Analytical Data
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Gene name
aAgAB
- Application
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Alternative Names
P34
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Species
Human
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Source
E. coli
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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
Q6PD74
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Expression Region
Met1~His315
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Molecular Weight
50kDa
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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
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.
