Cat: IPD-X38292

Recombinant Rat Alk-Smase Protein,His

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Analytical Data

  • Gene name

    Alk-Smase

  • Application

    SPRMSTBLIITCELISACELL ASSAYDRUG SCREENING

  • Alternative Names

    ENPP7; E-NPP 7; NPP-7; Ectonucleotide Pyrophosphatase/Phosphodiesterase 7; Sphingomyelin Phosphodiesterase; Intestinal alkaline sphingomyelinase

  • Species

    Rat

  • Source

    E. coli

  • Tag

    N-His

  • Purity

    Greater than 90% as determined by SDS-PAGE.

  • Uniprot

    Q5EZ72

  • Expression Region

    Gly22~Val439

  • Molecular Weight

    51kDa

  • 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

Alk-Smase, or alkaline sphingomyelinase, is an enzyme that plays a critical role in the metabolism of sphingolipids, essential components of cell membranes involved in various cellular processes, including signal transduction, cell growth, and apoptosis. Recent research has highlighted the importance of Alk-Smase in diverse physiological and pathological contexts, including cancer, neurodegenerative diseases, and inflammation. The enzyme catalyzes the hydrolysis of sphingomyelin to produce sphingosine and phosphocholine, leading to the generation of bioactive sphingolipids that can influence cell behavior. Understanding Alk-Smase’s structure and function is crucial for elucidating its role in disease mechanisms and identifying potential therapeutic targets. Recombinant Alk-Smase proteins are valuable tools for studying enzyme kinetics, structure-function relationships, and the regulation of sphingolipid metabolism. Advances in protein expression and purification techniques have made it possible to produce high yields of functional Alk-Smase, enabling detailed biochemical and biophysical analyses. Such studies are essential for deciphering the complex signaling pathways mediated by sphingolipids and for developing novel strategies to manipulate these pathways in disease contexts. Therefore, the exploration of Alk-Smase at the molecular level continues to be a significant focus in biomedical research, with the potential to reveal new insights into cell biology and open avenues for therapeutic interventions.

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