Anti-VCP Antibody Picoband®

Valosin-containing protein also called CDC48 is an enzyme that in humans is encoded by the VCP gene. It is a member of the AAA+ (ATPase associated with various activities) protein family. The VCP gene maps to chromosome 9p13.3. It is necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. It is involved in the formation of the transitional endoplasmic reticulum. This gene plays a role in vesicle transport and fusion, 26S proteasome function, and assembly of peroxisomes. It also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites.

Cerebral white matter and plasma. Isoform V0 and isoform V1 are expressed in normal brain, gliomas, medulloblastomas, schwannomas, neurofibromas, and meningiomas. Isoform V2 is restricted to normal brain and gliomas. Isoform V3 is found in all these tissues except medulloblastomas.

ER Proteins, Metabolism, Mitochondrial Markers, Mitochondrial Metabolism, Neurodegenerative Disease, Neurology Process, Neuroscience, Pathways and Processes, Protein Trafficking, Signal Transduction

Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER) . The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER) . Vesicle budding from the tER is an ATP-dependent process. The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1L-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope. Regulates E3 ubiquitin-protein ligase activity of RNF19A. Component of the VCP/p97-AMFR/gp78 complex that participates in the final step of the sterol-mediated ubiquitination and endoplasmic reticulum-associated degradation (ERAD) of HMGCR. Also involved in DNA damage response: recruited to double-strand breaks (DSBs) sites in a RNF8- and RNF168-dependent manner and promotes the recruitment of TP53BP1 at DNA damage sites. Recruited to stalled replication forks by SPRTN: may act by mediating extraction of DNA polymerase eta (POLH) to prevent excessive translesion DNA synthesis and limit the incidence of mutations induced by DNA damage. Required for cytoplasmic retrotranslocation of stressed/damaged mitochondrial outer-membrane proteins and their subsequent proteasomal degradation. .

1. Custer, S. K., Neumann, M., Lu, H., Wright, A. C., Taylor, J. P. Transgenic mice expressing mutant forms VCP recapitulate the full spectrum of IBMPFD including degeneration in muscle, brain and bone. Hum. Molec. Genet. 19: 1741-1755, 2010. 2. Haubenberger, D., Bittner, R. E., Rauch-Shorny, S., Zimprich, F., Mannhalter, C., Wagner, L., Mineva, I., Vass, K., Auff, E., Zimprich, A. Inclusion body myopathy and Paget disease is linked to a novel mutation in the VCP gene. Neurology 65: 1304-1305, 2005. 3. Mueller, B., Klemm, E. J., Spooner, E., Claessen, J. H., Ploegh, H. L. SEL1L nucleates a protein complex required for dislocation of misfolded glycoproteins. Proc. Nat. Acad. Sci. 105: 12325-12330, 2008. 4. Sacconi, S., Camano, P., de Greef, J. C., Lemmers, R. J. L. F., Salviati, L., Boileau, P., Lopez de Munain Arregui, A., van der Maarel, S. M., Desnuelle, C. Patients with a phenotype consistent with facioscapulohumeral muscular dystrophy display genetic and epigenetic heterogeneity. J. Med. Genet. 49: 41-46, 2012.

Store 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 freeze-thaw cycles.

Cytoplasm, cytosol. Endoplasmic reticulum. Nucleus. Present in the neuronal hyaline inclusion bodies specifically found in motor neurons from amyotrophic lateral sclerosis patients. Present in the Lewy bodies specifically found in neurons from Parkinson disease patients. Recruited to the cytoplasmic surface of the endoplasmic reticulum via interaction with AMFR/gp78. Following DNA double-strand breaks, recruited to the sites of damage. Recruited to stalled replication forks via interaction with SPRTN.