USP13 Protein, Human (GST)

The multifunctional USP13 protein functions as a deubiquitinase and complexly regulates autophagy, ERAD, cell cycle progression, and DNA damage responses. It affects key pathways through deubiquitination of BECN1, MITF, SKP2 and USP10. USP13 Protein, Human (GST) is the recombinant human-derived USP13 protein, expressed by E. coli , with N-GST labeled tag. The total length of USP13 Protein, Human (GST) is 862 a.a., .

The USP13 Protein, as outlined in this description, serves as a versatile deubiquitinase involved in various cellular processes, including autophagy, endoplasmic reticulum-associated degradation (ERAD), cell cycle progression, and DNA damage response. It mediates the deubiquitination of target proteins such as BECN1, MITF, SKP2, and USP10, exerting influence on critical pathways. In the regulation of autophagy and p53/TP53 levels, USP13 participates in a complex interplay by deubiquitinating BECN1, stabilizing PIK3C3/VPS34-containing complexes, and forming a deubiquitination complex with NEDD4 to promote autophagy. Additionally, it regulates the stability of USP10, influencing the intricate balance of p53/TP53. USP13 contributes to endoplasmic reticulum-associated degradation (ERAD) by deubiquitinating SKP2 and UBL4A. Furthermore, it plays essential roles in maintaining genomic stability, DNA replication checkpoint activation through regulation of RAP80 and TOPBP1, and modulation of interferon signaling by deubiquitinating STAT1 and STING1. The multifunctional nature of USP13 underscores its significance in orchestrating diverse cellular processes with implications for cellular homeostasis and response to external stimuli.

Human

E. coli

N-GST

Q92995 (Q2-S863)

8975

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

<1 EU/μg, determined by LAL method.