Analytical Data
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Gene name
RPL23A
- Application
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Alternative Names
60S ribosomal protein L23a
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P62750
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Expression Region
Ala2~Ile156
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Molecular Weight
27kDa
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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
RPL23A, a gene encoding a ribosomal protein that is part of the large subunit of the ribosome, plays a crucial role in ribosome assembly and protein synthesis. Research into RPL23A has gained momentum due to its implications in various biological processes, including cell growth, proliferation, and stress responses, as well as its potential involvement in cancer biology. Abnormal expression of RPL23A has been linked to tumorigenesis and cancer progression, thus making it a candidate for therapeutic interventions. Furthermore, RPL23A interacts with various regulatory proteins and is implicated in pathways related to cell cycle regulation and apoptosis. Understanding the structure, function, and regulatory mechanisms of RPL23A can provide insights into its role in normal cellular function and disease. Recent advances in recombinant techniques allow for the production of RPL23A in heterologous systems, facilitating detailed studies on its biochemical properties, interactions, and functions. This research not only enhances our understanding of ribosomal functions and their regulation but also opens avenues for developing novel strategies aimed at targeting RPL23A in cancer therapy and other diseases. As such, the study of RPL23A as a recombinant protein is crucial for the development of new therapeutic approaches and for enhancing our comprehension of fundamental cellular mechanisms.
