Analytical Data
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Gene name
RPL13
- Application
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Alternative Names
60S ribosomal protein L13; BBC1; Breast basic conserved gene 1; Breast basic conserved protein 1; D16S444E ; D16S44E; FLJ27453 ; FLJ27454 ; L13; MGC117342 ; MGC71373 ; OK/SW cl.46; OK/SWcl.46; Ribosomal protein L13; RL13_HUMAN; rpl13
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Species
Human
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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
P26373
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Expression Region
1-211 aa
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AA Sequence
MAPSRNGMVL KPHFHKDWQR RVATWFNQPA RKIRRRKARQ AKARRIAPRP ASGPIRPIVR CPTVRYHTKV RAGRGFSLEE LRVAGIHKKV ARTIGISVDP RRRNKSTESL QANVQRLKEY RSKLILFPRK PSAPKKGDSS AEELKLATQL TGPVMPVRNV YKKEKARVIT EEEKNFKAFA SLRMARANAR LFGIRAKRAK EAAEQDVEKK K
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Molecular Weight
24.2 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
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Protein Description
RPL13, a key member of the ribosomal protein family, plays a crucial role in the assembly and function of the ribosome, which is essential for protein synthesis in all living organisms. Research on RPL13 has gained significant attention due to its involvement in various cellular processes and its implications in human diseases, especially cancer. Aberrations in ribosomal proteins, including RPL13, have been linked to ribosomopathies, a group of disorders characterized by defects in ribosome biogenesis and function. Additionally, recent studies have suggested that RPL13 may play a role in regulating cell proliferation and apoptosis, thereby influencing tumorigenesis. Given the foundational role of RPL13 in ribosome function and its potential involvement in disease mechanisms, the study of RPL13 recombinant proteins has become increasingly important. Researchers utilize recombinant techniques to produce RPL13 for structural and functional analyses, aiming to elucidate its role in ribosome assembly and its interaction with various biomolecules. Understanding the structure-function relationship of RPL13 could provide insights into its regulatory mechanisms and help identify potential therapeutic targets for diseases associated with ribosome dysfunction. As such, the investigation of RPL13 and its recombinant forms represents a critical area of research with the potential to advance our understanding of fundamental biological processes and their implications in health and disease.
