Phospholipase C β2 (PLC β2) Antibody
Phospholipases are quite common enzymes that are present in a broad range of organisms, including bacteria, yeast, plants, animals, and viruses. Phospholipase C (PLC) constitutes a class of enzymes that cleave phospholipids on the diacylglycerol (DAG) side of the phosphodiester bond (Cocco et al., 2015). A growing body of evidence supports the role of phospholipase C (PLC) in the invasion and metastasis of different tumors, including breast cancer (Bertagnolo et al., 2006). PLC-β2 has been shown to be required for sweet, umami and bitter taste perception in mammals (Zhang et al., 2003). Data also suggests that PLC-β2 serves an unappreciated role assembling components of the p38MAPK signaling module (Barr et al., 2002).
Check out our PLC β2 antibody! Designed, purified, and characterized by PhosphoSolutions’ scientists, our PLC β2 antibody is an excellent marker for human taste cells.
|Phospholipase C β2 (PLC β2) Antibody||Rabbit Polyclonal, Affinity Purified||25 or 100 uL||1640-PLC||$109 – $365|
- Cocco L, Follo MY, Manzoli L, Suh PG. (2015) Phosphoinositide-specific phospholipase C in health and disease. J Lipid Res. (10):1853-60.
- Bertagnolo V, Benedusi M, Querzoli P, Pedriali M, Magri E, Brugnoli F, Capitani S. (2006) PLC-beta2 is highly expressed in breast cancer and is associated with a poor outcome: a study on tissue microarrays. Int J Oncol. (4):863-7
- Zhang, Y., Hoon, M. A., Chandrashekar, J., Mueller, K. L., Cook, B., Wu, D., Ryba, N. J. P. (2003) Coding of Sweet, Bitter, and Umami Tastes. Cell, 112(3), 293–301.
- Barr AJ, Marjoram R,Xu J, Snyderman R. (2002) Phospholipase C-2 interacts with mitogen-activated protein kinase kinase 3. Biochem Biophys Res Commun. (1):647-52.