Cat: IPD-X37403

Recombinant Human TGM2/Transglutaminase 2 Protein,His

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Analytical Data

  • Gene name

    TGM2/Transglutaminase 2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    tTG; TG2; C Polypeptide,Protein-Glutamine-Gamma-Glutamyltransferase; Transglutaminase 2, Tissue; Transglutaminase C; Transglutaminase H

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P21980

  • Expression Region

    Met1~Ala687

  • Molecular Weight

    100kDa

  • Endotoxin

    < 1.0 EU per μg protein as determined by the LAL method.

  • Form

    Freeze-dried powder

  • Buffer formulation

    PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

  • Reconstitution

    Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.

  • Customization

    Site-directed mutagenesis Custom tag design Custom buffer formulation Custom full-length protein production

  • Stability Test

    The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.

  • Storage & Shelf Life

    Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

  • Shipping

    In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.

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Protein Description

Transglutaminase 2 (TGM2) is a multifunctional enzyme involved in various biological processes, including protein crosslinking, intracellular signaling, and cell adhesion. It has garnered significant attention due to its role in various diseases, such as celiac disease, neurodegenerative disorders, and cancer. TGM2 catalyzes the formation of covalent bonds between glutamine and lysine residues in proteins, which impacts protein stability and function. The study of recombinant TGM2 has become increasingly important, as it allows researchers to explore its enzymatic activity, structure-function relationships, and interactions with other cellular components in a controlled environment. Recombinant technology enables the production of TGM2 in sufficient quantities for biochemical assays, structural studies, and potential therapeutic applications. Furthermore, understanding TGM2's mechanisms could lead to novel strategies for diagnosing and treating diseases associated with its dysregulation. Overall, the investigation of recombinant TGM2 serves as a key platform for elucidating its biological significance and potential as a therapeutic target.

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