Anti-CLPB Antibody Picoband® Fluoro594 Conjugated

This gene belongs to the ATP-ases associated with diverse cellular activities (AAA+) superfamily. Members of this superfamily form ring-shaped homo-hexamers and have highly conserved ATPase domains that are involved in various processes including DNA replication, protein degradation and reactivation of misfolded proteins. All members of this family hydrolyze ATP through their AAA+ domains and use the energy generated through ATP hydrolysis to exert mechanical force on their substrates. In addition to an AAA+ domain, the protein encoded by this gene contains a C-terminal D2 domain, which is characteristic of the AAA+ subfamily of Caseinolytic peptidases to which this protein belongs. It cooperates with Hsp70 in the disaggregation of protein aggregates. Allelic variants of this gene are associated with 3-methylglutaconic aciduria, which causes cataracts and neutropenia. Alternative splicing results in multiple transcript variants.

Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) . Has a low GTPase activity. Involved in COPI-independent retrograde transport from the Golgi to the ER (PubMed:25962623) .

1. Capo-Chichi, J.-M., Boissel, S., Brustein, E., Pickles, S., Fallet-Bianco, C., Nassif, C., Patry, L., Dobrzeniecka, S., Liao, M., Labuda, D., Samuels, M. E., Hamdan, F. F., Vande Velde, C., Rouleau, G. A., Drapeau, P., Michaud, J. L. Disruption of CLPB is associated with congenital microcephaly, severe encephalopathy and 3-methylglutaconic aciduria. J. Med. Genet. 52: 303-311, 2015. 2. Haslberger, T., Zdanowicz, A., Brand, I., Kirstein, J., Turgay, K., Mogk, A., Bukau, B. Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Nature Struct. Molec. Biol. 15: 641-650, 2008. 3. Saunders, C., Smith, L., Wibrand, F., Ravn, K., Bross, P., Thiffault, I., Christensen, M., Atherton, A., Farrow, E., Miller, N., Kingsmore, S. F., Ostergaard, E. CLPB variants associated with autosomal-recessive mitochondrial disorder with cataract, neutropenia, epilepsy, and methylglutaconic aciduria. Am. J. Hum. Genet. 96: 258-265, 2015.