Analytical Data
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Gene name
SPS1
- Application
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Alternative Names
Sucrose-phosphate synthase 1F Short name: AtSPS1F Sucrose-phosphate synthase 5.1 Short name: AtSPS5.1 UDP-glucose-fructose-phosphate glucosyltransferase
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Species
Arabidopsis thaliana
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q94BT0
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Expression Region
768-995aa
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Molecular Weight
41.5 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
SPS1 (Sphingoid Long-Chain base Synthase 1) is a crucial enzyme involved in the synthesis of sphingolipids, a class of bioactive lipids that play significant roles in cellular signaling, membrane structure, and various physiological processes. Understanding the function and regulation of SPS1 is essential due to its implications in various human diseases, including cancer, neurodegenerative disorders, and metabolic syndromes. Recent studies have highlighted the intricate mechanisms underlying SPS1's activity and its interactions with other cellular components, suggesting that dysregulation of SPS1 can lead to significant pathological consequences. As researchers continue to explore the biochemical pathways involving SPS1, the development of recombinant SPS1 proteins has become a pivotal tool. These recombinant proteins enable in-depth analyses of the enzyme's structure-function relationships, substrate specificity, and regulatory mechanisms. By employing techniques such as site-directed mutagenesis and crystallography, scientists aim to elucidate the molecular basis of SPS1's role in sphingolipid metabolism. Additionally, understanding how SPS1 interacts with other enzymes and cellular systems can potentially pave the way for novel therapeutic strategies targeting sphingolipid-related diseases. Thus, the study of SPS1 recombinant proteins not only enhances our fundamental understanding of lipid biology but also holds promise for innovative approaches in the treatment of various medical conditions.
