Transglutaminase 2

Guinea pig liver transglutaminase

(gpTG2, recombinantly produced in E. coli)
Quantity Unit Price Status
10 U 410 € Available
Documents
Art. No.
T039
Synonym
Tissue-type transglutaminase, TG2, TGase 2, GTGase, gpTG, tissue type protein-glutamine-γ-glutamyltransferase
Source
Recombinantly produced in E. coli
Purity
> 95 % (visually by SDS-PAGE),
Activation
10 mM CaCl2
Specific Activity
> 8 U/mg [Activity is determined using the hydroxamate assay according to Folk and Cole, Biochim. Biophys. Acta 122; 244-264, (1966). One unit is defined as the formation of 1 µmol hydroxamate per minute from Z-Gln-Gly-OH and hydroxylamine at pH 6,0 at 37 °C containing 10 mM CaCl2 (L-Glutamic acid γ-monohydroxamate is the standard)].
Appearance
White lyophilized solid.
Description
gpTG2-Gene has heen isolated from guinea pig liver cDNA and fused to 6 Histidine-codons at the 5´ end resulting in the N-terminal amino acid sequence MHHHHHHAEDLILE… His6-rgpTG2 is produced in E. coli and purified by ion metal chelating chromatography to more than 95 % purity.
Reagents
The purified transglutaminase is lyophilized from 10 mM NaH2PO4, 150 mM NaCl, pH 8. Sample contains maltodextrin.
Reconstitution
Add H2O to the vial of lyophilized powder. Rotate vial gently until solid dissolves.
Application
rgpTG2 catalyzes acyl transfer reactions from glutamin residues in proteins or peptides to primary amines, e. g. the formation of ε-(γ-glutamyl) lysine bonds between proteins by transferring the acyl group of a peptide-bound glutamine residue to the primary amino group of a peptide-bound lysine residue.
Storage
Store at -20°C. Avoid repeated freezing and thawing.
Delivery is possible at ambient temperature
Reference(s)
Hauser et al., Amino Acids. 2016, 1-17 
Wodtke et al., Chembiochem. 2016, DOI: 10.1002/cbic.201600048
Note
INTENDED FOR RESEARCH USE ONLY, NOT FOR USE IN HUMAN, THERAPEUTIC OR DIAGNOSTIC APPLICATIONS.

News

Blog

Events