|Application ||WB, IF|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||242984 Da|
|Other Names||CAD protein, Glutamine-dependent carbamoyl-phosphate synthase, Aspartate carbamoyltransferase, Dihydroorotase, CAD|
|Target/Specificity||A synthetic peptide corresponding to residues in the N-terminus of human CAD was used as immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CAD Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||This protein is a "fusion" protein encoding four enzymatic activities of the pyrimidine pathway (GATase, CPSase, ATCase and DHOase).|
|Cellular Location||Cytoplasm. Nucleus. Note=Cytosolic and unphosphorylated in resting cells, translocates to the nucleus in response to EGF stimulation, nuclear import promotes optimal cell growth|
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Provided below are standard protocols that you may find useful for product applications.
Carbamoyl phosphate synthetase-aspartate carbamoyltransferase-dihydroorotase (CAD) is a multifunctional protein that initiates and regulates mammalian de novo pyrimidine biosynthesis (1). This trifunctional protein which is associated with the enzymatic activities of the first 3 enzymes in the 6-step pathway of pyrimidine biosynthesis is the rate-limiting step in the de novo pyrimidine synthetic pathway (2). Although most of the CAD protein in the cell is cytosolic, phosphorylation at threonine 456 localizes the protein to the nucleus (3). While MAPK and EGF phosphorylate CAD at threonine 456, MAPK and c-myc have been found to induce over-expression of CAD (4-5).
1. Chen, et al. Hum. Genet. 82: 40-44, 1989.
2. Jones, M.E. (1980) Annu. Rev. Biochem., 49, 253
3. Sigoillot, F. D., Berkowski, A. J., Sigoillot, S. M., Kotsis, D. H., and Guy, H. I. (2003) J. Biol. Chem. 278,3403
4. Evans, D. R., and Guy, H. I. (2004) J. Biol. Chem. 279,33035
5. Graves et al. (2000) Nature, 403, 328
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