Transglutaminase 2

Dog tissue transglutaminase

(clTG2, recombinantly produced in insect cells)
Quantity Unit Price Status
250 µg 400 € Available
1 mg 1200 € Available
Documents
Art. No.
T072
Synonym
Tissue-type Transglutaminase, TG2, TGase 2, protein-glutamine-γ-glutamyltransferase
Molecular Weight
78 kDa
Source
Recombinant produced in insect cells.
Purity
> 90 % (visually by SDS-PAGE)
Activation
His6-rhTG2 is a Ca2+-dependent enzyme. Add 10 mM Ca2+ to activate His6-clTG2.
Activity
> 1500 U/mg [Activity is determined by measuring the rate of fluorescence enhancement after His6-clTG2-catalyzed monodansylcadaverine-incorporation into N,N-dimethylated casein according to Lorand et al., Anal. Biochem. 44 (221-231).
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)].
Appearance
White lyophilized solid.
Reagents
The Transglutaminase is lyophilized from 10 mM Tris-HCl pH 8.1, 150 mM NaCl, 1 mM EDTA, 5 mM DTT. Sample contains maltodextrin.
Reconstitution
Add the volume of H2O the protein is lyophilized from (see Certificate of Analysis) to the vial of lyophilized powder. Rotate vial gently until solid dissolves. After reconstitution the solution should be stored frozen in working aliquots. Keep cooled on ice for short term storage.
Application
His6-clTG2 catalyzes acyl transfer reactions from glutamine 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. His6-clTG2 may also be used for immunoprecipitation.
Storage
Store working aliquots at ≤ - 20°C. Avoid repeated freezing and thawing.
Delivery is possible at ambient temperature
Note
INTENDED FOR RESEARCH USE ONLY, NOT FOR USE IN HUMAN, THERAPEUTIC OR DIAGNOSTIC APPLICATIONS.

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