Native Human Factor XIII protein (Active) is a Human Full Length protein, expressed in Native, with >95% purity and suitable for SDS-PAGE, FuncS.
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
The B chain of factor XIII is not catalytically active, but is thought to stabilize the A subunits and regulate the rate of transglutaminase formation by thrombin.
Coagulation factor XIII B chain, Fibrin-stabilizing factor B subunit, Protein-glutamine gamma-glutamyltransferase B chain, Transglutaminase B chain, F13B
Native Human Factor XIII protein (Active) is a Human Full Length protein, expressed in Native, with >95% purity and suitable for SDS-PAGE, FuncS.
Constituents: 50% Glycerol (glycerin, glycerine), 0.0146% EDTA
Factor XIII is purified by barium citrate, ammonium sulfate and glycine precipitations, ion exchange chromatography and gel filtration. Factor XIII is homogeneous as judged by SDS PAGE.
The B chain of factor XIII is not catalytically active, but is thought to stabilize the A subunits and regulate the rate of transglutaminase formation by thrombin.
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Concentration varies from lot to lot but is between 5-10mg/ml
Factor XIII also known as fibrin-stabilizing factor is an enzyme that plays a role in blood coagulation. It is a zymogen of approximately 320 kDa expressed primarily in the liver megakaryocytes and placenta. In its active form Factor XIII is a heterotetramer composed of two A subunits and two B subunits. The A subunits are the catalytic parts while the B subunits function as carriers. Factor XIII is widely present in plasma and in platelets aiding in clot stabilization.
Factor XIII acts to strengthen and stabilize the fibrin clot by cross-linking fibrin molecules. The enzyme is part of a larger complex known as the blood coagulation pathway. Factor XIII becomes activated by thrombin in the presence of calcium ions. Upon activation it catalyzes the formation of covalent bonds between fibrin molecules enhancing the mechanical strength and resistance of the blood clot. This action prevents premature clot lysis and supports wound healing.
Factor XIII plays a significant role in the coagulation cascade and fibrinolytic system. In the coagulation pathway it functions downstream of fibrin formation providing cross-linking important to clot integrity. Factor XIII is closely associated with proteins such as fibrinogen and thrombin which are key components in the clotting process. Additionally Factor XIII interacts with the fibrinolytic system connecting to proteins like plasmin that are essential for clot breakdown.
Malfunction or deficiency of Factor XIII can lead to bleeding disorders such as Factor XIII deficiency characterized by a tendency to bleed excessively. This deficiency severely impacts the stabilization of clots resulting in poor wound healing. Additionally abnormal Factor XIII activity can contribute to thrombotic disorders where excessive clot stabilization occurs linking Factor XIII to proteins involved in thrombus formation like fibrin and plasminogen. Understanding these interactions is key in managing related conditions.
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