Analytical Data
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Gene name
SMS
- Application
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Alternative Names
SST;Somatostatin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
2-366aa
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AA Sequence
AAARHSTLDFMLGAKADGETILKGLQSIFQEQGMAESVHTWQDHGYLATYTNKNGSFANL RIYPHGLVLLDLQSYDGDAQGKEEIDSILNKVEERMKELSQDSTGRVKRLPPIVRGGAID RYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRAI MGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDVL DNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILDL SMKVLKQDGKYFTQGNCVNLTEALSLYEEQLGRLYCPVEFSKEIVCVPSYLELWVFYTVW KKAKP
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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
The study of SMS (sphingomyelin synthase) proteins has gained significant attention due to their crucial role in sphingolipid metabolism, which is essential for various cellular processes including cell signaling, apoptosis, and membrane structure maintenance. SMS proteins catalyze the synthesis of sphingomyelin from ceramide and phosphatidylcholine, thereby influencing lipid composition and the dynamics of cellular membranes. Dysregulation of SMS activity has been implicated in several pathological conditions, including neurodegenerative diseases, cancer, and metabolic disorders, highlighting the need for a deeper understanding of their functional mechanisms. Recent advancements in molecular biology techniques have facilitated the exploration of SMS structure-function relationships, enabling researchers to unravel the precise roles of SMS isoforms in health and disease. Moreover, the potential therapeutic implications of modulating SMS activity in disease contexts have spurred interest in developing targeted interventions. Ongoing research aims to elucidate the regulatory pathways governing SMS expression and activity, assess their contribution to lipid homeostasis, and explore how manipulating SMS function could lead to novel treatment strategies for sphingolipid-related disorders. As the interplay between SMS proteins and various signaling pathways becomes clearer, they are likely to emerge as critical players in the development of innovative therapeutic approaches to manage diseases linked to sphingolipid metabolism.
