Analytical Data
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Gene name
PSMD2
- Application
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Alternative Names
P97; S2; TRAP2; Rpn1; Tumor necrosis factor type 1 receptor-associated protein 2; 26S proteasome regulatory subunit RPN1; 26S proteasome subunit p97
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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
Q13200
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Expression Region
Asp645~Val872
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Molecular Weight
27kDa
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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
PSMD2, or Proteasome 26S Subunit, Non-ATPase 2, is a crucial component of the 26S proteasome, a multi-subunit complex responsible for the degradation of ubiquitinated proteins, which is essential for maintaining cellular homeostasis, regulating the cell cycle, and modulating various signaling pathways. Dysregulation of the proteasome function has been implicated in several diseases, including cancer, neurodegenerative disorders, and autoimmune diseases. As a non-ATPase subunit, PSMD2 plays a significant role in the substrate recognition and binding process, influencing the proteasomal degradation pathway. Recent studies have focused on characterizing the structure and function of the PSMD2 protein, exploring its interactions with other proteasome subunits and regulatory proteins. The recombinant expression of PSMD2 has enabled researchers to investigate its enzymatic activity and its regulatory roles in proteasome-mediated degradation. Understanding the precise mechanisms by which PSMD2 influences proteasome function can provide insights into its potential as a therapeutic target, particularly in the context of diseases where proteasomal activity is altered. Furthermore, the study of PSMD2 and its interactions may unveil novel regulatory pathways involved in cellular proteostasis and response to stress, contributing to the development of strategies aimed at modulating proteasome activity for therapeutic benefits.
