RNF5 Protein, Human (Cell-Free, His)

The RNF5 protein is a membrane-bound E3 ubiquitin protein ligase that is critical for ubiquitination of target proteins and can cooperate with UBE2D1/UBCH5A and UBE2D2/UBC4 to achieve ubiquitination over a broad substrate range. Notably, it mediates PXN/paxillin ubiquitination, affecting cell motility and cell positioning. RNF5 Protein, Human (Cell-Free, His) is the recombinant human-derived RNF5 protein, expressed by E. coli Cell-free , with N-10*His labeled tag. The total length of RNF5 Protein, Human (Cell-Free, His) is 179 a.a., with molecular weight of 25.8 kDa.

RNF5 Protein, a membrane-bound E3 ubiquitin-protein ligase, plays a pivotal role in the ubiquitination of target proteins, exhibiting diverse cellular functions. Teaming up with E2 ubiquitin-conjugating enzymes such as UBE2D1/UBCH5A and UBE2D2/UBC4, RNF5 orchestrates ubiquitination processes with a broad substrate range. Notably, it mediates the ubiquitination of PXN/paxillin, influencing cell motility and the cellular localization of PXN/paxillin. Additionally, RNF5 catalyzes the ubiquitination of Salmonella type III secreted protein sopA and JKAMP, modulating their functions. The 'Lys-63'-linked polyubiquitination of JKAMP regulates its association with the proteasome and ERAD components, while the 'Lys-48'-linked polyubiquitination of STING1 at 'Lys-150' leads to proteasomal degradation, impacting antiviral responses. Furthermore, RNF5 catalyzes the ubiquitination and subsequent degradation of ATG4B, providing a mechanism to inhibit autophagy. These diverse activities highlight the versatile regulatory role of RNF5 in cellular processes.

Human

E. coli Cell-free

N-10*His

Q99942 (A2-I180)

6048

AAAEEEDGGPEGPNRERGGAGATFECNICLETAREAVVSVCGHLYCWPCLHQWLETRPERQECPVCKAGISREKVVPLYGRGSQKPQDPRLKTPPRPQGQRPAPESRGGFQPFGDTGGFHFSFGVGAFPFGFFTTVFNAHEPFRRGTGVDLGQGHPASSWQDSLFLFLAIFFFFWLLSI

25.8 kDa

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

<1 EU/μg, determined by LAL method.