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T5398 Sigma

Transglutaminase from guinea pig liver

lyophilized powder, ≥1.5 units/mg protein

Synonym: Protein-glutamine:amine γ-glutamyltransferase, Protein-Glutamine-γ-Glutamyltransferase

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Properties

Related Categories 2.3.x.x Acyltransferases, 2.x.x.x Transferases, Application Index, Biochemicals and Reagents, Cell Biology,
form   lyophilized powder
composition   Protein, ≥80% modified Warburg-Christian
solubility   H2O: soluble1.0 mg/mL, clear
Featured Industry   Diagnostic Assay Manufacturing
shipped in   dry ice
storage temp.   −20°C

Description

Unit Definition

One unit will catalyze the formation of 1.0 μmole of hydroxamate per min from Nα-Z-Gln-Gly and hydroxylamine at pH 6.0 at 37 °C. (L-Glutamic acid γ-monohydroxamate is the standard.)

Physical form

Lyophilized powder containing Tris and dithioerythritol

Application

This product from Sigma has been used to demonstrate that tissue transglutaminase (tTG) selectively deamidates gluten peptides, which results in strongly enhanced T cell-stimulatory activity. It has also been used to assess immune responses to A-gliadin peptides. Furthermore, it has been used to demonstrate that tTG selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease.

Transglutaminase has been used in a study to improve quantifiable assays to fully characterize the role of transglutaminase in diseases such as Huntington′s disease and Alzheimer′s disease.Transglutaminase has also been used in a study to develop a nonradioactive dot blot assay for transglutaminase activity.

Biochem/physiol Actions

Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not glycosylated. The molecular mass is approximately 76.6 kDa. It is calcium dependent and has several calcium binding sites. The enzyme is inhibited by iodoacetamide and N-ethylmaleimide in the presence of calcium. It catalyzes the incorporation of small molecular weight amines into γ-glutamine sites of proteins. In the absence of small molecular weight amines, it catalyzes the cross linking of proteins that results in the formation of γ-glutamyl-ε-lysine side chain peptides. Liver transglutaminase is a nonzymogenic enzyme.

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Safety & Documentation

Safety Information

RIDADR 
NONH for all modes of transport
WGK Germany 
1
RTECS 
MA2370000
Protocols & Articles

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

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92210 Timestrip Plus 0 °C
06693 Timestrip Plus -20 °C

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