Phospholipase C β₂ Polyclonal Antibody

Phospholipase C β2 (PLCβ2) is an enzyme that catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate to the secondary messengers inositol 1,4,5-triphosphate (IP₃) and diacylglycerol (DAG).^1,2 It is approximately 135 kDa and is composed of a pleckstrin homology domain, four EF-hand motifs, a catalytic domain, and a C2 domain that are common to all PLCs, as well as a 400-amino acid C-terminal region that is required for PLCβ2 activation by the G-protein subunits Gα_q or Gα₁₁.³ PLCβ2 is also activated by Gβγ subunits. Upon activation by a G-protein subunit, PLCβ2 initiates intracellular signal transduction of extracellular signals using calcium as a cofactor. PLCβ2 colocalizes with T1R and T2R taste receptors and Plcb2^-/- mice exhibit selective and complete loss of sweet, amino acid, and bitter tastes.⁴ Plcb2^-/- mice also exhibit increased coxsackievirus A16-induced pro-inflammatory cytokine production and decreased survival compared with wild-type mice.⁵ Cayman's Phospholipase C β2 Polyclonal Antibody can be used for immunohistochemistry (IHC) and immunofluorescence (IF) applications.

WARNING This product is not for human or veterinary use.

1. Romoser, V., Ball, R., and Smrcka, A.V. Phospholipase C β₂ association with phospholipid interfaces assessed by fluorescence resonance energy transfer. G protein βγ subunit-mediated translocation is not required for enzyme activation. The Journal of Biological Chemisty 271(41), 25071-25078 (1996).

2. Drin, G., and Scarlata, S. Stimulation of phospholipase Cβ by membrane interactions, interdomain movement, and G protein binding - How many ways can you activate an enzyme? Cell Signal. 19(7), 1383-1392 (2007).

3. Zhang, W., and Neer, E.J. Reassembly of phospholipase C-β₂ from separated domains: analysis of basal and G protein-stimulated activities. The Journal of Biological Chemisty 276(4), 2503-2508 (2001).

4. Zhang, Y., Hoon, M.A., Chandrashekar, J., et al. Coding of sweet, bitter, and umami tastes: Different receptor cells sharing similar signaling pathways. Cell 112(3), 293-301 (2003).

5. Wang, L., Zhou, Y., Chen, Z., et al. PLCβ₂ negatively regulates the inflammatory response to virus infection by inhibiting phosphoinositide-mediated activation of TAK1. Nat. Commun. 10(1), 746 (2019).