FGA Protein (AA 37-258) (His tag)
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- Target See all FGA Proteins
- FGA (Fibrinogen alpha Chain (FGA))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 37-258
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Origin
- Rat
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Source
- Escherichia coli (E. coli)
- Purification tag / Conjugate
- This FGA protein is labelled with His tag.
- Sequence
- Gly 37-Met 258
- Characteristics
- A DNA sequence encoding the Rat FGA protein (P06399) (Gly 37-Met 258) was expressed with N-His tag.
- Purity
- > 95 % as determined by reducing SDS-PAGE.
- Top Product
- Discover our top product FGA Protein
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Fibrinogen alpha Chain (FGA) (AA 1-218) protein (GST tag)
FGA Origin: Human Host: Wheat germ Recombinant WB, ELISA, AA, AP
Fibrinogen alpha Chain (FGA) (AA 36-218) protein (His tag)FGA Origin: Human Host: Escherichia coli (E. coli) Recombinant > 90 % SDS
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- Restrictions
- For Research Use only
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- Format
- Lyophilized
- Buffer
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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
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- Target
- FGA (Fibrinogen alpha Chain (FGA))
- Alternative Name
- FGA (FGA Products)
- Background
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Abbreviation: FGA
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.
- Molecular Weight
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Calculated MW: 24.31 kDa
Observed MW: 30 kDa
- UniProt
- P06399
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