Analytical Data
-
Gene name
PSME4
- Application
-
Alternative Names
PA200; Proteasome activator PA200
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q14997
-
Expression Region
Leu1634~Ala1843
-
Molecular Weight
26kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
PSME4, or Proteasome Activator Complex Subunit 4, is a vital component of the proteasome, a multicatalytic enzyme complex responsible for degrading ubiquitinated proteins within the cell. This process is crucial for regulating various cellular functions, including the maintenance of protein homeostasis, the response to stress, and the control of cellular signaling pathways. Research on PSME4 has gained momentum due to its potential implications in various diseases, particularly cancer and neurodegenerative disorders. It is suggested that abnormal expression or malfunction of PSME4 may disrupt the proteasome’s activity, leading to the accumulation of damaged or misfolded proteins, which can contribute to pathological conditions. Moreover, PSME4 has also been implicated in modulating the immune response, thereby influencing the progression of inflammatory diseases. As such, the study of PSME4 and its recombinant protein forms has become crucial not only for understanding its role in cellular proteolysis but also for developing therapeutic strategies targeting PSME4-related pathologies. Investigating the structural and functional characteristics of recombinant PSME4 can provide insights into its mechanism of action and potential regulatory pathways, contributing to the broader field of proteasome research and its applications in drug development and disease management.
