Analytical Data
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Gene name
rpl36
- Application
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Alternative Names
rpl36；Large ribosomal subunit Protein eL36
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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
Q6DER2
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Expression Region
1-105aa
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AA Sequence
MAIRYPMAVGLNKGHRVTKNVTKPRHCRRRGRLTKHTKFVRDMIREVCGFAPYERRAMELLKVSKDKRALKFIKKRIGTHIRAKRKREELSNVLAAMRKAAAKKD
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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 crucial gene encoding ribosomal protein L36, is a component of the large ribosomal subunit in eukaryotic cells. Research on RPL36 has gained significance due to its involvement in fundamental biological processes such as protein synthesis, cell growth, and division. Mutations or dysregulations in ribosomal proteins like RPL36 have been implicated in various diseases, including cancer, where altered ribosome biogenesis is a hallmark. Additionally, studies have revealed that RPL36 plays a role in the response to cellular stress, indicating its potential involvement in stress-related diseases and aging. With the increasing understanding of the ribosome's role in maintaining cellular homeostasis, there is a growing interest in exploring RPL36’s structure, function, and interaction with other ribosomal proteins and RNA components. Investigations into RPL36 and its recombinant proteins can provide insights into ribosome assembly, function, and the molecular mechanisms underlying diseases associated with ribosomal dysfunction. Furthermore, recombinant RPL36 proteins hold potential for biotechnological applications, including the development of novel therapeutic strategies targeting ribosome activity in disease treatment. As such, RPL36 serves as a promising candidate for further research, which may lead to a deeper understanding of ribosomal biology and its implications in health and disease.
