Analytical Data
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Gene name
rpmJ
- Application
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Alternative Names
rpmJ；BRIP1；Large ribosomal subunit Protein bL36m
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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
P0A7Q6
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Expression Region
1-38aa
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AA Sequence
MKVRASVKKLCRNCKIVKRDGVIRVICSAEPKHKQRQG
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Molecular Weight
31.4 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 the RPMJ recombinant protein is rooted in the growing interest in understanding the molecular mechanisms of pathogenicity and infection in various organisms, particularly within the realm of bacterial and viral pathogens. RPMJ, a protein associated with the regulation of various cellular processes, has been identified as a potential target for therapeutic interventions due to its role in influencing microbial virulence and host-pathogen interactions. As researchers delve into the intricacies of this protein, they aim to determine its structural and functional characteristics, as well as its interactions with other biomolecules. The recombinant expression of RPMJ allows for the production of large quantities of the protein for detailed functional assays and structural studies, which are essential for elucidating its role in disease mechanisms and finding potential applications in drug development and vaccine design. Furthermore, understanding RPMJ’s involvement in stress responses and its regulatory functions provides insights into microbial adaptability and persistence, making it a significant focus in the field of microbiology and infectious diseases.
