Analytical Data
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Gene name
RPL3
- Application
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Alternative Names
HIV-1 TAR RNA-binding protein B ;TARBP-B
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Species
Human
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Source
E. coli
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Tag
GST (N-Term)
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P39023
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Expression Region
1-403aa
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AA Sequence
MSHRKFSAPRHGSLGFLPRKRSSRHRGKVKSFPKDDPSKPVHLTAFLGYKAGMTHIVREVDRPGSKVNKKEVVEAVTIVETPPMVVVGIVGYVETPRGLRTFKTVFAEHISDECKRRFYKNWHKSKKKAFTKYCKKWQDEDGKKQLEKDFSSMKKYCQVIRVIAHTQMRLLPLRQKKAHLMEIQVNGGTVAEKLDWARERLEQQVPVNQVFGQDEMIDVIGVTKGKGYKGVTSRWHTKKLPRKTHRGLRKVACIGAWHPARVAFSVARAGQKGYHHRTEINKKIYKIGQGYLIKDGKLIKNNASTDYDLSDKSINPLGGFVHYGEVTNDFVMLKGCVVGTKKRVLTLRKSLLVQTKRRALEKIDLKFIDTTSKFGHGRFQTMEEKKAFMGPLKKDRIAKEEGA
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Molecular Weight
72.5 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
Identification
Protein Description
RPL3, a vital component of the 60S ribosomal subunit, plays a critical role in protein synthesis and cellular function. Research on RPL3 has gained prominence due to its involvement in various cellular processes and its potential implications in human diseases, particularly cancer. Aberrant expression or mutations of RPL3 have been associated with tumorigenesis, highlighting its role in regulating cell proliferation and apoptosis. Scientists have focused on characterizing RPL3's structure and function to understand its contributions to ribosome assembly and translation. Recent advancements in recombinant protein technology have enabled researchers to produce RPL3 in vitro, facilitating detailed investigations into its biochemical properties and interactions with other ribosomal proteins and RNA. Understanding the precise mechanisms by which RPL3 influences ribosome function and its involvement in pathogenic processes could illuminate novel therapeutic targets for diseases linked to ribosomal dysfunction. Consequently, RPL3 stands at the intersection of molecular biology and clinical research, making it a significant subject of study for both basic science and translational medicine.











