Analytical Data
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Gene name
ail
- Application
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Alternative Names
ail；CDKN2AIP N-terminal-like 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
P16454
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Expression Region
24-178aa
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AA Sequence
ASESSISIGYAQSHVKENGYTLDNDPKGFNLKYRYELDDNWGVIGSFAYTHQGYDFFYGSNKFGHGDVDYYSVTMGPSFRINEYVSLYGLLGAAHGKVKASVFDESISASKTSMAYGAGVQFNPLPNFVIDASYEYSKLDSIKVGTWMLGAGYRF
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Molecular Weight
33.2 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
Ail (Attachment Invasion Locus) protein is a virulence factor found in several pathogenic bacteria, particularly in certain strains of Yersinia enterocolitica and Yersinia pestis. It plays a crucial role in the bacterial invasion and persistence within host tissues by facilitating adherence to host cells and evading the immune response. Given its importance in the pathogenesis of these bacteria, Ail has garnered significant interest in molecular microbiology and infectious disease research. Studies have revealed that Ail can interact with host cell receptors, modulating signaling pathways that promote bacterial survival and replication. These interactions not only contribute to the bacterium's virulence but also highlight potential therapeutic targets. Furthermore, the structural characteristics of Ail, including its transmembrane domain and hydrophobic regions, suggest that it may function similarly to other outer membrane proteins involved in bacterial invasion. Research on Ail and its mechanism of action could lead to novel strategies for developing vaccines or treatments against infections caused by Yersinia species. The exploration of Ail's role in bacterial pathogenicity emphasizes the need for comprehensive studies to understand its interactions with host cells and the immune system, paving the way for advancements in combating bacterial infections.
