Cat: IPD-X32816

Recombinant Human MMP-9 Protein (HEK293),His

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Analytical Data

  • Gene name

    MMP-9

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    GELB; Gelatinase B; CLG4B; CLG4-B; 92 KDa Gelatinase; 92kDa Type IV Collagenase

  • Species

    Human

  • Source

    HEK293

  • Tag

    N-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P14780

  • Expression Region

    Ala20~Asp707

  • 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.

Quality inspection process

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Protein Description

Matrix metalloproteinase-9 (MMP-9) is a zinc-dependent endopeptidase that plays a critical role in the degradation of extracellular matrix components, which is essential for various physiological processes, including tissue remodeling, wound healing, and angiogenesis. Abnormal regulation of MMP-9 has been implicated in numerous pathological conditions, such as cancer metastasis, cardiovascular diseases, and inflammatory disorders. As a result, MMP-9 has emerged as a significant biomarker and therapeutic target in these contexts. The recombinant protein form of MMP-9 allows for detailed studies of its functional properties, enzymatic activity, and interaction with specific inhibitors. Researchers have focused on understanding the structure-activity relationship of MMP-9, developing potent MMP inhibitors, and exploring potential applications in drug delivery systems. Additionally, the recombinant expression of MMP-9 provides valuable insights into its mechanism of action and the molecular pathways it affects, paving the way for the development of new therapeutic strategies aimed at modulating MMP-9 activity to treat various diseases. As the understanding of MMP-9's role in health and disease deepens, the opportunity to harness recombinant technology for both research and clinical applications continues to expand.

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