RNF11 Protein, Human

The RNF11 protein is an important component of protein complexes that regulate inflammatory signaling pathways. RNF11 Protein, Human is the recombinant human-derived RNF11 protein, expressed by E. coli , with tag free. The total length of RNF11 Protein, Human is 153 a.a., .

RNF11 takes center stage as an essential component of a ubiquitin-editing protein complex, a collaborative ensemble featuring TNFAIP3, ITCH, and TAX1BP1. This complex operates intricately to orchestrate the transient nature of inflammatory signaling pathways, exerting control over TNF- or LPS-mediated activation of NF-kappa-B. RNF11's role extends to promoting the association of TNFAIP3 with RIPK1 post-TNF stimulation. This, in turn, facilitates TNFAIP3's deubiquitination of 'Lys-63' polyubiquitin chains on RIPK1, initiating the formation of 'Lys-48'-polyubiquitin chains that culminate in RIPK1's proteasomal degradation. Furthermore, RNF11 acts as a recruiter, bringing STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, ultimately resulting in SMURF2's degradation by the 26S proteasome. This intricate web of interactions involves 14-3-3 (when phosphorylated), the E3 ubiquitin-ligases NEDD4, ITCH, SMURF2, and WWP1, as well as the E2 ubiquitin-conjugating enzymes UBE2D1 and UBE2N. Noteworthy associations include those with ZNF350, EPS15, STAMBP, TAX1BP1, TNFAIP3, RIPK1, and GGA1, revealing the multifaceted nature of RNF11's regulatory engagements.

Human

E. coli

Tag Free

Q9Y3C5 (G2-N154)

26994

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

<1 EU/μg, determined by LAL method.