Fibrinogen Protein | FGG protein
Fibrinogen, Mouse (Coagulation Factor I)
Purified by SPE extraction with immunoaffinity resins.
Purified by SPE extraction with immunoaffinity resins.
Plasma fibrinogen is large glycoprotein (40kD) synthesized in the liver and circulating at a concentration of 2.6mg/ml. It is a disulfide linked dimer composed of 3 pairs of disulfide linked non-identical polypeptide chains (Aa, Bb and g). Notable features of the Aa chain are the N-terminal peptide (fibrinopeptide A (FPA, 1-16)), factor XIIIa crosslinking sites and 2 phosphorylation sites. When synthesized, Fbg is fully phosphorylated, but circulates at only 20-30% phosphorylation. The Bb chain contains fibrinopeptide B (FPB, 1-14), one of the 3 N-linked carbohydrate moieties (Mr%00) and an N-terminal pyroglutamic acid. The g chain contains the other N-linked glycosylation site and a factor XIIIa crosslinking sites. The 2 elongated subunits ((AaBbg)2) are aligned in an antiparallel manner forming a trinodular arrangement of the six chains. The nodes are formed by disulfide rings between the 3 parallel chains. The central node (n-disulfide knot, E domain) is formed by the N-termini of all six chains held together by 11 disulfide bonds. This region contains the 2 IIa-sensitive sites. The release of FPA by cleavage at R16-G17 generates Fbn I, exposing a polymerization site (17-20) on the Aa chain. These regions bind to complimentary regions on the D domain of Fbn to form protofibrils. Subsequent IIa cleavage of FPB (R14-G15) from the Bb chain exposes additional polymerization sites and promotes lateral growth of the Fbn network.
NCBI and Uniprot Product Information
Uniprot Description
Function: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
Subunit structure: Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain
By similarity.
Subcellular location: Secreted.
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 modification: 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.
Sequence similarities: Contains 1 fibrinogen C-terminal domain.
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Product Notes
The FGG fgg (Catalog #AAA635241) is a Protein produced from Mouse Fibrinogen, from plasma. and is intended for research purposes only. The product is available for immediate purchase. It is sometimes possible for the material contained within the vial of "Fibrinogen, Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
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