MuRF1 (C-terminal region) Blocking Peptide
€155.00
In stock
SKU
ECM-MX3405
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.
Sequence: MuRF1 (C-terminal) synthetic peptide corresponding to amino acid residues in the C-terminal half of human MuRF1. This peptide sequence is highly conserved in rat and mouse MuRF1, and has 50% homology to MuRF2 (TRIM-55).
Specificity: The peptide is specifically recognized by MuRF1 (C-terminal region) antibody (MP3401) in ELISA, and has been shown to block the reactivity of MP3401 in Western blot. In addition, the peptide is recommended for use in blocking MP3401 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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.
Sequence: MuRF1 (C-terminal) synthetic peptide corresponding to amino acid residues in the C-terminal half of human MuRF1. This peptide sequence is highly conserved in rat and mouse MuRF1, and has 50% homology to MuRF2 (TRIM-55).
Specificity: The peptide is specifically recognized by MuRF1 (C-terminal region) antibody (MP3401) in ELISA, and has been shown to block the reactivity of MP3401 in Western blot. In addition, the peptide is recommended for use in blocking MP3401 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
| Is Featured? | No |
|---|
Write Your Own Review