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  • Transglutaminases (TGases) are enzymes that catalyze the formation of a stable isopeptide bond between the acyl group of the glutamine side chain and the alkyl amine of the lysine side chain. TGases are ubiquitous in multicellular organisms and play a role in protein cross-linking events in migration, apoptosis, and wound healing, as well as in physiological disorders such as Huntington’s disease and celiac sprue. In contrast to mammalian TGases, bacterial TGases do not require cofactors, such as Ca2+ or GTP, and function over a broad range of pH, buffers, and temperatures.

    With its strict substrate specificity and remarkable activity, enzyme-promoted bioconjugation provides a viable alternative to conventional protein labeling methods. Enzymes can be easily isolated from cell culture, and are low-cost and environmentally friendly. Therefore, a variety of enzymes are used for site-specific protein modifications that are generally limited to the N- or C-terminus of the protein. TGases differ from these enzymes in that their targeted residues do not need to be terminally located. They allow labeling or modification at any accessible and reactive position on proteins. Therefore, TGases can be used as a labeling device for protein substrates whose termini are not amenable to modified or which require internal modification. Biotinylation, PEGylation, or fluorescent dye site-specific labeling of proteins (such as primary amines or peptides containing glutamine) are common applications of TGase labeling.

    Transglutaminase Protein Labeling Kits

    Advantages of TGase mediated site-specific protein labeling

    • Definite degree of labeling
    • Definite label positions
    • Homogenously labeled protein
    • Higher solubility in water
    • Minimized amounts of unlabeled protein
    • No or reduced impact on the bioactivity of labeled proteins

    Requirements for TGase mediated protein labeling

    TGase mediated protein labeling requires accessible lysine residues or glutamine residues on the target protein surface and these substrate sequences are not generally abundant on proteins. If no lysine or glutamine residues are accessible, substrate sequence tags may be introduced recombinantly.

    Utilization of modified proteins

    • Fluorescence-based high-throughput screening assays
    • Diagnostics based on antibodies, antibody-binding proteins, lectins etc.
    • Therapeutic PEGylation proteins
    • Protein immobilization (after biotinylating)

    TGase Protein Labeling Kits

    TGase Protein Labeling Kits are designed to easily obtain milligram amounts of labeled proteins. TGases catalyzed labeling requires accessible glutamine (Q) or lysine (K) residues on the surface of target proteins. In the first step, Substrate Finder Kit is used to determine whether the target protein contains accessible glutamine residues or lysine residues, or both, or none at all. In addition, Substrate Finder Kit indicates which of the following labeling kits is appropriate to modify the target protein with the desired label: biotin, PEG1088, PEG5000 or ATTO-488™, ATTO-532™, ATTO-550™, ATTO-647 N™, ATTO-700™.

    Product Name Applications Label
    Substrate Finder Kit For determination of TGase substrate properties of proteins  
    Biotin TGase Protein Q-Labeling Kit For labeling proteins containing accessible glutamine (Q) residues Biotin
    PEG1,088 TGase Protein Q-Labeling Kit PEG1088
    ATTO-488TM TGase Protein Q-Labeling Kit ATTO-488™
    ATTO-532TM TGase Protein Q-Labeling Kit ATTO-532™
    ATTO-550TM TGase Protein Q-Labeling Kit ATTO-550™
    ATTO-647NTM TGase Protein Q-Labeling Kit ATTO-647N™
    ATTO-700TM TGase Protein Q-Labeling Kit ATTO-700™
    Biotin TGase Protein K-Labeling Kit For labeling proteins containing accessible lysine (K) residues Biotin
    PEG1,088 TGase Protein K-Labeling Kit PEG1088
    PEG5,000 TGase Protein K-Labeling Kit PEG5000

    Steps for selecting TGase protein labeling kits

    Steps for selecting TGase protein labeling kits

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