Factor XIII Paired Antibody Set
Affinity’s Factor XIII Paired Antibody Set consists of matched capture and detecting antibodies that have been titrated and optimized for use in sandwich style ELISA assays. The product as provided contains sufficient capture and detecting antibodies for five full 96-well microplates and contains a detailed protocol sheet containing directions for use, recipes for solutions and sources for additional materials required. This Factor XIII Paired Antibody Set is intended to facilitate the end user in establishing an “in-house” immunoassay for research purposes only and must not be used for diagnostic applications. Assay validation is the responsibility of the end user.
Product Code: FXIII-EIA
Capture Antibody (FXIII-EIA-C): One yellow-capped vial containing 0.5 ml of polyclonal affinity purified anti-Factor XIII antibody for coating plates.
Detecting Antibody (FXIII-EIA-D): One red-capped tube containing 0.5 ml of peroxidase conjugated affinity-purified polyclonal anti-Factor XIII antibody for detection of captured Factor XIII.
Species Cross Reactivity: View Chart
Product Datasheet: Factor XIII F13 Matched Pair Antibody Set for ELISA
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 fetal 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 Reviews:
- 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.