Human tissue transglutaminase

- Overview
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    Background
    
    Transglutaminases are a family of enzymes that catalyze the posttranslational modification of proteins by inserting an isopeptide bond within or between polypeptide chains. These enzymes catalyze the acyl transfer reaction between the γ-carboxyamide groups of peptide-bound glutamine residues and a variety of primary amines, particularly the ε-amino group of lysine. The resulting crosslink is of great significance, since it is highly stable and also resistant to mechanical and proteolytic degradation.
    
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    Zedira
- Properties
  - Name
    
    Tissue-type Transglutaminase, TG2, TGase 2, proteinglutamine-γ-glutamyltransferase
    
    Source
    
    HEK293F cells
    
    Type
    
    Recombinant Proteins
    
    Purification
    
    > 95 % (visually by SDS-PAGE)
    
    Formulation
    
    The Transglutaminase is lyophilized from 10 mM Tris-HCl pH 7.4, 300 mM NaCl, 1 mM EDTA, 1 mM DTT. Sample contains maltodextrin.
    
    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.
    
    Molecular Weight
    
    78 kDa (Val224-allele, Kanchan et al., Biochem. J. 2013, 455:261–72)
    
    Class
    
    Human Transglutaminase 2
    
    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.
    
    Activity
    
    His6-rhTG2 is a Ca2+-dependent enzyme. Add 10 mM Ca2+ to activate His6-rhTG2.
- Applications
  - Application Description
    
    Labelling, immobilisation, conjugation and modification of proteins.

Datasheet

MSDS

Human tissue transglutaminase

Background

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