Anti-USP9X Antibody Picoband® Fluoro647 Conjugated

Probable ubiquitin carboxyl-terminal hydrolase FAF-X is an enzyme that in humans is encoded by the USP9X gene. This gene is a member of the peptidase C19 family and encodes a protein that is similar to ubiquitin-specific proteases. Though this gene is located on the X chromosome, it escapes X-inactivation. Mutations in this gene have been associated with Turner syndrome. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.

Disintegrin and metalloproteinase domain-containing protein 15; ADAM 15; Metalloprotease RGD disintegrin protein; Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15; MDC-15; Metargidin; ADAM15; MDC15

Expressed in colon and small intestine. Expressed in airway smooth muscle and glomerular mesangial cells (at protein level) . Ubiquitously expressed. Overexpressed in atherosclerotic lesions. Constitutively expressed in cultured endothelium and smooth muscle. Expressed in chondrocytes. Expressed in airway smooth muscle and glomerular mesangial cells.

Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration. Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain.

1. Homan, C. C., Kumar, R., Nguyen, L. S., Haan, E., Raymond, F. L., Abidi, F., Raynaud, M., Schwartz, C. E., Wood, S. A., Gecz, J., Jolly, L. A. Mutations in USP9X are associated with X-linked intellectual disability and disrupt neuronal cell migration and growth. Am. J. Hum. Genet. 94: 470-478, 2014. 2. Jones, M. H., Furlong, R. A., Burkin, H., Chalmers, I. J., Brown, G. M., Khwaja, O., Affara, N. A. The Drosophila developmental gene fat facets has a human homologue in Xp11.4 which escapes X-inactivation and has related sequences on Yq11.2. Hum. Molec. Genet. 5: 1695-1701, 1996. Note: Erratum: Hum. Molec. Genet. 6: 334-335, 1997. 3. Perez-Mancera, P. A., Rust, A. G., van der Weyden, L., Kristiansen, G., Li, A., Sarver, A. L., Silverstein, K. A. T., Grutzmann, R., Aust, D., Rummele, P., Knosel, T., Herd, C., and 25 others. The deubiquitinase USP9X suppresses pancreatic ductal adenocarcinoma. Nature 486: 266-270, 2012. Note: Erratum: Nature 494, 390 only, 2013.