Analytical Data
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Gene name
splB
- 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
A7X3Q8
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Expression Region
37-240aa
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Molecular Weight
29.8 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
The study of recombinant SplB protein has gained significant attention due to its potential applications in various fields, including biotechnology and medicine. SplB, a protein derived from specific bacterial species, plays a crucial role in the biosynthesis of secondary metabolites and has been implicated in various biological processes, including stress response and virulence. The ability to produce this protein in a recombinant form allows researchers to investigate its functional properties and interactions in a controlled environment. Advances in molecular cloning and expression systems have facilitated the production of recombinant SplB, enabling studies on its structure-function relationships. Understanding the biochemical and biophysical characteristics of SplB is essential for harnessing its potential in drug development, enzyme engineering, and synthetic biology. Furthermore, research into its immunogenic properties may lead to the development of novel vaccines or therapeutic agents. As scientific inquiries continue to explore the diverse roles of SplB in microbial physiology and its applications in industrial processes, this research area remains a promising frontier in contemporary molecular biology and biochemistry.
