Description

  • Product name

    Native cow Fibrinogen protein
    See all Fibrinogen proteins and peptides
  • Biological activity

    Specific activity: 100% Clottable
  • Purity

    > 95 % SDS-PAGE.
    Prepared from fresh bovine plasma using several chromatographic steps. Plasminogen depleted by lysine affinity chromatography.
  • Expression system

    Native
  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Native
    • Species

      Cow
    • Additional sequence information

      Source = bovine plasma

Specifications

Our Abpromise guarantee covers the use of ab92827 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

    Functional Studies

  • Form

    Liquid
  • Additional notes

    Thaw at 37°C without agitation until completely liquid, then gently mix before use. Keep fibrinogen at 25-37°C, aliquot and flash freeze unused portion.
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

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

    pH: 7.40
    Constituent: 0.588% Sodium citrate

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

General Info

  • Alternative names

    • FGA
    • FGB
    • FGG
    • Fib2
    • FIBA_HUMAN
    • 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
  • Function

    Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
  • Tissue specificity

    Plasma.
  • Involvement in disease

    Defects 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 similarities

    Contains 1 fibrinogen C-terminal domain.
  • Domain

    A 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 extracellular medium.
  • Cellular localization

    Secreted.
  • Information by UniProt

References

ab92827 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

1-2 of 2 Abreviews or Q&A

Answer

Thank you for your reply. As these are purified native proteins, it is highly likely that they will be glycosylated. Please be aware that the proteins recommended are derived from different species: ab62394 Human ab92791 Mouse ab92827 Bovine ab92828 Pig ab93072 Rat Please do not hesitate to contact me should you have further questions.

Read More

Please note: All products are "FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC PROCEDURES"
For licensing inquiries, please contact partnerships@abcam.com

Sign up