Anti-ORC1 Antibody Picoband® Fluoro488 Conjugated

Origin recognition complex subunit 1 is a protein that in humans is encoded by the ORC1 gene. The origin recognition complex (ORC) is a highly conserved six subunits protein complex essential for the initiation of the DNA replication in eukaryotic cells. Studies in yeast demonstrated that ORC binds specifically to origins of replication and serves as a platform for the assembly of additional initiation factors such as Cdc6 and Mcm proteins. The protein encoded by this gene is the largest subunit of the ORC complex. While other ORC subunits are stable throughout the cell cycle, the levels of this protein vary during the cell cycle, which has been shown to be controlled by ubiquitin-mediated proteolysis after initiation of DNA replication. This protein is found to be selectively phosphorylated during mitosis. It is also reported to interact with MYST histone acetyltransferase 2 (MyST2/HBO1), a protein involved in control of transcription silencing. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.

Isoform 1 is predominantly expressed in thymus and is also found in peripheral blood leukocytes and kidney. Isoform 2 is predominantly expressed in skeletal muscle and is also found in thymus, kidney, testis, spleen, prostate, ovary, small intestine, heart, placenta and pancreas. Isoform 3 is expressed in thymus and kidney. Isoform 4 is expressed in thymus and skeletal muscle.

The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to the release of inositol trisphosphate (IP3) ; this then triggers calcium ion release into the cytosol. .

1. Bicknell, L. S., Bongers, E. M. H. F., Leitch, A., Brown, S., Schoots, J., Harley, M. E., Aftimos, S., Al-Aama, J. Y., Bober, M., Brown, P. A. J., van Bokhoven, H., Dean, J., and 15 others. Mutations in the pre-replication complex cause Meier-Gorlin syndrome. Nature Genet. 43: 356-359, 2011. 2. Bicknell, L. S., Walker, S., Klingseisen, A., Stiff, T., Leitch, A., Kerzendorfer, C., Martin, C.-A., Yeyati, P., Al Sanna, N., Bober, M., Johnson, D., Wise, C., Jackson, A. P., O'Driscoll, M., Jeggo, P. A. Mutations in ORC1, encoding the largest subunit of the origin recognition complex, cause microcephalic primordial dwarfism resembling Meier-Gorlin syndrome. Nature Genet. 43: 350-355, 2011. 3. Bongers, E. M. H. F., Opitz, J. M., Fryer, A., Sarda, P., Hennekam, R. C. M., Hall, B. D., Superneau, D. W., Harbison, M., Poss, A., van Bokhoven, H., Hamel, B. C. J., Knoers, N. V. A. M. Meier-Gorlin syndrome: report of eight additional cases and review. Am. J. Med. Genet. 102: 115-124, 2001.

Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Phosphorylation in response to agonist binding promotes receptor internalization. .