Fibrinogen alpha chain; Fibrinopeptide A; Fibrinogen alpha chain; FGA

For Research Use Only. Not for use in diagnostic procedures.

Monoclonal

IgM

471CT12.1.2

Mouse

This FGA antibody is generated from mice immunized with a KLH conjugated synthetic peptide between 116-144 amino acids from the N-terminal region of human FGA.

Mouse monoclonal antibody supplied in crude ascites with 0.09% (W/V) sodium azide.

Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C in small aliquots to prevent freeze-thaw cycles.

Small volumes of anti-FGA antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

The protein encoded by this gene is the alpha component of
fibrinogen, a blood-borne glycoprotein comprised of three pairs of
nonidentical polypeptide chains. Following vascular injury,
fibrinogen is cleaved by thrombin to form fibrin which is the most
abundant component of blood clots. In addition, various cleavage
products of fibrinogen and fibrin regulate cell adhesion and
spreading, display vasoconstrictor and chemotactic activities, and
are mitogens for several cell types. Mutations in this gene lead to
several disorders, including dysfibrinogenemia, hypofibrinogenemia,
afibrinogenemia and renal amyloidosis. Alternative splicing results
in two isoforms which vary in the carboxy-terminus. [provided by
RefSeq].

Cardiovascular; Metabolism

Western Blot (WB), ELISA (EIA)

WB~~1:500~2000

FGA Antibody (N-term) western blot analysis in mouse bladder tissue lysates (35ug/lane).This demonstrates the FGA antibody detected the FGA protein (arrow).

94973

fibrinogen alpha chain

fibrinogen alpha chain

Fibrinogen alpha chain

FIBA_HUMAN

The protein encoded by this gene is the alpha component of fibrinogen, a blood-borne glycoprotein comprised of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia, afibrinogenemia and renal amyloidosis. Alternative splicing results in two isoforms which vary in the carboxy-terminus. [provided by RefSeq, Jul 2008]

FGA: Fibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation. Defects in FGA are a cause of congenital afibrinogenemia (CAFBN). This is a rare autosomal recessive disorder characterized by bleeding that varies from mild to severe and by complete absence or extremely low levels of plasma and platelet fibrinogen. The majority of cases of afibrinogenemia are due to truncating mutations. Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha- dysfibrinogenemias. Defects in FGA are a cause of amyloidosis type 8 (AMYL8); also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Secreted, signal peptide; Secreted

Chromosomal Location of Human Ortholog: 4q28

Cellular Component: extracellular space; cell surface; fibrinogen complex; plasma membrane; extracellular region; cell cortex; vesicle; external side of plasma membrane

Molecular Function: protein binding, bridging; protein binding; cell adhesion molecule binding; structural molecule activity; receptor binding

Biological Process: protein polymerization; platelet activation; extracellular matrix organization and biogenesis; platelet degranulation; positive regulation of heterotypic cell-cell adhesion; cellular protein complex assembly; positive regulation of protein secretion; cell-matrix adhesion; positive regulation of vasoconstriction; innate immune response; blood coagulation; signal transduction; response to calcium ion; positive regulation of exocytosis

Disease: Amyloidosis, Familial Visceral; Afibrinogenemia, Congenital; Dysfibrinogenemia, Congenital

Bahadori, B., et al. Thromb. Res. 126(4):350-352(2010)
Chen, Z., et al. Hum. Genet. 128(4):443-452(2010)
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Gu, W.P., et al. Zhonghua Yi Xue Yi Chuan Xue Za Zhi 27(3):286-289(2010)
Ban, H.J., et al. BMC Genet. 11, 26 (2010) :

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