|Application ||WB, IHC|
|Calculated MW||94973 Da|
|Other Names||Fibrinogen alpha chain, Fibrinopeptide A, Fibrinogen alpha chain, FGA|
|Target/Specificity||A synthetic peptide corresponding to residues in human Fibrinogen alpha chain was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Fibrinogen alpha Antibody chain is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3- dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.|
|Tissue Location||Detected in blood plasma (at protein level).|
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Provided below are standard protocols that you may find useful for product applications.
Fibrinogen is a plasma glycoprotein synthesized primarily in the liver (1). It is comprised of two identical molecular halves, each consisting of three non-identical subunit polypeptides designated as A alpha, B beta- and gamma-chains held together by multiple disulfide bonds (2). Fibrinogen acts as the main factor in the formation of a blood clot by polymerization to a fibrin network and by enabling platelets to aggregate (3). The 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. Defects in fibrinogen are a cause of congenital afibrinogenemia, a rare autosomal recessive disorder, and amyloidosis type 8, also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis (4).
1. Redman CM, et al. Ann N Y Acad Sci. 936:480-95, 2001 2. Matsuda M, et al. Int J Hematol. 76(1):352-60, 2002 3. Fu Y, et al. Biochemistry 31:11968-11972, 1992 4. The UniProt Consortium, The Universal Protein Resource (UniProt). Nucleic Acids Res. 36:D190-195, (2008)
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