Analytical Data
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Gene name
lktA
- Application
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Alternative Names
lktA；AaLta；lktA；Leukotoxin
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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
P55118
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Expression Region
1-229aa
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AA Sequence
MGNKLTNISTNLKSSWLTAKSGLNRTGQSLAKAGQSLKTGAKKIILYIPKDYQYDTEKGNGLQDLVKAAEELGIEVQKEEGNDIAKAQTSLGTIQNVLGLTERGIVLSAPQLDKLLQKTKVGQAIGSAENLTKGFSNAKTVLSGIQSILGSVLAGMDLDEALQKNSNELTLAKAGLELTNSLIENIANSVKTLDAFGDQINQLGSKLQNVKGLSSLGDKLKGLSGFDKT
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Molecular Weight
29.2 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
LktA, a novel protein derived from the bacterium *Listeria monocytogenes*, has garnered significant interest in the field of microbiology and biotechnology due to its potential applications in vaccine development and therapeutic interventions. As a critical virulence factor, LktA plays a crucial role in the pathogenicity of *Listeria*, facilitating the bacterium's ability to evade host immune responses. Its unique structure and enzyme activity have led researchers to explore its role in bacterial survival and infection mechanisms. Advances in recombinant DNA technology have enabled the production of LktA as a recombinant protein, allowing for detailed biochemical characterization and functional studies. The ability to manipulate this protein in vitro provides insights into its immunogenic properties, potentially aiding in the formulation of protein-based vaccines. Moreover, understanding the regulatory pathways associated with LktA may uncover new targets for antimicrobial drug development. Research into LktA not only enhances our understanding of *Listeria* pathogenesis but also holds promise for innovative therapeutic strategies to combat infections caused by this and other related bacterial pathogens. The ongoing exploration of LktA's molecular function and its interaction with host immune cells is crucial for developing new biomedical applications and improving public health outcomes.
