Analytical Data
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Gene name
SMS
- Application
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Alternative Names
SPMSY; Spermidine aminopropyltransferase
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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
P52788
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Expression Region
Ala2~Pro366
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Molecular Weight
44kDa
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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
Related Products
Protein Description
The study of SMS (sphingomyelin synthase) and its associated proteins has gained significant attention due to their crucial role in cellular signaling and membrane dynamics. SMS is an enzyme that catalyzes the synthesis of sphingomyelin from ceramide and phosphatidylcholine, thereby influencing lipid metabolism and membrane composition. Alterations in SMS activity and sphingomyelin levels have been implicated in various diseases, including metabolic disorders, neurodegenerative diseases, and cancer. Recent research has uncovered that SMS not only contributes to membrane structure but also plays a key role in cell signaling pathways that regulate cell proliferation, apoptosis, and inflammation. Moreover, the interaction of SMS with other proteins and lipids is critical for maintaining cellular homeostasis. Understanding the molecular mechanisms underlying SMS function and its protein interactions is essential for developing therapeutic strategies aimed at addressing SMS-related diseases. As a result, the investigation of SMS and its associated proteins is rapidly evolving, encompassing cutting-edge techniques such as CRISPR-mediated gene editing, lipidomics, and advanced microscopy, which together provide deeper insights into lipid biology and its implications for health and disease.
