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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: MuRF1 (Muscle-specific RING-finger protein 1) is an E3 (ubiquitin protein ligase) that is involved in the conjugation of ubiquitin to target substrates along with E1 and E2 enzymes. MuRF1 is also known as TRIM63 (tripartite motif containing 63) containing a RING-finger/B-box/coiled-coil tripartite fold and is a member of the RING-domain E3 family. MuRF1 has been implicated as a component of atrophy-associated accelerated proteolysis. It is upregulated in a number of different models of atrophy and interacts with numerous myofibrillar proteins.
Biological Activity: Typical enzyme concentration of 100 nM - 5 mM is used for in vitro conjugation, depending on conditions.
Description: Human MuRF1 recombinant protein (Genbank Accession No. NP_115977), 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: NP_115977
Purity: ≥90% by SDS-PAGE
Storage Stability: Stable for≥1 year at -80°C.
Tags: N-terminal human SUMO-His-tags
Uniprot: Q969Q1
Warnings: Avoid freeze/thaw cycles.
Biosafety Level: Not applicable (BSL-1)
References: 1. Bodine, S.C., et al., Identification of ubiquitin ligases required for skeletal muscle atrophy. Science , 2001. 294:1704-8.
2. Centner, T., et al., Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain. J Mol Biol. 2001. 306:717-26.
3. Kedar, V., et al., Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I. Proc Natl Acad Sci USA, 2004. 101:18135-40.
4. Mrosek, M., et al., Molecular determinants for the recruitment of the ubiquitin-ligase MuRF-1 onto M-line titin. FASEB J. 2007. 21:1383-92.
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