TRIM38 Protein, Human (GST)

TRIM38 Protein: E3 ligase regulating innate immunity. Degrades AZI2/NAP1, suppressing IFN-beta production. Inhibits TLR3 signaling by degrading TICAM1. Activates cGAS-STING pathway via SUMOylation of CGAS and STING. Negatively regulates NF-kappa-B signaling by degrading TAB2 and TAB3 adapters via lysosomes. TRIM38 Protein, Human (GST) is the recombinant human-derived TRIM38 protein, expressed by E. coli , with N-GST labeled tag. The total length of TRIM38 Protein, Human (GST) is 464 a.a., .

TRIM38, a versatile E3 ubiquitin-protein and E3 SUMO-protein ligase, intricately regulates innate immunity. Functioning as a negative regulator of type I interferon IFN-beta production, TRIM38 catalyzes 'Lys-48'-linked polyubiquitination of AZI2/NAP1, leading to its degradation. Additionally, TRIM38 plays a pivotal role in inhibiting TLR3-mediated type I interferon signaling by mediating 'Lys-48'-linked polyubiquitination and proteasomal degradation of the critical TLR adapter TICAM1. Acting as a positive regulator of the cGAS-STING pathway, TRIM38 serves as an E3 SUMO-protein ligase, facilitating the sumoylation of CGAS and STING, thereby preventing their degradation and activating the innate immune response to DNA viruses. Beyond its E3 ligase activities, TRIM38 functions as a negative regulator of NF-kappa-B signaling by promoting lysosome-dependent degradation of TAB2 and TAB3 adapters, underscoring its multifaceted roles in modulating immune responses.

Human

E. coli

N-GST

O00635 (A2-D465)

10475

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

<1 EU/μg, determined by LAL method.