Cat: IPD-X38605

Recombinant Human TINAG Protein,His

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Analytical Data

  • Gene name

    TINAG

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    TIN1; TIN2; TIN-AG

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q9UJW2

  • Expression Region

    Met1~Pro476

  • Molecular Weight

    58Da

  • 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.

Quality inspection process

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Protein Description

TINAG (Tissue Inhibitor of Metalloproteinases 3) is a crucial protein that plays a significant role in various biological processes, including tissue remodeling and cell migration. It is particularly known for its involvement in the regulation of extracellular matrix components and metalloproteinases, which are vital for maintaining tissue homeostasis. Recent studies have highlighted its importance in pathological conditions, including cancer metastasis and fibrosis, making it a promising target for therapeutic interventions. The understanding of TINAG's structure and function has advanced through recombinant protein technologies, which allow for the production of TINAG in a controlled environment. Research focuses on elucidating TINAG's mechanism of action in cellular signaling pathways and its interactions with other proteins. Investigating TINAG's potential as a biomarker for disease progression and treatment response is also a growing area of interest. As the demand for targeted therapies increases, the development of TINAG-based strategies could offer novel approaches in the fields of oncology and regenerative medicine. Understanding TINAG's role at the molecular level is essential for harnessing its therapeutic potential, thus paving the way for innovative treatments that could improve patient outcomes in various diseases.

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