Factor XIII, human

For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 6; NC_000006.11 (6144311..6320924, complement). Location: 6p25.3-p24.3

Polyclonal

Sheep

Prior to conjugation, this antibody was specific for Factor XIII as demonstrated by immunoelectrophoresis and ELISA.

Peroxidase conjugated IgG.
Vial containing ml of whole IgG conjugated to horseradish peroxidase (HRP) through carbohydrate groups. Total protein is 0.2 mg.

IgG-HRP conjugate as a clear, slightly red-brown liquid.

IgG-HRP concentration is mg/ml, determined by absorbance using an extinction coefficient (E1%280) of 14. (lot specific)

Store between -10 and -20 degree C. Product will become viscous but will not freeze. Avoid storage in frost-free freezers. Keep vial tightly capped. Allow product to warm to room temperature and gently mix before use. Avoid exposure to sodium azide as this is an inhibitor of peroxidase activity.

Small volumes of anti-F13A1 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Factor XIII (F.XIII, 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, F.XIII 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 ug/ml (~80 nM). An intracellular form of F.XIII 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 F.XIII activity in platelet rich plasma. The activation of F.XIII involves several steps. Thrombin cleaves after Arg37 of each Asubunit 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. F.XIIIa is a cysteine protease that catalyses the formation of gamma-glutamyl-epsilon-lysyl bonds between the gamma and alpha chains of polymerised fibrin molecules. Other proteins found crosslinked into fibrin clots by F.XIIIa include fibrinogen, alpha2antiplasmin, fibronectin, vitronectin and von Willebrand factor 1-3.

Suitable as a source of peroxidase labelled antibodies to Factor XIII.

83,267 Da[Similar Products]

coagulation factor XIII, A1 polypeptide

coagulation factor XIII A chain; TGase; factor XIIIa; fibrinoligase; FSF, A subunit; OTTHUMP00000015990; coagulation factor XIIIa; transglutaminase A chain; transglutaminase. plasma; fibrin stabilizing factor, A subunit; coagulation factor XIII, A polypeptide; protein-glutamine gamma-glutamyltransferase A chain; bA525O21.1 (coagulation factor XIII, A1 polypeptide)

Coagulation factor XIII A chain

F13A??[Similar Products]

F13A_HUMAN

This gene encodes the coagulation factor XIII A subunit. Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as plasma carrier molecules. Platelet factor XIII is comprised only of 2 A subunits, which are identical to those of plasma origin. Upon cleavage of the activation peptide by thrombin and in the presence of calcium ion, the plasma factor XIII dissociates its B subunits and yields the same active enzyme, factor XIIIa, as platelet factor XIII. This enzyme acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot. It also crosslinks alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin. Factor XIII deficiency is classified into two categories: type I deficiency, characterized by the lack of both the A and B subunits; and type II deficiency, characterized by the lack of the A subunit alone. These defects can result in a lifelong bleeding tendency, defective wound healing, and habitual abortion. [provided by RefSeq]

Function: Factor XIII is activated by thrombin and calcium ion to a transglutaminase that catalyzes the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, thus stabilizing the fibrin clot. Also cross-link alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.

Catalytic activity: Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH3.

Cofactor: Binds 1 calcium ion per subunit.

Subunit structure: Tetramer of two A chains and two B chains.

Subcellular location: Cytoplasm. Secreted. Note: Secreted into the blood plasma. Cytoplasmic in most tissues, but also secreted in the blood plasma.

Post-translational modification: The activation peptide is released by thrombin.

Polymorphism: There are four main allelic forms of this protein; F13A*1A, F13A*1B, F13A*2A and F13A*2B. In addition two other intermediate forms (F13A*2A and F13A*2B) seem to exist. The sequence shown is that of F13A*2B.

Involvement in disease: Defects in F13A1 are the cause of factor XIII subunit A deficiency (FA13AD) [

MIM:613225]. FA13AD is an autosomal recessive disorder characterized by a life-long bleeding tendency, impaired wound healing and spontaneous abortion in affected women. Ref.16

Sequence similarities: Belongs to the transglutaminase superfamily. Transglutaminase family.

Sequence caution: The sequence AAA52489.1 differs from that shown. Reason: Erroneous initiation. The sequence BAD92089.1 differs from that shown. Reason: Erroneous initiation.

1. 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.
2. Inbal A, Muszbek L; Coagulation Factor Deficiencies and Pregnancy Loss; Seminars in Thrombosis and Haemostasis 29, pp 171-174, 2003.
3. 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.

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.