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Human Polyclonal F12 Primary Antibody for IHC, IHC (p) - ABIN4310030
Kato, Nicholson, Neiman, Rantalainen, Holmes, Barrett, Uhlén, Nilsson, Spector, Schwenk: Variance decomposition of protein profiles from antibody arrays using a longitudinal twin model. in Proteome science 2011
These mechanisms include newly recognized contributions of fibrin network structure and factor XIII(a)-mediated fibrin crosslinking to venous thrombus composition, size, and stability.
Downregulating FXII-mediated signaling in neutrophils is associated with improved wound healing.
findings suggest that the double mutations in the FXII gene were the causing reasons for the decreased FXII:C and FXII:Ag. These results not only enriched the F12 mutation database in this condition, but also helped to identify the genetic defects of FXII in China.
Heterozygous F12 mutation decreases the plasma FXII activity approximately by half and cause moderate FXII deficiency in a Chinese population.
High levels of FXII activity are present in the plasma of multiple sclerosis patients during relapse.
The induction of TG by BXPC3 cells was mainly driven by the TF pathway while TG generation triggered by MCF7 cells was also driven by FXII activation.
defective FXII contact activation provides thromboprotection, excess activation underlies the swelling disorder hereditary angioedema type III. This review provides an overview of the molecular basis of FXII contact activation and FXII contact activation-associated disease states.
Accumulation of FXII in acute respiratory distress syndrome lungs may contribute to the release of pro-inflammatory mediators, regulating lung inflammation.
Data suggest that coagulation factor XII (FXII) homozygous p.Gly341Arg mutation, caused by consanguineous marriage, probably underlies the congenital FXII deficiency in the pedigree.
FXII deficiency impairs thrombosis in animal models without inducing abnormal excessive bleeding. Recent work has established the FXIIa-driven contact system as promising target for anticoagulant and anti-inflammatory drugs. This review focuses on the biochemistry of the contact system, its regulation by endogenous and exogenous inhibitors, and roles in disease states
Results demonstrated that the composition of the solution and the surface properties of the material all contribute to the observation of contact activation, and the activation of FXII is not specific to anionic surfaces as has been long believed.
Report an independent association between FXII levels and the risk of hemorrhagic stroke in Swedish population.
analysis of how FXII reacts to surface materials, which can be applied to the activities of FXII in its natural environment [review]
beta-amyloid interacts with fibrinogen and factor XII. These interactions can lead to increased clotting, abnormal clot formation, persistent fibrin deposition, and generation of proinflammatory molecules.
Abeta activates FXII, resulting in FXI activation and thrombin generation in human plasma, thereby establishing Abeta as a possible driver of prothrombotic states
results support a model for induction of contact activation in which activity intrinsic to single-chain FXII initiates alphaFXIIa and alpha-kallikrein formation on a surface. alphaFXIIa, with support from alpha-kallikrein, 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 activator.
inhibition of FXI 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.
Deficiency or pharmacologic blockade of FXII renders mice less susceptible to experimental autoimmune encephalomyelitis (a model of multiple sclerosis) and is accompanied by reduced numbers of interleukin-17A-producing T cells.
FXI protects against sepsis derived from Streptococcus pneumoniae or Klebsiella pneumoniae pneumonia at least in part by enhancing the phagocytic capacity of neutrophils by a mechanism that is independent of activation via FXIIa.
FXII plays an important role in atherosclerotic lesion formation by functioning as a strong inducer of pro-inflammatory cytokines in antigen-presenting cells.
Genetic deficiency of factor XII diminished brain injury-induced bradykinin release and minimized brain lesion size.
FXI 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
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
FVIIa- and FXIIa-triggered coagulation pathways have distinct but complementary roles in atherothrombus formation.
Inhibiting factor XIIa with rHA-Infestin-4 may present a safe and effective treatment to decrease the morbidity of silent brain ischemia.
PKK or fXII deficiency reduced thrombus formation in both arterial and venous thrombosis models, without an apparent effect on hemostasis.
fXI and fXII contribute to thrombus formation even when factor VIIa/tissue factor 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