Analytical Data
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Gene name
RPL32
- Application
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Alternative Names
60S ribosomal protein L32; L32; PP9932; Ribosomal protein L32; RL32_HUMAN; rpl32
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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
P62910
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Expression Region
2-135 aa
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AA Sequence
AALRPLVKP KIVKKRTKKF IRHQSDRYVK IKRNWRKPRG IDNRVRRRFK GQILMPNIGY GSNKKTKHML PSGFRKFLVH NVKELEVLLM CNKSYCAEIA HNVSSKNRKA IVERAAQLAI RVTNPNARLR SEENE
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Molecular Weight
15.8 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
RPL32, a ribosomal protein L32, is an essential component of the 60S subunit of the eukaryotic ribosome, playing a critical role in protein synthesis. Recent studies have highlighted its importance not only in ribosomal function but also in various cellular processes, including stress response, cell growth, and apoptosis. Alterations in RPL32 expression have been associated with several diseases, including cancer, where it may contribute to dysregulated protein synthesis and cellular homeostasis. Additionally, RPL32 is implicated in translational control mechanisms that are crucial for cellular adaptation to environmental changes. The increased interest in RPL32 has driven research into its structural properties, post-translational modifications, and interactions with other ribosomal proteins and factors involved in translation. Understanding the functional dynamics of RPL32 is vital for elucidating its role in ribosome biogenesis and its potential as a therapeutic target. As a result, the reconstitution of RPL32 in vitro has become an important approach to dissect its function and interactions in the ribosomal context, paving the way for potential advancements in targeted therapies for diseases linked to ribosomal dysfunction.
