Analytical Data
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Gene name
SDS
- Application
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Alternative Names
(SDH)(L-serine deaminase)(L-threonine dehydratase)(TDH)
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Species
Human
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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
P20132
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Expression Region
2-328aa
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Molecular Weight
42.1 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
SDS (sodium dodecyl sulfate) is a widely used anionic surfactant that plays a crucial role in the study of proteins, particularly in the separation and characterization of proteins through techniques such as SDS-PAGE (polyacrylamide gel electrophoresis). In the realm of recombinant proteins, the expression and purification of these proteins are integral to biotechnology and pharmaceutical applications. Recombination techniques, such as cloning genes of interest into plasmid vectors and expressing them in host organisms like bacteria, yeast, or mammalian cells, allow for the production of proteins that may be difficult to obtain from natural sources. SDS not only denatures proteins, ensuring that they unfold and lose their native structure, but also imparts a negative charge proportional to the protein's mass. This property is essential for the effective separation of proteins based on their molecular weight during electrophoresis. The use of SDS in protein research has led to significant advancements in our understanding of protein structure and function, facilitating the analysis of protein-protein interactions, post-translational modifications, and the development of therapeutic proteins and vaccines. As the demand for novel therapeutic proteins continues to grow, understanding the roles of surfactants like SDS in protein biochemistry is increasingly vital for the optimization of recombinant protein production and purification processes. This research background underscores the importance of SDS in enhancing the efficacy of techniques used in the life sciences, paving the way for innovations ranging from drug development to synthetic biology applications.
