Human MuRF1/TRIM63 Ubiquitin Ligase Kit - S5a Substrate

  (1 citations)     
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Preparation and Storage
  • Stability & Storage
    Store the unopened product at -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date.
Background: MuRF1/TRIM63
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.
  • Long Name:
    Tripartite Motif-containing 63
  • Entrez Gene IDs:
    84676 (Human); 433766 (Mouse); 140939 (Rat)
  • Alternate Names:
    EC 6.3.2.-; IRF; IRFMURF2; Iris RING finger protein; MuRF1; MuRF-1; muscle specific ring finger protein 2; Muscle-specific RING finger protein 1; RING finger protein 28FLJ32380; RNF28; RNF28E3 ubiquitin-protein ligase TRIM63; SMRZ; SMRZMURF-1; Striated muscle RING zinc finger protein; TRIM63; tripartite motif containing 63; tripartite motif-containing 63; Tripartite motif-containing protein 63
Related Research Areas

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citations: Showing 1 - 1

  1. A high-coverage shRNA screen identifies TMEM129 as an E3 ligase involved in ER-associated protein degradation.
    Authors: van de Weijer M, Bassik M, Luteijn R, Voorburg C, Lohuis M, Kremmer E, Hoeben R, LeProust E, Chen S, Hoelen H, Ressing M, Patena W, Weissman J, McManus M, Wiertz E, Lebbink R
    Nat Commun, 2014;5(0):3832.  2014


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