRG are associated with activated partial thromboplastin time. in American journal of human genetics 2010
Show all 7 references for ABIN951608
Human Monoclonal F12 Primary Antibody for ELISA, WB - ABIN395773
Corral, Antón, Quiroga, González-Conejero, Pereira, Roldán, Vicente, Mezzano: Influence of the F12 -4 C>T polymorphism on hemostatic tests. in Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis 2010
Show all 5 references for ABIN395773
Human Polyclonal F12 Primary Antibody for WB - ABIN653621
Calafell, Almasy, Sabater-Lleal, Buil, Mordillo, Ramírez-Soriano, Sikora, Souto, Blangero, Fontcuberta, Soria: Sequence variation and genetic evolution at the human F12 locus: mapping quantitative trait nucleotides that influence FXII plasma levels. in Human molecular genetics 2009
Show all 2 references for ABIN653621
Human Polyclonal F12 Primary Antibody for WB - ABIN2776974
Melo, Mourão: An algal sulfated galactan has an unusual dual effect on venous thrombosis due to activation of factor XII and inhibition of the coagulation proteases. in Thrombosis and haemostasis 2008
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
Results report first report of FXii mutation causing angioedema in a Brazilian family with normal CI inhibitor status.
Factor XI and factor XII activities were significantly higher in patients with slow coronary flow than in controls, and could be associated with enhanced procoagulant state present in these patients.
Results support the importance of contact activation pathway-dependent TG as a risk factor for ischemic stroke, and indicate the importance of F12 SNPs for TG ex vivo and in vivo.
Genotyping these subjects revealed that the carriers of the minor alleles at the two loci- F12 and KLKB1 (show KLKB1 Antibodies) had a significant association with reduced levels of active plasma renin (show REN Antibodies).
The results provide an essential basis for the diagnosis of FXII deficiencies in Chinese.
We postulate that FXIIa first strengthens the clot (show TXNDC17 Antibodies) structure during clot (show TXNDC17 Antibodies) formation and thereafter contributes towards fibrinolysis.
Women with low FXII level might have an increased risk of premature delivery at < 34 GW.
Provide the structural basis for understanding FXII substrate recognition and zymogen activation.
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 (show RIPK4 Antibodies) or fXII deficiency reduced thrombus formation in both arterial and venous thrombosis models, without an apparent effect on hemostasis.
fXI (show F11 Antibodies) and fXII contribute to thrombus formation even when factor VIIa/tissue factor (show F3 Antibodies) 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