Cat: IPD-X40978

Recombinant Mouse Mmp3 Protein ,His

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Analytical Data

  • Gene name

    Mmp3

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    EMS-2Matrix metalloproteinase-3 ;MMP-3Transin-1

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N- His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P28862

  • Expression Region

    104-477aa

  • Molecular Weight

    46.2 kDa

  • 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

Mmp3 (Matrix metalloproteinase-3), also known as stromelysin-1, is an enzyme belonging to the matrix metalloproteinase (MMP) family, which plays a critical role in the degradation of extracellular matrix components. Research into Mmp3 has gained significant attention due to its involvement in various physiological and pathological processes, including tissue remodeling, wound healing, and inflammation. Additionally, Mmp3 has been implicated in several diseases, such as arthritis, cardiovascular diseases, and cancer, where its dysregulation can lead to excessive tissue damage and metastasis. Investigating the structure and function of Mmp3 is vital for understanding its role in these conditions and exploring potential therapeutic interventions. Recombinant Mmp3 protein serves as a valuable tool for studying its biochemical properties, substrate interactions, and regulatory mechanisms. By utilizing techniques such as recombinant DNA technology, researchers can produce Mmp3 in large quantities, allowing for in-depth analyses and screening of Mmp3 inhibitors, which may lead to novel treatment strategies aimed at mitigating the adverse effects of diseases associated with Mmp3 dysregulation. Overall, Mmp3 remains a focal point in matrix biology and therapeutic research, highlighting the need for ongoing studies to elucidate its diverse roles in health and disease.

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