Analytical Data
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Gene name
lspL
- Application
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Alternative Names
lspL；lsp；lspL；LipoProtein signal peptidase
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Species
E.coli
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
MRYLITGTAGFIGFHVAKRLIDEGHFVVGFDGMTPYYDVTLKERRHAILQRSNGFKAVTAMLEDRAALDRAAELAEPEVIIHLAAQAGVRYSLENPKAYVDANLVGSWNMLELAKAIAPKHLMLASTSSIYGANEKIPFAEADRADEPMTLYAATKKSMELMAHSYAHLYKVPTTSFRFFTVYGPWGRPDMALFKFVDAIHNGRPIDIYGEGRMSRDFTYIDDLVESIVRLSHVPPSEENRVAPEKATDTLSRHAPFRVVNTGGGQPVELMTFVETVEKAVGRPAIHNMLPMQQGDVPRTFASPDLLEALTGFKPSVSVEEGVARFVEWYDQNYRRAHTTV
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Molecular Weight
54.1kDa
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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
The study of LspL recombinant protein is grounded in the expanding field of biotechnology and its applications in various sectors, including medicine and agriculture. LspL, a protein characterized by its role in specific biochemical processes, has garnered interest due to its potential applications in developing novel therapeutic agents and in biocatalysis. Researchers have focused on the structural and functional characterization of LspL to understand its mechanisms and enhance its efficacy through recombinant DNA technology. By expressing LspL in host organisms, scientists aim to produce large quantities of this protein for detailed studies, which can reveal insights into enzyme kinetics, protein interactions, and structural dynamics. Moreover, the exploration of LspL's properties offers promising avenues for innovations in drug design and the enhancement of crop resilience. The integration of LspL studies within the broader context of protein engineering and systems biology underscores its significance, as researchers continue to investigate its potential in providing solutions to critical challenges in health and agricultural sustainability.
