PSMG4 Protein, Human (His, Strep)

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 (His, Strep) is the recombinant human-derived PSMG4 protein, expressed by E. coli , with N-Strep, N-6*His labeled tag. The total length of PSMG4 Protein, Human (His, Strep) is 123 a.a., .

PSMG4 (Proteasome assembly chaperone 4) is a chaperone protein that plays a crucial role in promoting the assembly of the 20S proteasome. Functioning in collaboration with PSMG3, PSMG4 facilitates the proper formation and maturation of the 20S proteasome, an essential component of the cellular protein degradation machinery. Notably, PSMG4 interacts with the alpha subunits of the 20S proteasome, indicating its involvement in coordinating the assembly of this multi-subunit complex. The chaperone activity of PSMG4 underscores its significance in ensuring the proper functioning and structural integrity of the 20S proteasome, contributing to the cell's ability to regulate protein turnover and maintain cellular homeostasis. It has to highlight PSMG4's role as a chaperone protein in promoting the assembly of the 20S proteasome and its interaction with both PSMG3 and the alpha subunits of the proteasome.

Human

E. coli

N-Strep;N-6*His

Q5JS54 (M1-F123)

389362

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.