|Other Names||Fibrinogen gamma chain, FGG|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP7325a was selected from the N-term region of human FGG. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. 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 antibacterial immune response via both innate and T-cell mediated pathways.|
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Provided below are standard protocols that you may find useful for product applications.
FGG is the gamma 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 protein lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia and thrombophilia.
Sie,M.P., Isaacs,A. J. Hypertens. 27 (7), 1392-1398 (2009)Nowak-Gottl,U., Weiler,H. Blood (2009) In pressde Willige,S.U., Pyle,M.E. Thromb. Haemost. 101 (6), 1078-1084 (2009)Yoshida,N., Imaoka,S. Thromb. Haemost. 68 (5), 534-538 (1992)
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