Analytical Data
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Gene name
MgA
- Application
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Alternative Names
MAD5; MXD5; MAX dimerization protein 5
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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
Q8IWI9
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Expression Region
Thr2450~Lys2733
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Molecular Weight
44kDa
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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
MgA recombinant protein, derived from the Mycobacterium gapidae bacterium, has garnered significant interest in the field of immunology and vaccine development due to its potential role in eliciting an immune response against mycobacterial infections. Research has consistently highlighted the importance of Mycobacterium species as pathogens responsible for diseases such as tuberculosis and leprosy. The study of MgA is particularly relevant as it represents a novel antigen that may offer insights into the immune mechanisms underlying mycobacterial infections. Previous studies have demonstrated that recombinant MgA can stimulate specific T cell responses, indicating its potential as a vaccine candidate. Additionally, the characterization of this protein could enhance our understanding of mycobacterial virulence factors and their interactions with host immune systems. The increasing prevalence of antibiotic-resistant mycobacterial strains further underscores the urgency for effective immunotherapeutic approaches, making the exploration of MgA and its immunological properties not only timely but critical. Ongoing research aims to optimize the expression and purification of MgA to facilitate its evaluation in preclinical and clinical settings, paving the way for novel vaccine strategies against mycobacterial diseases.
