Analytical Data
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Gene name
lspA
- Application
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Alternative Names
lspA；ls；LipoProtein signal peptidase
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Species
Human
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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
Q9HVM5
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Expression Region
1-169aa
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AA Sequence
MPDVDRFGRLPWLWITVLVFVLDQVSKAFFQAELSMYQQIVVIPDLFSWTLAYNTGAAFSFLADSSGWQRWLFALIAIVVSASLVVWLKRLKKGETWLAIALALVLGGALGNLYDRMVLGHVVDFILVHWQNRWYFPAFNLADSAITVGAVMLALDMFRSKKSGEAAHG
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Molecular Weight
18.9 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 lspA recombinant proteins has gained significant attention in molecular biology and biotechnology due to their potential applications in various fields, including vaccine development, therapeutic protein production, and diagnostic tools. LspA, or lipoprotein signal peptidase A, is an essential enzyme involved in the maturation of lipoproteins in both Gram-positive and Gram-negative bacteria. Understanding the function and structure of lspA can facilitate the design of targeted antibiotics and therapeutic agents, addressing the growing concern of antibiotic resistance. Additionally, recombinant lspA proteins can be utilized as biomarkers to diagnose specific bacterial infections, contributing to improved patient management. Recent advances in genetic engineering techniques, such as CRISPR and recombinant DNA technology, have enabled researchers to produce high yields of lspA proteins in heterologous systems, allowing for detailed characterization and practical applications. Investigating the immunogenic properties of lspA recombinant proteins may also pave the way for developing novel vaccines, particularly for diseases caused by pathogenic bacteria. Overall, the research on lspA recombinant proteins encapsulates a multidisciplinary approach that bridges fundamental microbiology with practical biomedical applications, positioning lspA as a key target for future studies aimed at enhancing public health.
