Analytical Data
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Gene name
R70M
- Application
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Species
Nitrosomonas europaea
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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
Q50927
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Expression Region
27-198aa(R70M)
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Molecular Weight
34.7 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 R70M recombinant protein has gained significant attention in the field of biomedical research due to its potential therapeutic applications, particularly in the treatment of various diseases, including cancer and infectious diseases. The R70M variant, a specific mutation of a naturally occurring protein, was identified for its enhanced stability and activity compared to its wild-type counterpart. Studies have shown that this modified protein can improve binding affinity to target receptors, potentially leading to more effective drug delivery and therapeutic outcomes. The background of this research lies in the growing challenge of developing efficient biomolecules that can overcome the limitations of existing treatments. The introduction of recombinant technology allows for precise modifications of proteins, leading to innovations in therapeutic design. Furthermore, the exploration of the R70M variant encourages a deeper understanding of protein structure-function relationships and how these can be manipulated to enhance biological performance. As researchers continue to investigate its properties and mechanisms of action, the R70M recombinant protein holds promise for advancing personalized medicine and improving patient care in various clinical settings.
