Cat: IPD-X30072

Recombinant Mouse MME Protein,His & GST

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Analytical Data

  • Gene name

    MME

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    NEP; MME; CALLA; SFE; Atriopeptidase; Enkephalinase; Skin fibroblast elastase; Common Acute Lymphoblastic Leukemia Antigen; Membrane Metallo-Endopeptidase

  • Species

    Mouse

  • Source

    E. coli

  • Tag

    N- His & GST

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q61391

  • Expression Region

    Leu455~Trp750

  • Molecular Weight

    64kDa

  • 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

The study of MME (membrane metalloendopeptidase), also known as neprilysin, is vital due to its significant role in maintaining various physiological functions and its implications in several pathological conditions. MME is a zinc-dependent metalloprotease that hydrolyzes a broad range of bioactive peptides, including neuropeptides and vasoactive peptides, thereby influencing processes such as blood pressure regulation, neurodegeneration, and inflammation. Its activity is particularly critical in the degradation of amyloid-beta peptides, linking it to Alzheimer’s disease pathology. Researchers have focused on understanding the structural and functional properties of MME to develop potential therapeutic strategies. Given the enzyme’s involvement in neurodegenerative disorders, selective inhibitors of MME have emerged as potential candidates for enhancing cognitive function and mitigating disease progression. Additionally, MME's expression levels and activity are associated with various cancers, further expanding the scope of its research as a biomarker or therapeutic target. Efforts are also directed toward elucidating the regulatory mechanisms governing MME expression and activity, which could inform strategies for modulating its function in clinical settings. Overall, the multifaceted role of MME in health and disease underscores the importance of ongoing research to exploit its potential in therapeutic interventions.

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