Analytical Data
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Gene name
PSMG4
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简介
PSMG4 protein functions as a chaperone, facilitating the assembly of the 20S proteasome. In its role as a chaperone, PSMG4 interacts with PSMG3, forming a functional complex that contributes to the proper assembly of the 20S proteasome. Notably, PSMG4 associates specifically with the alpha subunits of the 20S proteasome, highlighting its involvement in the intricate process of proteasomal maturation and functionality. PSMG4 Protein, Human is the recombinant human-derived PSMG4 protein, expressed by E. coli , with tag free.
- Application
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Alternative Names
PSMG4; Proteasome assembly chaperone 4; PAC-4; hPAC4
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5JS54
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Expression Region
M1-F123
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Protein Length
Full Length
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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
PSMG4 (Proteasome 26S Subunit, ATPase 4) is a crucial component of the 26S proteasome, a multi-protein complex responsible for degrading ubiquitinated proteins, thereby playing a vital role in regulating various cellular processes, including the cell cycle, apoptosis, and the response to oxidative stress. Understanding PSMG4's structure and function has garnered significant attention in recent years due to its implications in cancer and neurodegenerative diseases. Abnormalities in proteasome activity, often linked to the dysregulation of proteins involved in cellular signaling and stress responses, may contribute to the pathogenesis of several disorders. Additionally, PSMG4 has been identified as a potential therapeutic target, as modulating its activity could enhance proteasome function, promoting the degradation of misfolded proteins and potentially alleviating disease symptoms. Recent studies have focused on the recombinant expression of PSMG4 to elucidate its biochemical properties, interaction with other proteasome subunits, and role in ATP hydrolysis and substrate processing. By leveraging advanced techniques such as X-ray crystallography and cryo-electron microscopy, researchers aim to obtain high-resolution structural insights into PSMG4 and its complex interactions within the proteasome machinery. This research not only enhances our understanding of proteasomal function but may also pave the way for novel therapeutic strategies targeting the proteasome in various pathologies, highlighting the significance of PSMG4 in both basic and applied biomedical research.
