Analytical Data
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Gene name
splD
- Application
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Species
Staphylococcus aureus
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q2FXC5
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Expression Region
37-239aa
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Molecular Weight
29.5 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
Related Products
Protein Description
SPLD (Sphingomyelinase and Phospholipase D) is a crucial enzyme that plays a significant role in cellular signaling and membrane dynamics. The study of SPLD recombinant proteins has gained attention due to their potential implications in understanding various biological processes and disease mechanisms, including cancer and neurodegenerative disorders. SPLD is involved in lipid metabolism, contributing to the hydrolysis of sphingomyelin and phospholipids, leading to the production of bioactive metabolites that influence cell proliferation, apoptosis, and inflammation. The recombinant production of SPLD allows researchers to investigate its structure-function relationships, enzymatic activity, and interaction with other cellular components in a controlled environment. Advances in recombinant DNA technology have facilitated the expression of SPLD in various host systems, enabling the purification of the enzyme for detailed biochemical studies. Furthermore, understanding the enzymatic pathways mediated by SPLD can provide insights into therapeutic targets and biomarkers for diseases. Recent research has focused on characterizing the enzymatic properties of SPLD, elucidating its role in signal transduction pathways, and exploring its therapeutic potential. Overall, the investigation of SPLD recombinant proteins represents a promising avenue for both basic research and the development of novel therapeutic strategies.
