Analytical Data
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Gene name
rpl36
- Application
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Species
Xenopus tropicalis
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6DER2
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Expression Region
1-105aa
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Molecular Weight
19.8 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
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Protein Description
RPL36, a component of the ribosomal protein family, is essential for ribosome biogenesis and protein synthesis in eukaryotic cells. Its critical role lies in the assembly of ribosomes, which are molecular machines responsible for translating messenger RNA into proteins. Research into RPL36 has gained importance due to its involvement in various cellular processes and its potential links to diseases. Dysregulation or mutations in ribosomal proteins like RPL36 have been implicated in disorders such as cancer and Diamond-Blackfan anemia. Additionally, since ribosomes are integral to cell function and growth, understanding the structure and function of RPL36 could provide insights into the mechanisms of translation and regulatory networks in cells. Recent advancements in recombinant protein technology have enabled the detailed expression and purification of RPL36, allowing researchers to investigate its interactions and functional dynamics in greater depth. These studies may reveal pivotal information regarding the ribosomal assembly pathway and its impact on cellular physiology. Overall, the investigation of RPL36 through recombinant protein research is not only vital for understanding fundamental biological processes but may also pave the way for novel therapeutic strategies targeting ribosome-related diseases.
