Recombinant Human Fibrinogen gamma chain protein (ab158441)

Overview

Description

  • Nature
    Recombinant
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      RDNCCILDERFGSYCPTTCGIADFLSTYQTKVDKDLQSLEDILHQVENKT SEVKQLIKAIQLTYNPDESSKPNMIDAATLKSRKMLEEIMKYEASILTHD
    • Amino acids
      31 to 130
    • Tags
      proprietary tag N-Terminus

Associated products

Specifications

Our Abpromise guarantee covers the use of ab158441 in the following tested applications.

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

  • Applications

    ELISA

    Western blot

  • Form
    Liquid
  • Additional notes
    Protein concentration is above or equal to 0.05 mg/ml.
  • 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: 8.00
    Constituents: 0.31% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names
    • FGG
    • FIBG_HUMAN
    • Fibrinogen gamma chain
    • Fibrinogen gamma polypeptide
    • fibrinogen gamma-b chain
    see all
  • Function
    Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
  • Involvement in disease
    Defects in FGG are a cause of thrombophilia.
    Defects in FGG are a cause of congenital afibrinogenemia (CAFBN) [MIM:202400]. It is a rare autosomal recessive disorder characterized by complete absence of detectable fibrinogen.
  • 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
    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.
    Sulfation of C-terminal tyrosines increases affinity for thrombin.
  • Cellular localization
    Secreted.
  • Information by UniProt

Images

  • ab158441 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab158441 has not yet been referenced specifically in any publications.

Customer reviews and Q&As

There are currently no Customer reviews or Questions for ab158441.
Please use the links above to contact us or submit feedback about this product.

Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

Sign up