Recombinant Human Factor X protein (ab158407)
Key features and details
- Expression system: Wheat germ
- Tags: GST tag N-Terminus
- Suitable for: WB, ELISA
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Product name
Recombinant Human Factor X protein
See all Factor X proteins and peptides -
Expression system
Wheat germ -
Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
-
Species
Human -
Sequence
NNILARVTRANSFLEEMKKGHLERECMEETCSYEEAREVFEDSDKTNEFW NKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSL DNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERRK RSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNN LTRIVGGQECKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQA KRFKVRVGDRNTEQEEGGEAVHEVEVVIKHNRFTKETYDFDIAVLRLKTP ITFRMNVAPACLPERDWAESTLMTQKTGIVSGFGRTHEKGRQSTRLKMLE VPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSGGPHVTRFKDTY FVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPEV ITSSPLK -
Amino acids
32 to 488 -
Tags
GST tag N-Terminus
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Preparation and Storage
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Alternative names
- Activated factor Xa heavy chain
- Coagulation factor X
- F10
see all -
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. -
Tissue specificity
Plasma; synthesized in the liver. -
Involvement in disease
Defects in F10 are the cause of factor X deficiency (FA10D) [MIM:227600]. A hemorrhagic disease with variable presentation. Affected individuals can manifest prolonged nasal and mucosal hemorrhage, menorrhagia, hematuria, and occasionally hemarthrosis. Some patients do not have clinical bleeding diathesis. -
Sequence similarities
Belongs to the peptidase S1 family.
Contains 2 EGF-like domains.
Contains 1 Gla (gamma-carboxy-glutamate) domain.
Contains 1 peptidase S1 domain. -
Post-translational
modificationsThe vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
N- and O-glycosylated.
The activation peptide is cleaved by factor IXa (in the intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. -
Cellular localization
Secreted. - Information by UniProt