Analytical Data
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Gene name
lolA
- Application
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Alternative Names
lolA；lplA；yzzV；Outer-membrane lipoProtein carrier Protein
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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
A7ZYJ5
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Expression Region
22-203aa
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AA Sequence
DAASDLKSRLDKVSSFHASFTQKVTDGSGAAVQEGQGDLWVKRPNLFNWHMTQPDESILVSDGKTLWFYNPFVEQATATWLKDATGNTPFMLIARNQSSDWQQYNIKQNGDDFVLTPKASNGNLKQFTINVGRDGTIHQFSAVEQDDQRSSYQLKSQQNGAVDAAKFTFTPPQGVTVDDQRK
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Molecular Weight
22.3 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
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Protein Description
LolA, or lipoprotein localization factor A, is a crucial component involved in the post-translational modification and localization of lipoproteins in bacteria. Its primary function is to aid in the transfer of lipoproteins across the inner membrane and ensure their proper insertion into the outer membrane of Gram-negative bacteria. The study of LolA has gained significant attention due to its role in bacterial physiology and pathogenicity, as lipoproteins are essential for numerous functions, including cell wall maintenance, nutrient uptake, and signaling. The importance of lipoproteins in disease mechanisms makes LolA an attractive target for drug development, particularly against antibiotic-resistant pathogens. Researchers are increasingly focusing on the structural and functional characterization of LolA and its interactions with other proteins involved in lipoprotein maturation and trafficking. Understanding these processes at a molecular level could provide insights into bacterial survival strategies and lead to innovative therapeutic approaches. Recent advancements in techniques such as X-ray crystallography and cryo-electron microscopy have enabled a more detailed investigation of LolA and its complex network within the bacterial cell. Overall, the research on LolA and its associated pathways is not only significant for microbiology but also holds promise for the development of novel antimicrobial strategies, especially as the threat of multidrug-resistant bacteria continues to rise globally.
