Recombinant Human His6-MuRF1/TRIM63 Protein, CF
Recombinant Human His6-MuRF1/TRIM63 Protein, CF Summary
Product Specifications
Contains an N-terminal 6-His tag
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
E3-100
| Formulation | X mg/ml (X μM) in 50 mM HEPES pH 8.0, 100 mM NaCl, 10% Glycerol |
| Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: Synapsin I
Muscle-specific RING-finger Protein 1 (MuRF1), also known as TRIM63, is a Ubiquitin ligase (E3) and a member of a family of tripartite motif proteins that also includes MuRF2/TRIM55 and MuRF3/TRIM54. Human MuRF1/TRIM63 is 353 amino acids (aa) in length and has a predicted mass of 40 kDa. The human aa sequence is approximately 90% identical to the mouse and rat orthologs. MuRF1/TRIM63 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 (1,2). It is expressed primarily in striated muscle and evidence suggests MuRF1/TRIM63 has the ability to target many sarcomeric proteins for ubiquitination and proteasomal degradation. Some targeted proteins include Actin, Myosin-binding Protein C, and Myosin Light Chains 1 and 2 (3,4). MuRF1/TRIM63 has been implicated in muscle atrophy associated with chronic disease and inactivity (5).
- Wang, T. et al. (2009) J. Mol. Biol. 386:1011.
- Nakada, S. et al. (2010) Nature 466:941.
- Wiener, R. et al. (2012) Nature 483:618.
- Sato, Y. et al. (2012) J. Biol. Chem. 287:25860.
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