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F10 encodes the vitamin K-dependent coagulation factor X of the blood coagulation cascade. Zusätzlich bieten wir Ihnen Coagulation Factor X Kits (56) und Coagulation Factor X Proteine (23) und viele weitere Produktgruppen zu diesem Protein an.
Showing 10 out of 120 products:
Human Polyclonal Coagulation Factor X Primary Antibody für 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
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Human Polyclonal Coagulation Factor X Primary Antibody für 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
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Human Polyclonal Coagulation Factor X Primary Antibody für 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
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Human Monoclonal Coagulation Factor X Primary Antibody für 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 für 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 (zeige MSR1 Antikörper)-dependent manner.
Factor Xa has a role in inhibiting HMGB1 (zeige HMGB1 Antikörper)-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 (zeige F2RL1 Antikörper) 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 (zeige APC Antikörper) administration to mice overexpressing human EPCR (zeige PROCR Antikörper). FX does not effectively interact with EPCR (zeige PROCR Antikörper) 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 (zeige LEPR Antikörper) mice
Data suggest that tissue factor (zeige F3 Antikörper) and factor V induction by LPS (zeige TLR4 Antikörper) may in part accelerate mesangioproliferative glomerulonephritis through activation of factor X and downstream proinflammatory and procoagulant mechanisms.
Gene targeting of tissue factor (zeige F3 Antikörper), factor X, and factor VII (zeige TH Antikörper) in mice: their involvement in embryonic development
Factor Xa functions in airway remodeling in asthma by stimulating mucin (zeige SLC13A2 Antikörper) production, through regulation of amphiregulin (zeige AREG Antikörper) expression and collagen deposition.
Results show that although factor Xa induces p42 (zeige EPB42 Antikörper)/44 MAP Kinase (zeige MAPK1 Antikörper) phosphorylation in endothelial cells, it has no direct effect on endothelial cell proliferation, protein synthesis and tube formation.
analysis of how physiological concentrations of Tissue factor pathway inhibitor (zeige TFPI Antikörper) inhibit FXa
According to our study, compounds 1a, 1g and 1s displayed evident FXa inhibitory activity and excellent selectivity over thrombin (zeige F2 Antikörper) in in vitro inhibition activities studies.
Large deletions play a minor but essential role in the mutational spectrum of the F7 and F10 genes. Copy number analyses (e. g. MLPA) should be considered if sequencing cannot clarify the underlying reason of an observed coagulopathy. Of note, in cases of combined FVII (zeige F7 Antikörper)/FX deficiency, a deletion of the two contiguous genes might be part of a larger chromosomal rearrangement.
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 (zeige MARK2 Antikörper) and annexin A2 (zeige ANXA2 Antikörper) and involving integrin coactivation.
FXa may inhibit lipopolysaccharide-mediated expression of sPLA2-IIA (zeige PLA2G2A Antikörper) by suppression of cytosolic phospholipase A2 (zeige PLA2G4A Antikörper) and extracellular signal-regulated kinase 1/2 (zeige MAPK3 Antikörper).
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 (zeige TFPI Antikörper) and TFPI (zeige TFPI Antikörper) constructs.
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 (zeige FGL2 Antikörper) complex formation appears to regulate blood coagulation.
thrombin (zeige F2 Antikörper) and factor Xa diffusion along the heparin molecule explains the effects of extended heparin chain lengths
Factor Xa (fXa), a key serine protease (zeige F2 Antikörper) 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