RNF7 Protein, Human (GST)

RNF7 Protein, Human (GST) is the recombinant human-derived RNF7, expressed by E. coli , with N-GST labeled tag. ,

CUL5-RBX2 is the catalytic component of multiple cullin-5-RING E3 ubiquitin-protein ligase complexes (ECS complexes), mediating ubiquitination and subsequent proteasomal degradation of target proteins, thereby participating in various biological processes such as cell cycle progression, signal transduction, and transcription. The functional specificity of ECS complexes depends on the variable SOCS box-containing substrate recognition component. Within ECS complexes, RNF7/RBX2 recruits the E2 ubiquitination enzyme via its RING domain, bringing it into proximity with the substrate. As a catalytic subunit of various SOCS-containing ECS complexes, such as the ECS(SOCS7) complex (by similar), it regulates reelin signaling by mediating ubiquitination and degradation of DAB1. The ECS(SOCS2) complex mediates ubiquitination and degradation of phosphorylated EPOR and GHR. Additionally, CUL5-RBX2 promotes ubiquitination and degradation of NF1 (by similar), regulating Ras protein signal transduction. As part of the ECS(ASB9) complex, it catalyzes ubiquitination and degradation of CKB. The ECS(SPSB3) complex catalyzes ubiquitination of nuclear CGAS. As part of the ECS(RAB40C) complex, it mediates ANKRD28 ubiquitination and degradation, inhibiting protein phosphatase 6 (PP6) complex activity and focal adhesion assembly during cell migration. Some ECS complexes catalyze 'Lys-11'-linked ubiquitination and degradation of BTRC. ECS complexes collaborate with ARIH2 to mediate ubiquitination of target proteins, with ARIH2 adding the first ubiquitin to CRLs targets. CUL5-RBX2 specifically catalyzes neddylation of CUL5 via interaction with UBE2F but does not neddylate other cullins (CUL1, CUL2, CUL3, CUL4A, or CUL4B). It may also play a role in protecting cells from apoptosis induced by redox agents.

Human

E. coli

N-GST

Q9UBF6-1 (A2-K113)

9616

Full Length of Isoform-1 Mature Protein

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

<1 EU/μg, determined by LAL method.