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CS1070

Sigma-Aldrich

Transglutaminase Assay Kit

sufficient for assays in two 96-well plates

Synonym(s):

TGases Assay Kit

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About This Item

UNSPSC Code:
12161503
NACRES:
NA.28

Quality Level

shipped in

dry ice

storage temp.

−20°C

Related Categories

General description

The Transglutaminase Assay Kit is designed for the detection of transglutaminase activity in biological samples. The kit can also be used for screening of transglutaminase inhibitors/activators.

Application

The assay is based on transglutaminase catalysis of a covalent bond formation between the free amine group of Poly L-Lysine, which is covalently attached to the plate surface, and the γ-carboxamide group of biotin-TVQQEL-OH substrate present in the assay buffer. This reaction immobilizes biotin to the plate surface. The amount of immobilized biotin is proportional to the amount of active transglutaminase in the sample. The amount of immobilized biotin is determined using streptavidin-peroxidase and TMB substrate.

Biochem/physiol Actions

Transglutaminases (TGases) are a widely distributed and unique group of calcium dependent enzymes that catalyze the post-translational modification of proteins by the formation of isopeptide bonds. This occurs either through protein cross-linking via formation of γ-glutamyl-ε-lysine bonds or through incorporation of primary amines at selected peptide-bound glutamine residues. The cross-linked products, often of high molecular mass, are highly resistant to mechanical challenge and proteolytic degradation, and their accumulation is found in a number of tissues and processes, where such properties are important including skin, hair, blood clotting, and wound healing. Deregulation of the enzyme activity contributes to a number of human diseases.

Other Notes

The detection limit is 0.003 mU/assay or 0.03mU/ml of Transglutaminase.

Kit Components Also Available Separately

Product No.
Description
SDS

  • T5398Transglutaminase from guinea pig liver, lyophilized powder, ≥1.5 units/mg protein 2 eaSDS

  • T04403,3′,5,5′-Tetramethylbenzidine (TMB) Liquid Substrate System for ELISA, peroxidase substrateSDS

  • S5512Streptavidin−Peroxidase from Streptomyces avidinii, lyophilized powder 100 μgSDS

Pictograms

Health hazardCorrosion

Signal Word

Danger

Hazard Statements

Hazard Classifications

Aquatic Chronic 3 - Eye Dam. 1 - Met. Corr. 1 - Resp. Sens. 1 - Skin Irrit. 2

Storage Class Code

8A - Combustible corrosive hazardous materials


Certificates of Analysis (COA)

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Transglutaminases and their substrates.
Francesco Facchiano et al.
Progress in experimental tumor research, 38, 37-57 (2005-03-05)
G Korner et al.
The Biochemical journal, 262(2), 633-641 (1989-09-01)
Bovine aortic endothelial cells contain Ca2+-dependent tissue-type transglutaminase. Its activity in these cells was high, with apparent Km and Vmax. values with respect to putrescine of 0.203 mM and 18.5 nmol/min per mg of protein, and its activity was inhibited
Claudia Damaris Müller et al.
Scientific reports, 12(1), 13326-13326 (2022-08-04)
Transglutaminases (TGs) catalyze the covalent crosslinking of proteins via isopeptide bonds. The most prominent isoform, TG2, is associated with physiological processes such as extracellular matrix (ECM) stabilization and plays a crucial role in the pathogenesis of e.g. fibrotic diseases, cancer
Martin Griffin et al.
The Biochemical journal, 368(Pt 2), 377-396 (2002-10-09)
Transglutaminases (Tgases) are a widely distributed group of enzymes that catalyse the post-translational modification of proteins by the formation of isopeptide bonds. This occurs either through protein cross-linking via epsilon-(gamma-glutamyl)lysine bonds or through incorporation of primary amines at selected peptide-bound
Seong-Gon Kim et al.
Oncology reports, 25(6), 1597-1602 (2011-03-23)
Resistance to chemotherapy is very important in the prognosis of tumors. Transglutaminase-2 (TG-2) mediated chemotherapy resistance has been widely reported. The objective of this study was to demonstrate the effect of 4-hexylresorcinol (4-HR) on TG-2 activity in nasopharyngeal squamous cell

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