Microbial transglutaminase with C-terminal His6-Tag

- Overview
  - Please contact us at for specific academic pricing.
    
    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.
    
    More Details
    
    Zedira
- Properties
  - Name
    
    EC 2.3.2.13; Protein-glutamine-γ-glutamyltransferase
    
    Source
    
    E. coli
    
    Type
    
    Recombinant Proteins
    
    Formulation
    
    The purified transglutaminase is lyophilized from 50 mM NaOAc pH 5.0 + 0.3 M NaCl.
    
    Storage
    
    Store at –20°C in working aliquots. Repeated freezing and thawing is not recommended. Delivery is possible at ambient temperature
    
    Note
    
    INTENDED FOR RESEARCH USE ONLY, NOT FOR USE IN HUMAN, THERAPEUTIC OR DIAGNOSTIC APPLICATIONS.
    
    Molecular Weight
    
    39 kDa (Dispase-activated MTG with N-terminal sequence: FRAPDSDDR...)
    
    Class
    
    Microbial (Pro)TGase
    
    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.Reconstituted MTG solution might be turbid. However, MTG activity is not affected. In this case, centrifuge the solution and collect the supernatant.After reconstitution, the solution should be stored frozen in working aliquots.
    
    More Information
    
    Animal-Free
    
    yes
- Applications
  - Application Description
    
    Labeling, immobilisation, conjugation and modification of proteins.