Cat: IPD-X32714

Recombinant Human MMP-2 Protein,His

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Analytical Data

  • Gene name

    MMP-2

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    CLG4; CLG4A; MMP-II; MONA; TBE-1; PEX; Gelatinase A; 72kDa Gelatinase; 72kDa Type IV Collagenase

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P08253

  • Expression Region

    Ala30~Cys660

  • Molecular Weight

    75kDa

  • 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

Matrix metalloproteinase-2 (MMP-2), also known as gelatinase A, is a member of the matrix metalloproteinase family and plays a crucial role in the degradation of extracellular matrix components, particularly type IV and type V collagen. It is involved in various physiological and pathological processes, including embryogenesis, wound healing, tissue remodeling, and cancer metastasis. The overexpression and activation of MMP-2 have been linked to the progression of several diseases, including cancer, cardiovascular diseases, and neurodegenerative disorders, making it a significant target for therapeutic intervention. Given its relevance in disease mechanisms, the production of recombinant MMP-2 proteins has become a focus of research. This allows for detailed studies of its enzymatic activity, regulation, and interactions with various inhibitors. Recombinant MMP-2 can be utilized as a model to investigate its role in disease or to develop novel pharmacological agents that can inhibit its activity, providing valuable insights into potential clinical applications. The advancement of biotechnological methods has significantly improved the efficiency and yield of producing functional recombinant MMP-2, enabling extensive research paths that explore its structure-function relationship, regulatory mechanisms, and potential as a biomarker for various diseases. This ongoing research underscores the importance of MMP-2 not only in fundamental biology but also in the development of new therapeutic strategies aimed at mitigating its contribution to disease pathology.

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