Natural Human Factor VIIa protein (ab62387)

Overview

Description

  • Nature
    Native
  • Source
    Native
  • Amino Acid Sequence
    • Species
      Human

Specifications

Our Abpromise guarantee covers the use of ab62387 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Functional Studies

    SDS-PAGE

  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot. Store at -80°C. Avoid freeze / thaw cycle.

    Preservative: None
    Constituents: 50% Glycerol

General Info

  • Alternative names
    • Coagulation factor VII
    • Eptacog alfa
    • F7
    • FA7_HUMAN
    • Factor VII heavy chain
    • FVII coagulation protein
    • Proconvertin
    • Serum prothrombin conversion accelerator
    • SPCA
    see all
  • Function
    Initiates 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.
  • Tissue specificity
    Plasma.
  • Involvement in disease
    Defects 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 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
    modifications
    The 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.
  • Cellular localization
    Secreted.
  • Information by UniProt

References

ab62387 has not yet been referenced specifically in any publications.

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