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Fibrinogen Protein | FGG protein

Fibrinogen, Mouse (Coagulation Factor I)

Purity
Purified
Purified by SPE extraction with immunoaffinity resins.
Synonyms
Fibrinogen; Mouse (Coagulation Factor I); FGG protein
Ordering
For Research Use Only!
Host
Mouse Fibrinogen, from plasma.
Purity/Purification
Purified
Purified by SPE extraction with immunoaffinity resins.
Form/Format
Supplied as a liquid in 0.2M sodium citrate HCl, pH 7.4.
Preparation and Storage
For long-term storage, aliquot to avoid repeated freezing and thawing and freeze at -70 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Aliquots are stable for at least 6 months.
Related Product Information for FGG protein
The thrombin (IIa) catalyzed cleavage of soluble fibrinogen (Fbg) to form fibrin (Fbn) is the terminal proteolytic event in the coagulation cascade. These soluble Fbn monomers spontaneously polymerize to form an insoluble Fbn network which is stabilized by the factor XIIIa catalyzed crosslinking of lys and glu residues of a and g chains. This Fbn network is the major protein component of the hemostatic plug.

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.
Product Categories/Family for FGG protein

NCBI and Uniprot Product Information

NCBI GI #
350
NCBI GeneID
UniProt Accession #
Molecular Weight
~330kD
NCBI Official Full Name
fibrinogen
NCBI Official Synonym Full Names
fibrinogen gamma chain<
NCBI Official Symbol
FGG
NCBI Protein Information
fibrinogen gamma-B chain; gamma'; fibrinogen, gamma polypeptide
UniProt Protein Name
Fibrinogen gamma-B chain
Protein Family
UniProt Gene Name
FGG
UniProt Synonym Gene Names
Gamma'
UniProt Entry Name
FIBG_BOVIN

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

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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