Analytical Data
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Gene name
PSMD5
- Application
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Alternative Names
S5B; 26S protease subunit S5 basic
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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
Q16401
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Expression Region
Lys143~Arg341
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Molecular Weight
26kDa
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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
PSMD5, a subunit of the 26S proteasome, plays a crucial role in the ubiquitin-proteasome pathway, which is essential for the regulation of protein degradation and turnover in eukaryotic cells. Research into PSMD5 has garnered significant attention due to its involvement in various cellular processes, including cell cycle regulation, signal transduction, and the modulation of gene expression. Abnormalities in proteasome activity, often linked to dysfunctions in PSMD5, have been implicated in several diseases, particularly cancer and neurodegenerative disorders. Understanding the structure and function of PSMD5 is vital for deciphering its role in proteasome function and exploring its potential as a therapeutic target. Recent studies have focused on the recombinant expression of PSMD5 to facilitate in-depth analyses of its biochemical properties and interactions with other proteasome subunits and regulatory factors. This research not only advances our understanding of the proteasomal mechanism but also opens avenues for the development of novel treatments that can modulate proteasome activity in disease states. Thus, the study of PSMD5 is pivotal in both basic research and clinical applications, highlighting its significance in the broader context of cellular homeostasis and disease pathogenesis.
