BackgroundImagesBuffer & StorageReviews 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 54 kDa 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. Western blot image of human recombinant Atrogin 1 (lanes 1-6). The blot was probed with rabbit polyclonal Atrogin-1 (lanes 1-3) and rat monoclonal Atrogin-1 (lanes 4-6) at 1:1000 (lanes 1 & 4), 1:2000 (lanes 2 & 5), and 1:4000 (lanes 3 & 6). Atrogin 1 recombinant protein lysate is supplied at a concentration of 0.5 μg/µl in electrophoresis sample buffer (62.5 mM Tris pH 6.8, 2% SDS, 5% glycerol, 0.003% bromophenol blue, 0.9% β-mercaptoethanol). Store at –20°C. Do not boil or dilute. Stable for 1 year. The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blotmobilities of known proteins with similar MW.This kit contains:KIT SUMMARY