Analytical Data
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Gene name
RPL8
- Application
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Alternative Names
AP-2 mu chain;Adaptin-mu2Adaptor protein complex AP-2 subunit muAdaptor-related protein complex 2 subunit muClathrin assembly protein complex 2 mu medium chain;Clathrin coat assembly protein AP50Clathrin coat-associated protein AP50HA2 50KDA subunitPlasma membrane adaptor AP-2 50KDA protein
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P62917
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Expression Region
3-257aa
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Molecular Weight
54.8 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
RPL8, a vital ribosomal protein, plays a crucial role in the assembly and function of the ribosome, serving as a key component in protein synthesis. Recent research has revealed its involvement in various cellular processes, including the regulation of gene expression and the cell cycle. Abnormalities in RPL8 expression have been associated with several diseases, particularly cancer, where altered ribosome biogenesis and protein synthesis contribute to tumorigenesis. Understanding the structure and function of RPL8 at the molecular level is critical for elucidating its role in cellular mechanisms and its impact on health and disease. Investigating the recombinant protein of RPL8 offers insights into its properties, interactions, and potential as a therapeutic target. By expressing RPL8 in various systems, researchers aim to generate sufficient quantities for detailed biochemical and structural studies, enhancing our comprehension of its functional significance in ribosome assembly and cellular homeostasis. Moreover, exploring the regulatory pathways and factors that influence RPL8 activity may provide new avenues for cancer treatment and other related disorders, making it a compelling focus of ongoing biomedical research. This exploration is expected to lead to novel insights into the molecular underpinnings of ribosome dynamics and its broader implications in cellular biology.
