Product nameNative human Factor VIIa protein
See all Factor VIIa proteins and peptides
Protein lengthFull length protein
Amino Acid Sequence
Molecular weight50 kDa
Additional sequence informationPrepared from purified Human Factor VII using Human Factor XIIa from human plasma.
Our Abpromise guarantee covers the use of ab184890 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Activity is determined via clotting assay. Factor Vlla, in the presence of calcium ions and Tissue factor, activates Factors IX and X to their enzymatically active forms, Factor IXa and Xa.
Purity> 95 % SDS-PAGE.
The Factor Xlla is removed using affinity chromatography.
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Preparation and Storage
Stability and Storage
Shipped on Dry Ice. Store at -80°C.
Constituents: 0.32% Tris HCl, 0.58% Sodium chloride
This product is an active protein and may elicit a biological response in vivo, handle with caution.
- Coagulation factor VII
- Eptacog alfa
FunctionInitiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium.
Involvement in diseaseDefects in F7 are the cause of factor VII deficiency (FA7D) [MIM:227500]. A hemorrhagic disease with variable presentation. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Finally, numerous subjects are completely asymptomatic despite very low factor VII levels.
Sequence similaritiesBelongs to the peptidase S1 family.
Contains 2 EGF-like domains.
Contains 1 Gla (gamma-carboxy-glutamate) domain.
Contains 1 peptidase S1 domain.
modificationsThe vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
O- and N-glycosylated. N-glycosylation at Asn-205 occurs cotranslationally and is mediated by STT3A-containing complexes, while glycosylation at Asn-382 is post-translational and is mediated STT3B-containing complexes before folding. O-fucosylated by POFUT1 on a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines.
- Information by UniProt
ab184890 has not yet been referenced specifically in any publications.