bsm-70547M

DATASHEET

Host: Mouse

Target Protein: MuRF1 (C-terminal region)

Specificity: The antibody detects a full length human MuRF1 recombinant protein on SDS-PAGE immunoblots. This peptide sequence is highly conserved in rat and mouse MuRF1, and has 50% homology to MuRF2 (TRIM-55).

Clonality: Monoclonal

Isotype: IgG1

Swiss Prot: Q969Q1

Source: Clone M316 was generated from a synthetic peptide (coupled to KLH) corresponding to amino acid residues in the C-terminal half of human MuRF1.

Purification: Antigen Affinity purification

Storage Buffer: PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol

Storage: Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.

Background:

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.