Anti-PCYOX1 Antibody Picoband® Fluoro488 Conjugated

Prenylcysteine oxidase 1 is an enzyme that in humans is encoded by the PCYOX1 gene. Prenylcysteine is released during the degradation of prenylated proteins. PCYOX1 catalyzes the degradation of prenylcysteine to yield free cysteines and a hydrophobic isoprenoid product.

70 kDa ribosomal protein S6 kinase 1 antibody, KS6B1_HUMAN antibody, p70 alpha antibody, P70 beta 1 antibody, p70 ribosomal S6 kinase alpha antibody, p70 ribosomal S6 kinase beta 1 antibody, p70 S6 kinase alpha antibody, P70 S6 Kinase antibody, p70 S6 kinase alpha 1 antibody, p70 S6 kinase alpha 2 antibody, p70 S6K antibody, p70 S6K-alpha antibody, p70 S6KA antibody, p70 (S6K) alpha antibody, p70 (S6K) -alpha antibody, p70-alpha antibody, p70-S6K 1 antibody, p70-S6K antibody, P70S6K antibody, P70S6K1 antibody, p70S6Kb antibody, PS6K antibody, Ribosomal protein S6 kinase 70kDa polypeptide 1 antibody, Ribosomal protein S6 kinase beta 1 antibody, Ribosomal protein S6 kinase beta-1 antibody, Ribosomal protein S6 kinase I antibody, RPS6KB1 antibody, S6K antibody, S6K-beta-1 antibody, S6K1 antibody, Serine/threonine kinase 14 alpha antibody, Serine/threonine-protein kinase 14A antibody, STK14A antibody

E.coli-derived human PCYOX1 recombinant protein (Position: R101-D452) . Human PCYOX1 shares 78.7% and 76.1% amino acid (aa) sequence identity with mouse and rat PCYOX1, respectively.

Downstream effector of TOR signaling pathway involved in osmotic stress response. Could be involved in the control of plant growth and development. Phosphorylates the ribosomal proteins P14, P16 and S6. Functions as a repressor of cell proliferation and required for maintenance of chromosome stability and ploidy levels through the RBR1-E2F pathway.

1. Nagase, T., Ishikawa, K., Suyama, M., Kikuno, R., Hirosawa, M., Miyajima, N., Tanaka, A., Kotani, H., Nomura, N., Ohara, O. Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 5: 355-364, 1998. 2. Tschantz, W. R., Zhang, L., Casey, P. J. Cloning, expression, and cellular localization of a human prenylcysteine lyase. J. Biol. Chem. 274: 35802-35808, 1999.