Analytical Data
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Gene name
PSMD9
- Application
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Alternative Names
Rpn4; p27; 26S proteasome regulatory subunit p27; 26S proteasome non-ATPase regulatory subunit 9
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O00233
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Expression Region
Ser2~Arg223
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Molecular Weight
30kDa
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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
PSMD9 (Proteasome 26S Subunit, Non-ATPase 9) is a crucial component of the 26S proteasome, which plays a vital role in protein degradation and cellular regulation. The proteasome itself is responsible for the ubiquitin-proteasome pathway, a major mechanism for controlling protein levels and functions, influencing various cellular processes such as the cell cycle, signal transduction, and response to stress. Research on PSMD9 has gained significance due to its implication in multiple biological pathways and diseases, including cancer and neurodegenerative disorders. Dysregulation of the proteasome system can lead to the accumulation of damaged or misfolded proteins, contributing to cellular dysfunction. Consequently, studying the structure, function, and regulation of PSMD9 recombinant protein is essential for understanding its role in proteasome activity and potential therapeutic targets. Advances in recombinant protein technology have facilitated the production and characterization of PSMD9, enabling researchers to investigate its interaction with other proteasome subunits and regulatory proteins. This knowledge may provide insights into the development of novel drugs that can modulate proteasome activity, offering potential therapeutic strategies for diseases associated with proteasome dysfunction. Overall, understanding the biology of PSMD9 and its role within the proteasome complex is crucial for advancing our knowledge of protein homeostasis and its impact on human health.
