Anti-VCP Antibody Picoband® Fluoro647 Conjugated

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.

Atherosclerosis, Cardiovascular, Hematopoietic Progenitors, Mesenchymal Stem Cells, Myeloid, Protein Phosphorylation, Receptor Tyrosine Kinases, Signal Transduction, Stem Cells, Tyrosine Kinases

Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses. .

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.