TRIM16 Protein, Human (Sf9, His, Strep)

TRIM16 protein is an essential E3 ubiquitin ligase that participates in autophagy reaction and ubiquitination during lysosome and phagosome damage. TRIM16 Protein, Human (Sf9, His, Strep) is the recombinant human-derived TRIM16 protein, expressed by Sf9 insect cells , with N-Strep, N-8*His labeled tag. The total length of TRIM16 Protein, Human (Sf9, His, Strep) is 563 a.a., .

TRIM16, functioning as an E3 ubiquitin ligase, assumes a crucial role in orchestrating the autophagic response and ubiquitination processes in the face of lysosomal and phagosomal damages. Notably, it contributes to the stress-induced biogenesis and degradation of protein aggresomes by intricately regulating the p62-KEAP1-NRF2 signaling axis. A central aspect of its functionality lies in modulating ubiquitination levels and, consequently, the stability of NRF2, a key player in cellular stress responses. As a scaffold protein, TRIM16 facilitates the autophagic degradation of protein aggregates, forming interactions with p62/SQSTM, ATG16L1, and LC3B/MAP1LC3B. This multifaceted role positions TRIM16 as a guardian against oxidative stress-induced cell death, particularly in response to endomembrane damage.

Human

Sf9 insect cells

N-Strep;N-8*His

O95361 (A2-P564)

/

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

<1 EU/μg, determined by LAL method.