Analytical Data
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Gene name
munIM
- Application
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Alternative Names
Adenine-specific methyltransferase MunI ;M.MunI
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Species
Mycoplasma sp
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P43641
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Expression Region
1-233aa
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Molecular Weight
42.9 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
The study of munIM recombinant proteins is situated within the broader context of biotechnology and protein engineering, aiming to understand and harness the functional capabilities of microbial proteins. MunIM, derived from certain microorganisms, has garnered interest due to its potential applications in industrial processes, environmental bioremediation, and therapeutic development. The recombinant expression of munIM enables the production of large quantities of this protein, allowing researchers to investigate its structural properties, enzymatic activities, and interactions with other biomolecules. This research is particularly relevant in the field of enzyme design, where modifications to the munIM protein can enhance its stability, specificity, and efficiency under varying conditions. By elucidating the mechanisms by which munIM operates, scientists can pave the way for innovative solutions in areas such as biofuel production, waste management, and drug discovery. Overall, the exploration of munIM recombinant proteins not only contributes to fundamental biological knowledge but also holds promise for numerous practical applications that could address global challenges in health and sustainability.
