Analytical Data
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Gene name
RPL35A
- Application
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Alternative Names
RPL35A;Large ribosomal subunit Protein eL33
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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
P18077
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Expression Region
1-110aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSGRLWS KAIFAGYKRG LRNQREHTAL LKIEGVYARD ETEFYLGKRC AYVYKAKNNT VTPGGKPNKT RVIWGKVTRA HGNSGMVRAK FRSNLPAKAI GHRIRVMLYP SRI
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Molecular Weight
15 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
RPL35A, a gene encoding ribosomal protein L35a, plays a crucial role in ribosome assembly and protein synthesis, making it a key component in cellular function and development. This protein is part of the large ribosomal subunit, contributing to the structure and stability of the ribosome, which is essential for translating messenger RNA into proteins. Research into RPL35A has gained momentum due to its association with various diseases, including cancers and genetic disorders, where its expression levels may be altered. Understanding the biological mechanisms underlying RPL35A's function can provide insights into ribosomal biogenesis and the molecular basis of related pathologies. Moreover, studies involving the recombinant expression of RPL35A allow for detailed investigations into its structure and interaction with other ribosomal proteins and RNA components. This can facilitate the exploration of ribosome-related processes, such as translation regulation and cellular response to stress. As the ribosome is a critical target for therapeutic interventions, insights from RPL35A research may pave the way for novel approaches to disease treatment. Therefore, the study of RPL35A not only enhances our understanding of fundamental biological processes but also holds potential implications for medical advancements.
