Overview

Description

  • Nature
    Native
  • Source
    Native
  • Amino Acid Sequence
    • Species
      Human
    • Amino acids
      47 to 461

Specifications

Our Abpromise guarantee covers the use of ab81593 in the following tested applications.

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

  • Biological activity
    <1% Factor IXa activity. Assay is performed to determine percent contaminating IXa activity. IXa activity is based on a IXa standard curve. Chromagenic assay uses Spectrozyme-IXa (American Diagnostica) as substrate. Active site blocked by EGR.
  • Applications

    SDS-PAGE

    Functional Studies

  • Purity
    > 95 % SDS-PAGE.

  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: 20mM HEPES, 150mM Sodium chloride, pH 7.4

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

General Info

  • Alternative names
    • Christmas factor
    • Coagulant factor IX
    • Coagulation factor IX
    • Coagulation factor IXa heavy chain
    • F9
    • F9 DEFICIENCY
    • FA9_HUMAN
    • Factor 9
    • Factor IX
    • FIX
    • Plasma thromboplastin component
    • PLASMA THROMBOPLASTIN COMPONENT DEFICIENCY
    • PTC
    see all
  • Function
    Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa.
  • Tissue specificity
    Synthesized primarily in the liver and secreted in plasma.
  • Involvement in disease
    Defects in F9 are the cause of recessive X-linked hemophilia B (HEMB) [MIM:306900]; also known as Christmas disease.
    Note=Mutations in position 43 (Oxford-3, San Dimas) and 46 (Cambridge) prevents cleavage of the propeptide, mutation in position 93 (Alabama) probably fails to bind to cell membranes, mutation in position 191 (Chapel-Hill) or in position 226 (Nagoya OR Hilo) prevent cleavage of the activation peptide.
    Defects in F9 are the cause of thrombophilia due to factor IX defect (THR-FIX) [MIM:300807]. A hemostatic disorder characterized by a tendency to thrombosis.
  • 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.
  • Domain
    Calcium binds to the gamma-carboxyglutamic acid (Gla) residues and, with stronger affinity, to another site, beyond the Gla domain.
  • Post-translational
    modifications
    Activated by factor XIa, which excises the activation peptide.
    The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.
  • Cellular localization
    Secreted.
  • Information by UniProt

References

This product has been referenced in:
  • Fischer M  et al. Novel in vitro inhibitory functions of potato tuber proteinaceous inhibitors. Mol Genet Genomics 290:387-98 (2015). Read more (PubMed: 25260821) »

See 1 Publication for this product

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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