Natural Human Factor IXa protein (ab185253)

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Overview

Description

  • Nature
    Native
  • Source
    Native
  • Amino Acid Sequence
    • Accession
      P00740
    • 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.

Publishing research using ab185253? Please let us know so that we can cite the reference in this datasheet.

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