Cat: IPD-X32498

Recombinant Human SMPD1 Protein (HEK293),His

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Analytical Data

  • Gene name

    SMPD1

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    SMPD1; NPD; SMase; aSMase; Sphingomyelin Phosphodiesterase 1,Acid Lysosomal; Simply Sphingomyelinase

  • Species

    Human

  • Source

    HEK293

  • Tag

    N-His

  • Purity

    Greater than 95% as determined by SDS-PAGE.

  • Uniprot

    P17405

  • Expression Region

    His62~Pro628

  • 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.

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Protein Description

SMPD1, also known as sphingomyelin phosphodiesterase 1, is a critical enzyme involved in sphingolipid metabolism, specifically in the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. This enzymatic activity has significant implications in various biological processes, including cell signaling, apoptosis, and inflammation. Dysregulation of SMPD1 has been linked to numerous pathological conditions such as neurodegenerative diseases, atherosclerosis, and certain cancers. Research into recombinant SMPD1 proteins has gained traction as scientists seek to better understand the enzyme’s structure-function relationship, regulatory mechanisms, and its role in cellular homeostasis. By producing recombinant SMPD1, researchers can explore its enzymatic properties, analyze the effects of specific mutations, and develop potential therapeutic interventions targeting sphingolipid metabolism. Furthermore, the availability of recombinant SMPD1 opens avenues for high-throughput screening of small molecules that may modulate its activity, paving the way for innovative treatments for diseases associated with sphingolipid imbalance. This growing field emphasizes the importance of SMPD1 as a biochemical target and underlines the potential benefits of advancing our understanding of its role in human health.

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