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F10 encodes the vitamin K-dependent coagulation factor X of the blood coagulation cascade. Additionally we are shipping Coagulation Factor X Antibodies (239) and Coagulation Factor X Kits (62) and many more products for this protein.
Showing 10 out of 28 products:
zymogen-like factor Xa variants are conformationally dynamic and ligands such as its cofactor, factor Va, stabilize the molecule rescuing procoagulant activity. At the site of vascular injury, the variants in the presence of factor Va serve as effective prohemostatic agents.
Data suggest that, for all coagulation proteins tested (prothrombin, factor X, activated factor VII, activated protein C), tighter binding to lipid bilayers (lower Kd) is observed as the proportion of anionic phospholipid increases. These studies were conducted in high-throughput screening using phospholipid bilayers in nanodiscs with multiplexed silicon photonic sensor (micro-ring resonator) array technology.
A coagulation initiating pathway is revealed in which the TF-FVIIa-nascent FXa complex activates FVIII (show F8 Proteins) apart from thrombin (show F2 Proteins) feedback.
Data suggest oxidized lipid vesicles with phosphatidylserine/polyunsaturated fatty acids promote inactivation of ZPI (show SERPINA10 Proteins)-PZ complex or free ZPI (show SERPINA10 Proteins); binding of PZ-complexed or free ZPI (show SERPINA10 Proteins) to oxidized vesicles mediates inactivation of ZPI (show SERPINA10 Proteins) (an inhibitor of FXa); blocking heparin- (anticoagulant-)binding site on ZPI (show SERPINA10 Proteins) interferes with binding to lipid or PZ. (ZPI (show SERPINA10 Proteins) = protein Z-dependent protease inhibitor (show SERPINA10 Proteins); PZ = protein Z (show PROZ Proteins); FXa = factor Xa)
Factor Va reduced by 100-fold the apparent Kd of myosin for factor Xa (Kd approximately 0.48 nM), primarily by reducing koff, indicating formation of a stable ternary complex of myosin:Xa:Va.
PTX2 (show APCS Proteins) was identified PTX2 (show APCS Proteins) as a novel partner for FX, and both proteins cooperated to prevent their SR-AI (show MSR1 Proteins)-mediated uptake by macrophages.
annexin A2 (show ANXA2 Proteins) contributes to lung injury and fibrotic disease by mediating the fibrogenic actions of FXa.
Individuals suffering from relapsing-remitting and secondary progressive multiple sclerosis had significantly higher prothrombin (show F2 Proteins) and factor X levels than healthy donors, whereas levels were unchanged in primary progressive MS and neuromyelitis optica patients.
Low concentrations of TF and exogenous FXIa, each too low to elicit a burst in thrombin (show F2 Proteins) production alone, act synergistically when in combination to cause substantial thrombin (show F2 Proteins) production.
analysis of how physiological concentrations of Tissue factor pathway inhibitor (show TFPI Proteins) inhibit FXa
PTX2 (show PITX2 Proteins) was identified PTX2 (show PITX2 Proteins) as a novel partner for FX, and both proteins cooperated to prevent their SR-AI (show MSR1 Proteins)-mediated uptake by macrophages.
Enhanced FXa and PAR2 (show F2RL1 Proteins) exacerbate DN and that both are promising targets for preventing diabetic nephropathy.
Macrophages regulate FX plasma levels in an SR-AI (show MSR1 Proteins)-dependent manner.
Factor Xa has a role in inhibiting HMGB1 (show HMGB1 Proteins)-induced septic responses in human umbilical vein endothelial cells and in mice
Selective inhibition of FXa improves the left ventricular function during CVB3-induced myocarditis and seems to be associated with an improved myocardial remodeling.
Activated factor X signaling via protease-activated receptor 2 (show F2RL1 Proteins) suppresses pro-inflammatory cytokine production from lipopolysaccharide-stimulated myeloid cells.
There was no detectable increase in plasma levels of mouse FX after active-site inhibited human APC (show APC Proteins) administration to mice overexpressing human EPCR (show PROCR Proteins). FX does not effectively interact with EPCR (show PROCR Proteins) in vivo, at least in regards to the mouse system.
investigation of role of F10a in progression of diabetic nephropathy: data from studies using inhibitor of F10a suggest that F10a does play a role in development of proteinemia, glomerular hypertrophy, and protein deposition in kidney of db/db (show LEPR Proteins) mice
Data suggest that tissue factor (show F3 Proteins) and factor V induction by LPS (show TLR4 Proteins) may in part accelerate mesangioproliferative glomerulonephritis through activation of factor X and downstream proinflammatory and procoagulant mechanisms.
Data suggest factor Xa (FXa) and factor Va (FVa) compete to bind FXa on both PS model membranes and microparticles from activated platelets; this competition between dimerization/prothrombinase (show FGL2 Proteins) complex formation appears to regulate blood coagulation.
thrombin (show F2 Proteins) and factor Xa diffusion along the heparin molecule explains the effects of extended heparin chain lengths
Factor Xa (fXa), a key serine protease (show F2 Proteins) of the coagulation system, was used as a model enzyme to test the canonical conformation hypothesis.
These findings as well as the prolonged survival of f10(-/-) mutants will enable us to expand our understanding of the molecular mechanisms of hemostasis, including a platform for screening variants of uncertain significance in patients with F10 deficiency and other coagulation disorders
This gene encodes the vitamin K-dependent coagulation factor X of the blood coagulation cascade. This factor undergoes multiple processing steps before its preproprotein is converted to a mature two-chain form by the excision of the tripeptide RKR. Two chains of the factor are held together by 1 or more disulfide bonds\; the light chain contains 2 EGF-like domains, while the heavy chain contains the catalytic domain which is structurally homologous to those of the other hemostatic serine proteases. The mature factor is activated by the cleavage of the activation peptide by factor IXa (in the intrisic pathway), or by factor VIIa (in the extrinsic pathway). The activated factor then converts prothrombin to thrombin in the presence of factor Va, Ca+2, and phospholipid during blood clotting. Mutations of this gene result in factor X deficiency, a hemorrhagic condition of variable severity.
, factor Xa
, stuart factor
, coagulation factor 10
, factor XA light chain
, virus activating protease
, virus-activating protease
, coagulation factor X
, vitamin K dependent serine protease
, coagulation factor X preproprotein
, blood coagulation factor X
, Coagulation factor X
, coagulation factor 10 L homeolog