Description
Factor XIII Polyclonal Antibody – HRP Conjugated
Affinity’s Factor XIII Polyclonal Antibody – HRP Conjugated is the base level of our horseradish peroxidase conjugated Factor XIII antibodies. The purity of IgG is typically 90% and is provided in a solution of HEPES buffered saline containing 50% glycerol (v/v). The titre is essentially the same as the starting antiserum and each vial typically contains the amount of IgG recovered from one milliliter of antiserum however this IgG has been conjugated with Horseradish Peroxidase as an enzyme reporter. This Factor XIII Polyclonal Antibody – HRP Conjugated is generally intended for use as labeled primary antibodies in applications such as immunoassay and immunoblotting.
Product Code: SAFXIII-HRP
Retail Product Size: 0.2mg vial
Host Animal: Sheep Anti-Human Factor XIII Polyclonal Antibody – HRP Conjugated
Species Cross Reactivity: View Chart
Product Datasheet: Factor XIII F13 Polyclonal Antibody, hrp conjugated anti-human sheep IgG
Description of Factor XIII (FXIII)
Factor XIII (FXIII, fibrin stabilizing factor) is the proenzyme form of a transamidase that is essential for normal haemostasis and fibrinolysis, wound healing, female fertility and foetal development. Extracellular F.XIII consists of A subunits (83 kDa each) which contain the enzyme moiety, and B subunits (76 kDa each) which act as a carrier protein for the A subunit in circulation. Both subunits are produced under separate genetic control. In plasma, FXIII exists as a non-covalent tetrameric complex (320 kDa) of two A-subunits and two B-subunits (A2B2). The concentration of F.XIII tetramer in plasma is ~25 μg/ml (~80 nM). An intracellular form of FXIII is found in platelets, megakaryocytes and monocytes. This form of F.XIII presents as a dimer of two A-subunits only and has a molecular weight of 160 kDa. The importance of these intracellular stores is demonstrated by the observation that platelets can contribute up to half of the FXIII activity in platelet rich plasma. The activation of FXIII involves several steps. Thrombin cleaves after Arg37 of each A-subunit in the A2B2 tetramer, releasing a 4.5 kDa activation peptide. Additional conformational changes induced by the binding of calcium, and by dissociation of the B-subunits from the A-subunit dimer are required to obtain full enzyme activity. FXIIIa is a cysteine protease that catalyses the formation of γ-glutamyl-ε-lysyl bonds between the γ and α chains of polymerised fibrin molecules. Other proteins found crosslinked into fibrin clots by FXIIIa include fibrinogen, α2antiplasmin, fibronectin, vitronectin and von Willebrand factor 1-3.
References and Review
- McDonagh J; Structure and Function of Factor XIII; in Hemostasis and Thrombosis, 3rd Edition, eds. RW Colman, J Hirsh, VJ Marder and EW Salzman, pp 301-313, J.B. Lippincott Co., Philadelphia PA, USA, 1994.
- Inbal A, Muszbek L; Coagulation Factor Deficiencies and Pregnancy Loss; Seminars in Thrombosis and Haemostasis 29, pp 171-174, 2003.
- Murdock PJ, Owens DL, Chitolie A, Hutton RA, Lee CA; Development and Evaluation of ELISAs for Factor XIIIA and XIIIB Subunits in Plasma; Thrombosis Research 67, pp 73-79, 1992.
