Analytical Data
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Gene name
lexA
- Application
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Alternative Names
lexA；exrA；spr；tsl；LexA repressor
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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
P0A7C2
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Expression Region
1-202aa
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AA Sequence
MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL
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Molecular Weight
38.4 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 LexA protein, originally identified in Escherichia coli, plays a crucial role in the bacterial SOS response, a cellular mechanism triggered by DNA damage. As a repressor, LexA binds to specific DNA sequences to inhibit the expression of genes involved in DNA repair and recombination. Under stress conditions, such as the presence of harmful agents that damage DNA, LexA undergoes auto-proteolysis, leading to its inactivation and the subsequent activation of SOS genes. This process is essential for bacterial survival in adverse environments. The study of LexA and its regulatory functions provides insights into bacterial adaptability and resistance mechanisms. Additionally, due to its well-defined structure and interaction with DNA and other proteins, LexA has become a valuable model for investigating protein-DNA interactions and protein-protein interactions. Research on LexA has implications beyond microbiology, influencing fields such as synthetic biology, where it is utilized as a genetic switch, and biochemistry, where its mechanisms can inform drug discovery efforts targeting similar pathways in pathogenic organisms. Understanding the molecular details of LexA's function could lead to novel strategies for combating bacterial infections and enhancing our knowledge of cellular stress responses in various organisms. As researchers continue to unravel the complexities of LexA's interactions and regulations, this protein remains a significant focus in the study of microbial genetics and cellular response to DNA damage.
