Analytical Data
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Gene name
rpmI
- Application
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Alternative Names
Ribosomal protein A
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Species
Escherichia coli
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0A7Q1
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Expression Region
7-64aa
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Molecular Weight
33.5 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
RPMI recombinant proteins, derived from the RPMI-1640 culture medium initially developed for human lymphocyte growth, are crucial in biomedical research and therapeutic applications. The RPMI medium has been widely used for culturing various cell types, including immune cells, which has led to significant advancements in immunology and cancer research. The production of recombinant proteins involves the incorporation of specific genes into host cells, enabling the expression and purification of proteins that are critical for studying biological processes and developing targeted therapies. Researchers focus on optimizing expression systems to ensure high yield and functionality of these proteins for applications in vaccine development, antibody production, and enzyme assays. Furthermore, understanding the properties of these recombinant proteins, including their structure and interaction with other biomolecules, is essential for advancing personalized medicine and improving treatment outcomes for various diseases. As the field of biotechnology progresses, the continued exploration of RPMI recombinant proteins promises to unlock new insights into cellular mechanisms and therapeutic strategies.
