Anti-MuRF1 (C-terminal region) Antibody
Our MuRF1 (C-terminal region) rabbit polyclonal primary antibody from PhosphoSolutions is produced in-house. It detects human, mouse, and rat MuRF1 (C-terminal region) and is antigen affinity purified. It is great for use in WB, ICC.
SKU: MP3401
Ships: 1-2 business days
Product Details
MuRF1 (C-terminal region)
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.
Antigen Affinity Purified
Polyclonal
IgG
ELISA, ICC, WB
Rabbit
TRIM63
30/38
MuRF1 (C-terminal) synthetic peptide (coupled to KLH) 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).
Human
Human, Mouse, Rat
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.
Liquid
PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
WB: 1:1000
ICC: 1:300
ICC: 1:300
Unconjugated
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.
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
United States
After date of receipt, stable for at least 1 year at -20°C.
IRF; Tripartite motif 63,TRIM63; MURF2; RNF28; SMRZ; E3 ubiquitin-protein ligase TRIM63; RING-type E3 ubiquitin transferase TRIM63; iris ring finger protein; muscle specific ring finger protein 2; muscle-specific RING finger protein 1; ring finger protein 28; striated muscle RING zinc finger protein; tripartite motif-containing protein 63; Muscle RING finger; MURF-1
Q969Q1
UniProt Summary: E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.
UniProt Summary: E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.
84676
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