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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 Kits (69) and Coagulation Factor X Proteins (21) and many more products for this protein.
Showing 10 out of 121 products:
Human Polyclonal Coagulation Factor X Primary Antibody for EIA, WB - ABIN452984
Alba, Bradshaw, Parker, Bhella, Waddington, Nicklin, van Rooijen, Custers, Goudsmit, Barouch, McVey, Baker: Identification of coagulation factor (F)X binding sites on the adenovirus serotype 5 hexon: effect of mutagenesis on FX interactions and gene transfer. in Blood 2009
Show all 3 references for ABIN452984
Human Polyclonal Coagulation Factor X Primary Antibody for ELISA, WB - ABIN1536097
Leytus, Foster, Kurachi, Davie: Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C. in Biochemistry 1986
Show all 2 references for ABIN1536097
Human Polyclonal Coagulation Factor X Primary Antibody for ELISA, WB - ABIN1536116
Messier, Pittman, Long, Kaufman, Church: Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X. in Gene 1991
Show all 2 references for ABIN1536116
Human Monoclonal Coagulation Factor X Primary Antibody for EIA, WB - ABIN951606
Suvarna, Rauova, McCracken, Goss, Sachais, McKenzie, Reilly, Gunn, Cines, Poncz, Arepally: PF4/heparin complexes are T cell-dependent antigens. in Blood 2005
Cow (Bovine) Polyclonal Coagulation Factor X Primary Antibody for WB - ABIN2776973
Hsu, Tsai, Sun, Chang, Huang, Yu, Lin, Mao, Yang: Factor Xa active site substrate specificity with substrate phage display and computational molecular modeling. in The Journal of biological chemistry 2008
Macrophages regulate FX plasma levels in an SR-AI (show MSR1 Antibodies)-dependent manner.
Factor Xa has a role in inhibiting HMGB1 (show HMGB1 Antibodies)-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 Antibodies) 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 Antibodies) administration to mice overexpressing human EPCR (show PROCR Antibodies). FX does not effectively interact with EPCR (show PROCR Antibodies) 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 Antibodies) mice
Data suggest that tissue factor (show F3 Antibodies) and factor V induction by LPS (show TLR4 Antibodies) may in part accelerate mesangioproliferative glomerulonephritis through activation of factor X and downstream proinflammatory and procoagulant mechanisms.
Gene targeting of tissue factor (show F3 Antibodies), factor X, and factor VII (show TH Antibodies) in mice: their involvement in embryonic development
Factor Xa functions in airway remodeling in asthma by stimulating mucin (show SLC13A2 Antibodies) production, through regulation of amphiregulin (show AREG Antibodies) expression and collagen deposition.
Results show that although factor Xa induces p42 (show EPB42 Antibodies)/44 MAP Kinase (show MAPK1 Antibodies) phosphorylation in endothelial cells, it has no direct effect on endothelial cell proliferation, protein synthesis and tube formation.
homozygous mutation g.27881G>A(p.Val298Met) of the F10 gene has been identified, which probably accounts for the low FX concentrations in this pedigree
Establish FXa as a potentially important asthma mediator, stimulating airway smooth muscle function through actions requiring PAR-1 (show MARK2 Antibodies) and annexin A2 (show ANXA2 Antibodies) and involving integrin coactivation.
FXa may inhibit lipopolysaccharide-mediated expression of sPLA2-IIA (show PLA2G2A Antibodies) by suppression of cytosolic phospholipase A2 (show PLA2G4A Antibodies) and extracellular signal-regulated kinase 1/2 (show MAPK3 Antibodies).
Several members of a family had a c.112 G>C mutation in exon 2 of the F10 gene. Although in-silico analysis predicts this is a benign mutation, this family suggests that the amino acid substitution affects the properties of the factor X protein.
Various acylcarnitines inhibited factor Xa-initiated clotting.
The model of human prothrombinase presented here provides a powerful resource for contextualizing previous data and for designing future experiments
Describe inhibition of tissue factor:factor VIIa-catalyzed factor IX and factor X activation by TFPI (show TFPI Antibodies) and TFPI (show TFPI Antibodies) constructs.
Factor Xa plasma levels were higher in shift work nurses compared to daytime working nurses.
Increased coagulation activity and genetic polymorphisms in the F5, F10 and EPCR (show PROCR Antibodies) genes are associated with breast cancer.
Asp (show ASIP Antibodies)-185 deletion in FX predisposes FX deficient patient to mild bleeding phenotype. The catalytic activity of the recombinant mutant protease is severely impaired.
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 Antibodies) complex formation appears to regulate blood coagulation.
thrombin (show F2 Antibodies) 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 Antibodies) of the coagulation system, was used as a model enzyme to test the canonical conformation hypothesis.
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.
coagulation factor 10
, coagulation factor X
, vitamin K dependent serine protease
, coagulation factor X preproprotein
, Coagulation factor X
, stuart factor
, Stuart-Prower factor
, factor Xa
, blood coagulation factor X
, factor XA light chain
, virus activating protease
, virus-activating protease