Analytical Data
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Gene name
modA
- Application
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Alternative Names
modA;CBP20;Nuclear cap-binding Protein subunit 2
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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
P37329
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Expression Region
25-257aa
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AA Sequence
DEGKITVFAAASLTNAMQDIATQFKKEKGVDVVSSFASSSTLARQIEAGAPADLFISADQKWMDYAVDKKAIDTATRQTLLGNSLVVVAPKASVQKDFTIDSKTNWTSLLNGGRLAVGDPEHVPAGIYAKEALQKLGAWDTLSPKLAPAEDVRGALALVERNEAPLGIVYGSDAVASKGVKVVATFPEDSHKKVEYPVAVVEGHNNATVKAFYDYLKGPQAAEIFKRYGFTIK
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Molecular Weight
37.9 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
Related Products
Protein Description
ModA is a prominent recombinant protein studied for its significant role in various biological processes, particularly in microbial metabolism and environmental bioremediation. Originating from certain bacteria, ModA is known to participate in the uptake of molybdenum, an essential trace element crucial for the activity of various enzymes. The understanding of ModA's structure and function has garnered attention due to its potential applications in biotechnology, such as bioremediation strategies to address heavy metal contamination. Moreover, scientists are exploring its use in biosensors to detect molybdenum levels in environmental and clinical samples. Research into ModA involves genetic engineering techniques to enhance its stability and activity, making it a valuable tool for both basic research and applied sciences. Furthermore, studies utilizing recombinant DNA technology have facilitated the production of ModA in heterologous systems, allowing for easier access to the protein for diverse applications. Overall, the exploration of ModA not only advances our understanding of microbial nutrient cycling but also opens new avenues for addressing environmental challenges and developing innovative biotechnological solutions.











