Natural Dog Fibrinogen protein (FITC) (ab92970)



  • NatureNatural
  • SourceNative
  • Amino Acid Sequence
    • SpeciesDog
    • Additional sequence informationSource = US origin dog plasma
  • ConjugationFITC. Ex: 493nm, Em: 528nm


Our Abpromise guarantee covers the use of ab92970 in the following tested applications.

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

  • Applications


  • Purity> 95 % SDS-PAGE.
    Purified using several chromatographic steps. Plasminogen depleted by lysine affinity chromatography.
  • FormLiquid
  • Additional notesThaw at 37oC without agitation until completely liquid, then gently mix before use. Keep fibrinogen at 25-37oC, aliquot and flash freeze unused portion. Protect from light.
  • 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 Sodium citrate-HCl, pH 7.4

General Info

  • Alternative names
    • FGA
    • Fib2
    • Fibrinogen A alpha polypeptide
    • Fibrinogen alpha chain
    • Fibrinogen B alpha polypeptide
    • Fibrinogen beta chain
    • Fibrinogen G alpha polypeptide
    • Fibrinogen gamma chain
    • fibrinogen, B beta polypeptide
    • fibrinogen, G gamma polypeptide
    • fibrinogen, gamma polypeptide
    • Fibrinogen--alpha -polypeptide chain
    • Fibrinogen--beta -polypeptide chain
    • Fibrinogen--gamma-polypeptide chain
    see all
  • FunctionFibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
  • Tissue specificityPlasma.
  • Involvement in diseaseDefects in FGA are a cause of congenital afibrinogenemia (CAFBN) [MIM:202400]. This is a rare autosomal recessive disorder characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. Note=The majority of cases of afibrinogenemia are due to truncating mutations. Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias.
    Defects in FGA are a cause of amyloidosis type 8 (AMYL8) [MIM:105200]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.
  • Sequence similaritiesContains 1 fibrinogen C-terminal domain.
  • DomainA long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.
  • Post-translational
    The alpha chain is not glycosylated.
    Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.
    About one-third of the alpha chains in the molecules in blood were found to be phosphorylated.
    Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.
    Phosphorylation sites are present in the extracellular medium.
  • Cellular localizationSecreted.
  • Information by UniProt

References for Natural Dog Fibrinogen protein (FITC) (ab92970)

ab92970 has not yet been referenced specifically in any publications.

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