Anti-MURF1/TRIM63 Antibody Picoband®, APC Conjugate

E3 ubiquitin-protein ligase TRIM63 is an enzyme that in humans is encoded by the TRIM63 gene. This gene encodes a member of the RING zinc finger protein family found in striated muscle and iris. The product of this gene is an E3 ubiquitin ligase that localizes to the Z-line and M-line lattices of myofibrils. This protein plays an important role in the atrophy of skeletal and cardiac muscle and is required for the degradation of myosin heavy chain proteins, myosin light chain, myosin binding protein, and for muscle-type creatine kinase.

E3 ubiquitin-protein ligase which ubiquitinates MYC and inhibits its transcription activation activity, maintaining the pluripotency of embryonic stem cells. Involved in the synthesis of unanchored K48-linked polyubiquitin chains which interact with and activate the serine/threonine kinase IKBKE, leading to phosphorylation of STAT1 and stimulation of an antiviral response .

1. Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., Pan, Z.-Q., Valenzuela, D. M., DeChiara, T. M., Stitt, T. N., Yancopoulos, G. D., Glass, D. J. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 294: 1704-1708, 2001. 2. Cai, D., Frantz, J. D., Tawa, N. E., Jr., Melendez, P. A., Oh, B.-C., Lidov, H. G. W., Hasselgren, P.-O., Frontera, W. R., Lee, J., Glass, D. J., Shoelson, S. E. IKK-beta/NF-kappa-B activation causes severe muscle wasting in mice. Cell 119: 285-298, 2004. 3. Centner, T., Yano, J., Kimura, E., McElhinny, A. S., Pelin, K., Witt, C. C., Bang, M.-L., Trombitas, K., Granzier, H., Gregorio, C. C., Sorimachi, H., Labeit, S. Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain. J. Molec. Biol. 306: 717-726, 2001.

Store at -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freeze-thaw cycles.