FGA Protein (AA 434-789) (His tag)

Catalog No. ABIN7505430

Product Details

Target: FGA (Fibrinogen alpha Chain (FGA))

Protein Type: Recombinant

Protein Characteristics: AA 434-789

Origin: Mouse

Source: Escherichia coli (E. coli)

Purification tag / Conjugate: This FGA protein is labelled with His tag.

Sequence: Asp 434-Gln 789

Characteristics: A DNA sequence encoding the Mouse FGA protein (E9PV24 ) (Asp 434-Gln 789) was expressed with N-His tag.

Purity: > 95 % as determined by reducing SDS-PAGE.

Application Details

Restrictions: For Research Use only

Handling

Format: Lyophilized

Buffer: Lyophilized from sterile PBS, pH 7.4.
Normally 5 % - 8 % trehalose, mannitol and 0.01 % Tween80 are added as protectants before lyophilization.

Storage: 4 °C,-20 °C,-80 °C

Storage Comment: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

Expiry Date: 12 months

Target Details

Target: FGA (Fibrinogen alpha Chain (FGA))

Alternative Name: FGA (FGA Products)

Background:

Abbreviation: FGA,Fibrinogen A

Target Synonym: FGA,Fib2,Fibrinogen A,Fibrinogen alpha chain,Fibrinogen Type I,fibrinogen,A alpha polypeptide,FPA

Background: Fibrinogen is a 340 kDa, secreted glycoprotein complex that is found in blood at concentrations of 150-400 mg/dL. It is secreted primarily by hepatocytes, but is also reported to be expressed by fibroblasts, type I alveolar epithelium, intestinal epithelium and some tumor cells. Fibrinogen is a homodimer that is composed of two, three-polypeptide chain subunits. Fibrinogen plays a central role in clot formation. 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. Fibrinogen is also a component of the ECM and binds to cell surface molecules on inflammatory cells. Mature mouse alpha, beta and gamma -chains share 67 % , 85 % and 83 % aa identity with human alpha, beta and gamma -chains, respectively.

Molecular Weight:

Calculated MW: 39.05 kDa

Observed MW: 50 kDa

UniProt: E9PV24