F13A1
F13A1 (coagulation factor XIII A chain, also known as F13A) encodes the catalytic A subunit of factor XIII, a transglutaminase that stabilises the fibrin clot. It is the last zymogen to be activated in the blood coagulation cascade. Browse Assay Genie's current range of F13A1 research reagents below, or read on for the biology behind the target.
The F13A1 gene encodes the A subunit of coagulation factor XIII. Factor XIII is activated by thrombin and calcium ions to become a transglutaminase, factor XIIIa, which catalyses the formation of gamma-glutamyl-epsilon-lysine cross-links between fibrin chains and so stabilises the fibrin clot. The active enzyme also cross-links alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.
Plasma factor XIII is a heterotetramer of two A subunits and two B subunits. The A subunits carry the catalytic function, whereas the B subunits have no enzymatic activity and may act as plasma carrier molecules. Platelet factor XIII is made up of two A subunits only, identical to those of plasma origin. When thrombin cleaves the activation peptide in the presence of calcium, plasma factor XIII releases its B subunits and yields the same active enzyme as the platelet form. The F13A1 protein is found in the cytoplasm and is also secreted, and it belongs to the transglutaminase family.
HGNC places F13A1 in the groups of transglutaminases, coagulation factors and microRNA protein coding host genes. The gene was formerly named coagulation factor XIII, A1 polypeptide, with the earlier symbol F13A. Factor XIII deficiency is classed as type I, with loss of both A and B subunits, or type II, with loss of the A subunit alone. These defects can cause a lifelong bleeding tendency, defective wound healing and habitual abortion, which makes F13A1 a frequent subject in haemostasis research. Mouse and rat both carry an F13a1 ortholog.
F13A1 encodes the catalytic subunit of the last zymogen activated in the cascade, making it central to studies of how clots are finalised.
Factor XIIIa forms gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, a defining mechanism for work on clot structure and stability.
As a calcium- and thrombin-activated member of the transglutaminase family, F13A1 is a model for zymogen activation and cross-linking catalysis.
Loss of the A subunit causes type II deficiency, linked to bleeding tendency, defective wound healing and habitual abortion.
F13A1 encodes the catalytic A subunit of factor XIII. After activation by thrombin and calcium, the enzyme forms gamma-glutamyl-epsilon-lysine cross-links between fibrin chains, stabilising the clot. It also cross-links alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin.
The HGNC symbol is F13A1, with F13A as a previous symbol. The earlier gene name was coagulation factor XIII, A1 polypeptide. The activated enzyme is called factor XIIIa, and the protein is classed as a transglutaminase with EC number 2.3.2.13.
Mouse and rat each have an F13a1 ortholog. Deficiency of the A subunit alone is termed type II factor XIII deficiency, and defects can cause lifelong bleeding tendency, defective wound healing and habitual abortion. Check the datasheet of any product for its validated reactivity.
Other coagulation factors, fibrin-related proteins and transglutaminases with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P00488; product specifications from Assay Genie datasheets.