Description
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.Human recombinant Atrogin 1 is a 54kDa protein that includes the full length sequence along with N-terminal His tag and Sumo fusion tag. This Atrogin 1 fusion protein is detected by rabbit polyclonal anti-Atrogin 1 and rat monoclonal anti-Atrogin 1