The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Use at an assay dependent dilution. Predicted molecular weight: 95 kDa.
Use at an assay dependent dilution.
Use a concentration of 2.5 µg/ml. Perform heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.
Use at an assay dependent dilution.
Use at an assay dependent concentration.
FunctionFibrinogen has a double function: yielding monomers that polymerize into fibrin and acting as a cofactor in platelet aggregation.
Involvement in diseaseDefects in FGA are a cause of congenital afibrinogenemia (CAFBN) [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. Note=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) [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.
DomainA 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 modificationsThe alpha chain is not glycosylated. Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers. About one-third of the alpha chains in the molecules in blood were found to be phosphorylated. 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. Phosphorylation sites are present in the extracellular medium.
ab118488 at 2.5µg/ml staining Fibrinogen in Formalin-fixed, Paraffin-embedded Human kidney tissue by Immunohistochemistry, followed by biotinylated secondary antibody, alkaline phosphatase-streptavidin and chromogen.
ab118488 at 2.5µg/ml staining Fibrinogen in Formalin-fixed, Paraffin-embedded Human liver tissue by Immunohistochemistry, followed by biotinylated secondary antibody, alkaline phosphatase-streptavidin and chromogen.
References for Anti-Fibrinogen antibody (ab118488)
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