RBCK1 Protein, Human (His)

RBCK1 is an E3 ubiquitin protein ligase that cooperates with specific E2 enzymes such as UBE2L3/UBCM4 to transfer ubiquitin to substrates. It acts as an E3 ligase that oxidizes IREB2, relying on heme and oxygen for IREB2 ubiquitination. RBCK1 Protein, Human (His) is the recombinant human-derived RBCK1 protein, expressed by E. coli , with N-6*His labeled tag. The total length of RBCK1 Protein, Human (His) is 509 a.a., .

RBCK1 Protein functions as an E3 ubiquitin-protein ligase, receiving ubiquitin from specific E2 enzymes, including UBE2L3/UBCM4, and transferring it to substrates. It acts as an E3 ligase for oxidized IREB2, requiring heme and oxygen for IREB2 ubiquitination. RBCK1 promotes the ubiquitination and proteasomal degradation of TAB2 and IRF3. As part of the LUBAC complex, RBCK1 catalyzes the conjugation of linear polyubiquitin chains to substrates, crucial for NF-kappa-B activation and inflammation regulation. The LUBAC complex is recruited to TNF-R1 signaling complex components, contributing to complex stability and preventing TNF-induced cell death. RBCK1, in conjunction with OTULIN, regulates canonical Wnt signaling during angiogenesis and binds polyubiquitin of various linkage types. Additionally, the LUBAC complex plays a role in innate immunity by forming a ubiquitin coat around bacteria invading the cytosol, acting as an 'eat-me' signal for xenophagy and promoting NF-kappa-B activation.

Human

E. coli

N-6*His

Q9BYM8 (D2-H510)

/

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

<1 EU/μg, determined by LAL method.