Anti-DNAJC6 Antibody Picoband® Fluoro647 Conjugated

Putative tyrosine-protein phosphatase auxilin is an enzyme that in humans is encoded by the DNAJC6 gene. DNAJC6 belongs to the evolutionarily conserved DNAJ/HSP40 family of proteins, which regulate molecular chaperone activity by stimulating ATPase activity. DNAJ proteins may have up to 3 distinct domains: a conserved 70-amino acid J domain, usually at the N terminus, a glycine/phenylalanine (G/F) -rich region, and a cysteine-rich domain containing 4 motifs resembling a zinc finger domain (Ohtsuka and Hata, 2000

Cancer, Cancer Susceptibility, Cardiovascular, Domain Families, Epigenetics and Nuclear Signaling, Hlh/Leucine Zipper, Hypertrophy, Immunology, Innate Immunity, Oncoproteins, Oncoproteins/Suppressors, Proto-Oncogenes, TLR Signaling, Transcription, Transcription Factors

1. Edvardson, S., Cinnamon, Y., Ta-Shma, A., Shaag, A., Yim, Y.-I., Zenvirt, S., Jalas, C., Lesage, S., Brice, A., Taraboulos, A., Kaestner, K. H., Greene, L. E., Elpeleg, O. A deleterious mutation in DNAJC6 encoding the neuronal-specific clathrin-uncoating co-chaperone auxilin, is associated with juvenile parkinsonism. PLoS One 7: e36458, 2012. Note: Electronic Article. 2. Elsayed, L. E. O., Drouet, V., Usenko, T., Mohammed, I. N., Hamed, A. A. A., Elseed, M. A., Salih, M. A. M., Koko, M. E., Mohamed, A. Y. O., Siddig, R. A., Elbashir, M. I., Ibrahim, M. E., Durr, A., Stevanin, G., Lesage, S., Ahmed, A. E., Brice, A. A novel nonsense mutation in DNAJC6 expands the phenotype of autosomal-recessive juvenile-onset Parkinson's disease. (Letter) Ann. Neurol. 79: 335-338, 2016. 3. Fotin, A., Cheng, Y., Grigorieff, N., Walz, T., Harrison, S. C., Kirchhausen, T. Structure of an auxilin-bound clathrin coat and its implications for the mechanism of uncoating. Nature 432: 649-653, 2004.