Fibrinogen alpha chain Rabbit mAb

Human,Mouse,Rat

WB,IHC,IF,ELISA

单克隆抗体

FGA

Fibrinogen alpha chain [Cleaved into: Fibrinopeptide A; Fibrinogen alpha chain]

95kD

Endogenous

PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA

Monoclonal, Rabbit,IgG

IHC 1:500-1:2000; WB 1:2000-1:10000; IF 1:200-1:1000; ELISA 1:5000-1:20000; Note: For IHC, we suggest antigen retrieval with TE buffer pH 9.0

Protein A

1 mg/ml

-15°C to -25°C/1 year(Do not lower than -25°C)

This gene encodes the alpha subunit of the coagulation factor fibrinogen, which is a component of the blood clot. Following vascular injury, the encoded preproprotein is proteolytically processed by thrombin during the conversion of fibrinogen to fibrin. Mutations in this gene lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia, afibrinogenemia and renal amyloidosis. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that undergoes proteolytic processing. [provided by RefSeq, Jan 2016],

Disease:Defects in FGA are a cause of amyloidois type 8 (AMYL8) [MIM:105200]; 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.,Disease:Defects in FGA are a cause of congenital afibrinogenemia [MIM:202400]. 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.,Disease:Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias.,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.,Function:Fibrinogen has a double Function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.,online information:Fibrinogen entry,online information:The Singapore human mutation and polymorphism database,PTM:About one-third of the alpha chains in the molecules in blood were found to be phosphorylated.,PTM: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.,PTM:Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.,PTM:The alpha chain is not glycosylated.,similarity:Contains 1 fibrinogen C-terminal domain.,subunit: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.,