Analytical Data
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Gene name
RPL37A
- Application
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Alternative Names
RPL37A; 60S ribosomal protein L37a; Large ribosomal subunit protein eL43
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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
P61513
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Expression Region
2-92 aa
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AA Sequence
AKRTKKVGI VGKYGTRYGA SLRKMVKKIE ISQHAKYTCS FCGKTKMKRR AVGIWHCGSC MKTVAGGAWT YNTTSAVTVK SAIRRLKELK DQ
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Molecular Weight
10.2 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
Related Products
Protein Description
RPL37A, a critical component of the ribosomal protein family, plays a pivotal role in ribosome biogenesis and protein synthesis. Research into RPL37A has garnered attention due to its essential functions in cellular processes, such as translation and cellular growth. Abnormalities in ribosomal proteins, including RPL37A, are linked to various diseases, including cancer and ribosomopathies, highlighting their importance in maintaining cellular homeostasis. Recent studies have focused on the structural and functional characterization of RPL37A, utilizing recombinant protein techniques to explore its interactions with ribosomal RNA and other ribosomal proteins. Understanding the molecular mechanisms of RPL37A can provide insights into ribosome assembly and function, as well as potential therapeutic targets for diseases associated with ribosomal dysfunction. Advances in recombinant protein technology have facilitated the production and purification of RPL37A, allowing researchers to investigate its role in translation regulation and to study the effects of mutations on ribosome assembly. Overall, the study of RPL37A recombinant proteins is critical for elucidating the fundamental roles of ribosomal components in cell biology and their implications in health and disease.
