Analytical Data
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Gene name
munIM
- Application
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Alternative Names
munIM；Type II methyltransferase M.MunI
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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
P43641
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Expression Region
1-233aa
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AA Sequence
MENKVTAYSIYNKKAKKNTKVNPLDEVFPQLPRKKYQVIYADPPWDYGGKMQYDKSTIKSENEGFKRDIFISSASFKYPTLKLKELQQLDVPSITADDCILFMWTTGPQMANSILLGESWGFEYKTVAFVWDKMVHNPGRYTLSQTEFVLVFKKGKIPTPRGARNVRQLLQIHRGQHSEKPYAVIDGITKMFPALDKIELFARNNFVGWDNWGLEIPDNKIEIPTQGEIDENK
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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
MunIM is a protein of interest due to its significant role in various biological processes and potential applications in biotechnology and medicine. Research surrounding MunIM has intensified, particularly in the context of its involvement in microbial metabolism and its ability to influence important pathways within cells. Understanding the structure and function of MunIM, along with its interaction with other molecular components, is crucial for elucidating its biological significance. The reconstitution of MunIM into functional proteins through recombinant DNA technology allows scientists to study its properties in detail, providing insights into its enzymatic activity and stability. Recent studies have demonstrated the potential of MunIM in biocatalysis, making it a candidate for industrial applications, such as bioremediation and biosynthesis. Additionally, the elucidation of its structure could aid in the design of inhibitors or activators that may have therapeutic uses. Overall, research on the recombinant MunIM protein embodies a multidisciplinary approach combining molecular biology, biochemistry, and applied sciences, with the aim of unlocking new avenues for innovation in health and environmental sustainability.
