Analytical Data
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基因名
ail
- Application
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别名
ail;CDKN2AIP N-terminal-like Protein
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种属
E.coli
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P16454
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表达区间
24-178aa
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氨基酸序列
ASESSISIGYAQSHVKENGYTLDNDPKGFNLKYRYELDDNWGVIGSFAYTHQGYDFFYGSNKFGHGDVDYYSVTMGPSFRINEYVSLYGLLGAAHGKVKASVFDESISASKTSMAYGAGVQFNPLPNFVIDASYEYSKLDSIKVGTWMLGAGYRF
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分子量
33.2 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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.












