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Encompassing Amino Acids: full length
Applications: Useful as an E3 ligase in ubiquitin-conjugating reactions and to analyze upregulation/downregulation of E3 enzymes.
Background: MuRF3 is a RING domain E3 ligase that is involved in the conjugation of ubiquitin to target substrates. MuRF3 has been demonstrated to function with the E2 enzyme UBE2D3 (UbcH5c) in vitro. MuRF3 is also known as TRIM54 (tripartite motif containing 54) containing a RING-finger/B-box/coiled-coil tripartite fold. MuRF3 has been implicated along with MuRF1 as regulators of protein degradation in striated muscle. MuRF3 also plays important roles in maintaining cardiac function after myocardial infarction.
Biological Activity: Typical enzyme concentration of 20-1000 nM is used for in vitro conjugation depending on assay conditions.
Description: Human MuRF3 recombinant protein (Genbank Accession No. Q9BYV2), full length with N-terminal SUMO (variant 3)- and His-tags, expressed in E. coli.
Format: Aqueous buffer solution
Formulation: 50 mM Tris, 150 mM NaCl pH 7.5, 5 mM DTT, 10% glycerol
Genbank: Q9BYV2
Purity: ≥90% by SDS-PAGE
Storage Stability: Stable for≥1 year at -80°C.
Tags: N-terminal human SUMO-His-tags
Uniprot: Q9BYV2
Warnings: Avoid freeze/thaw cycles.
Biosafety Level: Not applicable (BSL-1)
References: 1. Balasubramanian, S., et al. Enhanced ubiquitination of cytoskeletal proteins in pressure overloaded myocardium is accompanied by changes in specific E3 ligases. J. Mol. Cell Cardiol., 2006. 41(4): p. 669-79.
2. Fielitz, J., et al. Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3. J. Clin. Invest., 2007. 117(9): p. 2486-95.
3. Fielitz, J., et al. Loss of muscle-specific RING-finger 3 predisposes the heart to cardiac rupture after myocardial infarction. Proc. Natl. Acad. Sci. USA, 2007. 104(11): p. 4377-82.
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