Recombinant Human Factor X protein
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Recombinant Human Factor X protein is a Human Full Length protein, in the 32 to 488 aa range, expressed in Wheat germ, suitable for ELISA, WB.
View Alternative Names
Coagulation factor X, Stuart factor, Stuart-Prower factor, F10
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human Factor X protein (AB158407)
ab158407 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Factor X contributes significantly to the coagulation process by activating prothrombin into thrombin. It is not part of a larger complex but functions closely with other components of the coagulation cascade to maintain hemostasis. Factor X interacts with calcium ions and phospholipids on the surface of platelets enhancing its enzymatic activity. This activation ensures proper regulation of blood clotting preventing excessive bleeding or uncontrolled clot formation.
Pathways
Factor X is central to both the intrinsic and extrinsic coagulation pathways. It interacts with proteins such as factor VIIa in the extrinsic pathway and factor IXa in the intrinsic pathway both pathways leading to the activation of factor Xa. In turn factor Xa is key in the common pathway which combines inputs from the intrinsic and extrinsic pathways to produce thrombin essential for fibrin clot formation.
Specifications
Form
Liquid
General info
Function
Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting (PubMed : 22409427). Factor Xa activates pro-inflammatory signaling pathways in a protease-activated receptor (PAR)-dependent manner (PubMed : 24041930, PubMed : 30568593, PubMed : 34831181, PubMed : 18202198). Up-regulates expression of protease-activated receptors (PARs) F2R, F2RL1 and F2RL2 in dermal microvascular endothelial cells (PubMed : 35738824). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2 and IL6, in cardiac fibroblasts and umbilical vein endothelial cells in PAR-1/F2R-dependent manner (PubMed : 30568593, PubMed : 34831181). Triggers the production of pro-inflammatory cytokines, such as MCP-1/CCL2, IL6, TNF-alpha/TNF, IL-1beta/IL1B, IL8/CXCL8 and IL18, in endothelial cells and atrial tissues (PubMed : 24041930, PubMed : 35738824, PubMed : 9780208). Induces expression of adhesion molecules, such as ICAM1, VCAM1 and SELE, in endothelial cells and atrial tissues (PubMed : 24041930, PubMed : 35738824, PubMed : 9780208). Increases expression of phosphorylated ERK1/2 in dermal microvascular endothelial cells and atrial tissues (PubMed : 24041930, PubMed : 35738824). Triggers activation of the transcription factor NF-kappa-B in dermal microvascular endothelial cells and atrial tissues (PubMed : 24041930, PubMed : 35738824). Activates pro-inflammatory and pro-fibrotic responses in dermal fibroblasts and enhances wound healing probably via PAR-2/F2RL1-dependent mechanism (PubMed : 18202198). Activates barrier protective signaling responses in endothelial cells in PAR-2/F2RL1-dependent manner; the activity depends on the cleavage of PAR-2/F2RL1 by factor Xa (PubMed : 22409427). Up-regulates expression of plasminogen activator inhibitor 1 (SERPINE1) in atrial tissues (PubMed : 24041930).
Sequence similarities
Belongs to the peptidase S1 family.
Post-translational modifications
The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.. N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans.. Proteolytically cleaved and activated by cathepsin CTSG (PubMed:8920993). The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway) (By similarity).. The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
Target data
Product promise
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