Analytical Data
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基因名
aAgAB
- Application
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别名
P34
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种属
Human
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表达系统
E. coli
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标签
N-His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q6PD74
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表达区间
Met1~His315
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分子量
50kDa
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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
aAgAB recombinant protein is derived from the antigenic components of certain pathogens, particularly focusing on the Ag85 complex found in Mycobacterium tuberculosis and related species. The study of aAgAB is significant for its potential role in diagnostic assays, vaccine development, and understanding immune responses. Mycobacterium tuberculosis remains a major global health challenge, infecting millions and causing tuberculosis. The ability of Ag85 proteins to elicit strong immune responses makes aAgAB a target of interest in immunology and infectious disease research. Previous studies have identified that recombinant forms of these proteins can induce cellular and humoral immunity, leading to protective responses in animal models. This has sparked interest in creating optimized versions of aAgAB for enhanced immunogenicity and stability. Furthermore, research is focused on understanding the structural and functional properties of aAgAB, which could unveil insights into its mechanisms of action and interaction with the host immune system. The versatility of recombinant protein technologies enables modifications that can improve efficacy and safety, paving the way for novel therapeutic strategies against tuberculosis and potentially other diseases caused by pathogenic mycobacteria. Overall, the investigation of aAgAB aligns with broader efforts to combat infectious diseases through innovative vaccine approaches and biomarkers for disease diagnosis, making it a pivotal subject in contemporary biomedical research.












