Analytical Data
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Gene name
SPRL2A
- Application
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Alternative Names
LEP2; LCE1B; Late Cornified Envelope 1B,Epidermal Differentiation Complex; Small proline-rich-like epidermal differentiation complex protein 2A
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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
J3QP15
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Expression Region
Met1~Gly111
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Molecular Weight
20kDa
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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
SPRL2A (Sphingolipid Phosphate Regulatory like 2A) is a member of the sphingolipid phosphate regulatory protein family, which has garnered interest due to its potential role in various biological processes, including cell signaling, proliferation, and apoptosis. Recent studies have indicated that SPRL2A may have significant implications in cancer biology, as it appears to be involved in the regulation of sphingolipid metabolism, thereby influencing cell membrane dynamics and signaling pathways. As an emerging player in the field of lipid biology, SPRL2A's precise functions and mechanisms of action are still being elucidated, with particular attention to its interactions with other cellular components and its influence on tumor microenvironments. The recombinant expression of SPRL2A protein has become a pivotal area of research, providing insights into its biochemical properties and potential therapeutic applications. Understanding the structure and function of SPRL2A through recombinant protein studies may pave the way for novel strategies in targeting sphingolipid signaling pathways, contributing to the development of innovative treatments for diseases characterized by dysregulated sphingolipid metabolism, particularly cancer. Hence, ongoing research into SPRL2A not only enhances our understanding of sphingolipid biology but also holds promise for advancing therapeutic interventions in oncology and other related fields.
