Anti-Fibrinopeptide A antibody (Biotin) (ab48256)

Overview

  • Product nameAnti-Fibrinopeptide A antibody (Biotin)
    See all Fibrinopeptide A primary antibodies
  • Description
    Rabbit polyclonal to Fibrinopeptide A (Biotin)
  • ConjugationBiotin
  • Tested applicationsSuitable for: IP, RIA, ELISAmore details
  • Species reactivity
    Reacts with: Human
    Predicted to work with: Macaque Monkey
  • Immunogen

    Synthetic peptide:

    ADSGEGDFLAEGGGVR

    conjugated to KLH via carboxyl group, corresponding to amino acids 20-35 of Human Fibrinopeptide A

Properties

  • FormLiquid
  • Storage instructionsShipped at 4°C. Store at +4°C short term (1-2 weeks). Store at -20°C or -80°C. Avoid freeze / thaw cycle.
  • Storage bufferPreservative: 0.01% Thimerosal (merthiolate)
    Constituents: 50% Glycerol, PBS, pH 7.5
  • Concentration information loading...
  • PurityProtein G purified
  • ClonalityPolyclonal
  • IsotypeIgG
  • Research areas

Applications

Our Abpromise guarantee covers the use of ab48256 in the following tested applications.

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

Application Abreviews Notes
IP Use at an assay dependent dilution.
RIA Use at an assay dependent dilution.
ELISA Use at an assay dependent dilution.

Target

  • 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
    modifications
    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 extracelllular medium.
  • Cellular localizationSecreted.
  • Information by UniProt
  • Database links
  • Alternative names
    • A alpha polypeptide antibody
    • FGA antibody
    • Fib2 antibody
    • FIBA_HUMAN antibody
    • Fibrinogen alpha chain antibody
    • Fibrinogen alpha/alpha E chain [Precursor] antibody
    see all

References for Anti-Fibrinopeptide A antibody (Biotin) (ab48256)

ab48256 has not yet been referenced specifically in any publications.

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