Anti-TRIM2 Antibody Picoband®

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The protein localizes to cytoplasmic filaments. It plays a neuroprotective role and functions as an E3-ubiquitin ligase in proteasome-mediated degradation of target proteins. Mutations in this gene can cause early-onset axonal neuropathy. Alternative splicing results in multiple transcript variants.

E.coli-derived human TRIM2 recombinant protein (Position: Q78-E398) . Human TRIM2 shares 99.4% and 98.8% amino acid (aa) sequence identity with mouse and rat TRIM2, respectively.

1. Balastik, M., Ferraguti, F., Pires-da Silva, A., Lee, T. H., Alvarez-Bolado, G., Lu, K. P., Gruss, P. Deficiency in ubiquitin ligase TRIM2 causes accumulation of neurofilament light chain and neurodegeneration. Proc. Nat. Acad. Sci. 105: 12016-12021, 2008. 2. Nagase, T., Ishikawa, K., Miyajima, N., Tanaka, A., Kotani, H., Nomura, N., Ohara, O. Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 5: 31-39, 1998. 3. Pehlivan, D., Coban Akdemir, Z., Karaca, E., Bayram, Y., Jhangiani, S., Yildiz, E. P., Muzny, D., Uluc, K., Gibbs, R. A., Baylor-Hopkins Center for Mendelian Genomics, Elcioglu, N., Lupski, J. R., Harel, T. Exome sequencing reveals homozygous TRIM2 mutation in a patient with early onset CMT and bilateral vocal cord paralysis. Hum. Genet. 134: 671-673, 2015.

At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing.