Analytical Data
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Gene name
RPN13
- Application
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Alternative Names
Proteasome non-ATPase subunit 13
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Species
Saccharomyces cerevisiae
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O13563
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Expression Region
2-156aa
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Molecular Weight
33.8 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
RPN13, a pivotal component of the 26S proteasome, plays a critical role in the regulation of protein degradation, which is essential for maintaining cellular homeostasis and regulating various cellular processes, including cell cycle progression, apoptosis, and stress responses. Recent studies have highlighted the involvement of RPN13 in the recognition and processing of ubiquitinated substrates, thus ensuring that damaged or misfolded proteins are efficiently targeted for degradation. Its unique structure, featuring a ubiquitin-binding domain, allows RPN13 to interact directly with ubiquitin chains, facilitating the delivery of substrates to the proteasome. Furthermore, aberrations in RPN13 expression or function have been implicated in several diseases, including cancer and neurodegenerative disorders, making it an attractive target for therapeutic interventions. The recombinant expression of RPN13 not only aids in the elucidation of its biochemical properties and interaction mechanisms but also enables the development of potential inhibitors that could modulate its activity in pathological conditions. Investigating RPN13 as a recombinant protein presents a valuable opportunity to deepen our understanding of proteasomal regulation and to explore its therapeutic potential in enhancing proteostasis and targeting diseases associated with proteasome dysfunction.
