Analytical Data
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Gene name
lspL
- Application
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Alternative Names
UDP-glucuronic acid epimerase
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Species
Rhizobium meliloti
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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
O54067
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Expression Region
1-341aa
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Molecular Weight
54.1 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
The study of the LspL protein, an important member of the Lsp family (Lateral Sensing Proteins), has gained traction due to its potential applications in biotechnology and medicine. LspL is primarily found in bacteria and is involved in various cellular processes, including stress response, signaling, and cell-to-cell communication. As antibiotic resistance becomes increasingly prevalent, understanding the biochemical pathways influenced by LspL may provide insights into new therapeutic strategies. Researchers are particularly interested in its structural and functional characteristics, as these could reveal mechanisms that underpin its role in bacterial physiology. The recombinant production of LspL allows for detailed studies of its interactions and functions in vitro, facilitating the investigation of its potential as a target for drug development. Furthermore, LspL and related proteins might also serve as valuable tools in synthetic biology for engineering microbial systems. With advances in molecular biology techniques, including CRISPR and high-throughput screening, the exploration of LspL's capabilities could lead to innovative applications, making it a significant focus of current research in microbial physiology and therapeutic development.
