Analytical Data
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Gene name
SMPD2
- Application
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Alternative Names
(Lyso-platelet-activating factor-phospholipase C)(Lyso-PAF-PLC)(Neutral sphingomyelinase)(N-SMase)(nSMase)(nSMase1)
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60906
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Expression Region
1-423aa
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Molecular Weight
49.1 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
SMPD2 (sphingomyelin phosphodiesterase 2) is an essential enzyme involved in the metabolism of sphingolipids, particularly in the hydrolysis of sphingomyelin to ceramide and phosphocholine. Ceramide plays a pivotal role in various cellular processes, including apoptosis, cell signaling, and membrane dynamics. Aberrant sphingolipid metabolism is linked to several diseases, including cancer, neurodegenerative disorders, and metabolic syndromes. Recent studies have highlighted the significance of SMPD2 in modulating cellular responses under stress and in disease pathogenesis. However, the molecular mechanisms underlying the regulation and function of SMPD2 remain incompletely understood. The production and characterization of recombinant SMPD2 protein provide valuable tools for investigating its biochemical properties, enzymatic activity, and potential interactions with other cellular components. This research aims to elucidate the structure-function relationships of SMPD2, its role in sphingolipid metabolism, and its impact on cellular homeostasis. Ultimately, understanding the function of SMPD2 may contribute to the development of therapeutic strategies targeting sphingolipid metabolism-related diseases, offering new avenues for intervention and treatment in conditions influenced by sphingolipid dysregulation.
