MuRF1 (C-terminal region) Antibody

Muscle proteolysis is regulated by the ATP-dependent ubiquitin–proteasome system. This system involves ubiquitination of specific proteins, leading to recognition and degradation by the 26S proteasome complex. Ubiquitination requires interactions with ubiquitin related proteins, ubiquitin-activating (E1), ubiquitin-conjugating (E2) and ubiquitin-ligating enzymes (E3) known as ligases. Two muscle specific ubiquitin ligases have been identified, muscle ring finger 1 (MuRF-1) and Atrogin 1. Both ligases are regulated by the Akt1/FOXO1 signaling pathway, and both proteins have been shown to be upregulated prior to the onset of atrophy in multiple models of muscle wasting, including disuse and cachexia. MuRF1 is also known as TRIM63, SMRZ, and RNF28, and its expression is upregulated after TNFα treatment in C2C12 cells and muscle tissue, while localization of MuRF1 protein has been observed in the cytoplasm and nucleus of cells.

The antibody detects 38 and 30 kDa* proteins corresponding to the apparent molecular mass of MuRF1 isoforms on SDS-PAGE immunoblots of mouse C2C12 cells, and detects a 38 kDa band in mouse heart and muscle tissue. This peptide sequence is highly conserved in rat and mouse MuRF1, and has 50% homology to MuRF2 (TRIM-55) .