Cat: IPD-X18549

Recombinant Human Neprilysin/CD10 Protein, His

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Analytical Data

  • Gene name

    Neprilysin/CD10

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

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

  • Species

    Human

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    P08473

  • Expression Region

    Phe565~Trp750

  • Molecular Weight

    22kDa

  • 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

Neprilysin, also known as neutral endopeptidase or CD10, is an important zinc-dependent metallopeptidase involved in the degradation of bioactive peptides, including neuropeptides and natriuretic peptides. Its regulatory role in neuropeptide metabolism has garnered attention for its implications in various physiological and pathological processes, such as cardiovascular health, neurodegenerative diseases, and cancer. Neprilysin's activity contributes to the modulation of signaling pathways in the nervous system and plays a crucial role in maintaining blood pressure homeostasis. In cancer research, aberrant expression of neprilysin/CD10 has been linked to tumor progression and metastasis, making it a potential biomarker and therapeutic target. Understanding the structure, function, and regulation of neprilysin/CD10 through recombinant protein studies can provide insights into its biological roles and therapeutic potential. Recent advances in recombinant DNA technology have facilitated the production of high-purity neprilysin proteins, allowing for detailed biochemical characterization and the exploration of its interactions with peptide substrates. This research is pivotal for developing neprilysin inhibitors or enhancers that could be harnessed in treating diseases where neprilysin activity is compromised or dysregulated.

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