Description
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor.
Abbr
TG, Recombinant (Human)
Applications
Recombinant human transglutaminase is a homodimer (a2) composed of two chains held together by non covalent bonds. After activation of the zymogen by Thrombin and Ca2+ to its active form (a*2, Factor XIIIa), Factor XIIIa catalyzes the formation of covalent bridges (ε-(γ-glutamyl) lysine bonds) between fibrin units to increase the elasticity of the clot network. The resulting cross-linked fibrin is insoluble and resistant to lysis.
Form
The transglutaminase is formulated in 10 mM Sodium Phosphate pH 8.0, 15 mM NaCl. Sample contains 50% glycerol. hFXIII is a Ca2+-dependent enzyme.
Enzyme Commission Number
EC 2.3.2.13
Activity
> 750 U/mg [Activity is determined by measuring the rate of fluorescence enhancement after transglutaminase-catalyzed monodansylcadaverine-incorporation into N,N-dimethylated casein according to Lorand et al., Anal. Biochem. 44 (221-231).
Purity
> 95 % (visually by SDS-PAGE)
Unit Definition
1 U is defined as the increase in fluorescence intensity of 1 a.u./min (measured on a Cary eclipse fluorescence spectrophotometer, Varian; λex = 332 nm, λem = 500 nm; band filter = 5 nm; detector strength = 600 V; temperature = 37°C, assay volume = 1 ml)].
Activators
Add Thrombin and 10 mM Ca2+ to activate transglutaminase.
Storage
Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing.
Synonyms
transglutaminase; EC 2.3.2.13; 80146-85-6; transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase; protein-glutamine γ-glutamyltransferase; TG1
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