Natural Human Factor IXa protein (ab185253)

Overview

Description

  • Nature
    Native
  • Source
    Native
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Sequence
      MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSG KLEEFVQGNLERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESN PCLNGGSCKDDINSYECWCPFGFEGKNCELDVTCNIKNGRCEQFCKNSAD NKVVCSCTEGYRLAENQKSCEPAVPFPCGRVSVSQTSKLTRAETVFPDVD YVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPWQVVLNGKVDA FCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRII PHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGS GYVSGWGRVFHKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFH EGGRDSCQGDSGGPHVTEVEGTSFLTGIISWGEECAMKGKYGIYTKVSRY VNWIKEKTKLT
    • Molecular weight
      42 kDa
    • Amino acids
      1 to 461

Specifications

Our Abpromise guarantee covers the use of ab185253 in the following tested applications.

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

  • Applications

    SDS-PAGE

  • Purity
    >95% by SDS-PAGE .
    ab185253 purity is determined by SDS-PAGE and shows total reduction upon incubation with 2-mercaptoethanol.
  • Form
    Liquid
  • Additional notes

    ab185253 is prepared from Human Factor IX by activation with Bovine Factor XIa. This Bovine Factor XIa is removed after activation. Complete activation is observed by SDS-PAGE. The Factor XIa activates Factor IX in a two-step reaction. In the first step, an internal Arg-Ala bond is cleaved, and in the second step, an Arg-Val bond is cleaved. The second cleavage leads to the liberation of an activation peptide from the NH2-terminal portion of the heavy chain to produce Factor IXa-beta. Factor IXa-alpha has only the second cleavage at the Arg-Val bond with about half the coagulant activity of Human Factor IXa-beta. Complete activation is observed by SDS-PAGE.  Factor IXa-alpha has only the second cleavage at the Arg-Val bond with about half the coagulant activity of Human Factor IXa beta.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

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

    pH: 7.40
    Constituents: 0.32% Tris HCl, 0.58% Sodium chloride

    Thaw rapidly in a 37°C water bath without allowing protein to warm to 37°C and immediately cool on ice.

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

ab185253 has not yet been referenced specifically in any publications.

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