TRIM3 Protein, Human (GST)

TRIM3 protein is an E3 ubiquitin ligase that regulates neuronal plasticity, learning, and memory. TRIM3 Protein, Human (GST) is the recombinant human-derived TRIM3 protein, expressed by E. coli , with N-GST labeled tag. The total length of TRIM3 Protein, Human (GST) is 743 a.a., .

TRIM3, an E3 ubiquitin ligase, assumes crucial roles in neuronal functions, orchestrating the regulation of neuronal plasticity, learning, and memory. Beyond its neuronal involvement, TRIM3 extends its influence to various biological processes, including innate immunity and cell cycle regulation. Within neurons, it becomes a key component of the cytoskeleton-associated recycling or transport complex, exerting its regulatory role by polyubiquitinating gamma-actin and thereby influencing neuronal plasticity. Additionally, TRIM3 ubiquitinates the postsynaptic scaffold GKAP, contributing to synaptic remodeling and modulation of dendritic spine morphology. It positively regulates the motility of the microtubule-dependent motor protein KIF21B. Moreover, TRIM3, through its RING-dependent E3 ligase activity, induces growth arrest and ubiquitinates CDKN1A. In the realm of innate immunity, it plays a positive regulatory role in TLR3-mediated signaling by mediating 'Lys-63'-linked polyubiquitination of TLR3, subsequently facilitating the recognition and sorting of polyubiquitinated TLR3 by the ESCRT complexes.

Human

E. coli

N-GST

O75382 (A2-Q744)

10612

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

<1 EU/μg, determined by LAL method.