Analytical Data
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Gene name
RPL35
- Application
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Alternative Names
RPL35;Large ribosomal subunit Protein uL29
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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
P42766
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Expression Region
1-123aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAKIKAR DLRGKKKEEL LKQLDDLKVE LSQLRVAKVT GGAASKLSKI RVVRKSIARV LTVINQTQKE NLRKFYKGKK YKPLDLRPKK TRAMRRRLNK HEENLKTKKQ QRKERLYPLR KYAVKA
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Molecular Weight
17 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
RPL35 is a vital ribosomal protein that plays a crucial role in ribosome biogenesis and protein synthesis in eukaryotic cells. It is a component of the large ribosomal subunit (60S) and is essential for the proper assembly and function of ribosomes, which are the cellular machinery responsible for translating messenger RNA (mRNA) into proteins. Aberrations in RPL35 expression and function have been linked to various pathological conditions, including cancer, where altered ribosome biogenesis can lead to dysregulated protein synthesis, promoting tumor growth and development. Research on RPL35 recombinant protein has gained interest due to its potential implications in understanding the molecular mechanisms underlying these diseases. By studying RPL35 in a recombinant form, scientists aim to elucidate its structural and functional properties, allowing for a better understanding of its role in ribosome assembly and the regulation of translation. Furthermore, recombinant RPL35 can be produced for use in biochemical assays to investigate its interactions with other ribosomal proteins, RNA components, and translational factors. This research not only contributes to basic biological knowledge but also opens avenues for therapeutic interventions targeting the ribosomal machinery in diseases characterized by altered protein synthesis.
