Analytical Data
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Gene name
ltxA
- Application
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Alternative Names
AaLta lktA
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Species
Aggregatibacter actinomycetemcomitans
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Source
Yeast
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P16462
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Expression Region
721-1055aa
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Molecular Weight
38.3 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
Related Products
Protein Description
LtxA (leukotoxin A) is a virulence factor produced by certain strains of *Actinobacillus actinomycetemcomitans*, a bacterium associated with periodontal disease and systemic conditions. This exotoxin has garnered significant attention due to its ability to induce cytotoxicity in host cells, particularly immune cells such as lymphocytes and macrophages, leading to immune evasion and tissue damage. Studies have shown that LtxA can modulate various cellular pathways, contributing to inflammation and cell death. Understanding the molecular mechanisms by which LtxA exerts its effects is crucial for developing potential therapeutic interventions against the diseases associated with this pathogen. Recombinant LtxA proteins have been produced to facilitate investigations into its structure-function relationships, interactions with host cells, and potential as a vaccine candidate. Research efforts focus on elucidating the detailed biochemical properties of LtxA and exploring its role in pathogenicity, with the aim of uncovering novel strategies for prevention and treatment of *A. actinomycetemcomitans*-related conditions. The study of LtxA not only enhances our understanding of bacterial pathogenesis but also contributes to the broader field of immunology and cellular biology.
