|Detection of Human/Mouse/Rat MuRF1 by Western Blot. Western blot shows lysates of human heart, mouse heart, and rat muscle tissue. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human/Mouse/Rat MuRF1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5366) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). A specific band was detected for MuRF1 at approximately 41‑44 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 8.|
Detection of Human MuRF1/TRIM63 by Simple WesternTM. Simple Western lane view shows lysates of human heart tissue, loaded at 0.2 mg/mL. A specific band was detected for MuRF1/TRIM63 at approximately 46 kDa (as indicated) using 10 µg/mL of Goat Anti-Human/Mouse/Rat MuRF1/TRIM63 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5366) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the|
12-230 kDa separation system.
TRIM63 (Tripartite motif-containing protein 63; also MURF-1, SMRZ and RING finger protein 28) is a 41 kDa member of the RING finger-B-box-coiled-coil family of proteins. It is a striated muscle protein that is found in both cytoplasm and nucleus. TRIM63 has multiple finctions, among which are the inhibition of PKC epsilon -mediated cardiomyocyte hypertrophy and the maintenance of skeletal muscle M-line integrity. Human TRIM63 is 353 amino acids (aa) in length. It contains one RING finger domain (aa 23‑82), a B-Box type zinc-finger region (aa 117‑159), a coiled-coil region (aa 207‑269) and a C-terminal COS domain. Isoforms of TRIM63 show one potential alternate start site at Met14, a deletion of aa 105‑132 and a 21 aa substitution for aa 326‑353. Over aa 1‑325, human TRIM63 exhibits 93% aa identity with mouse TRIM63.
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