Cell Signaling Technology

Product Pathways - Ca / cAMP / Lipid Signaling

Phospho-PLCbeta3 (Ser537) (D8K2R) Rabbit mAb #29021

No. Size Price
29021S 100 µl ( 10 western blots ) ¥4,050.00 现货查询 购买询价 防伪查询
29021 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat, Endogenous 150 Rabbit IgG

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting,

Specificity / Sensitivity

Phospho-PLCbeta3 (Ser537) (D8K2R) Rabbit mAb recognizes endogenous levels of total PLCbeta3 only when phosphorylated at Ser537. The antibody cross-reacts with a murine protein of ~75 kDa whose identity was not determined.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser537of human PLCβ3 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from HeLa cells untreated (-) or treated with anisomycin (20 μg/ml for 15 min, +), or λ phosphatase-treated (+), using Phospho-PLCbeta3 (Ser537) (D8K2R) Rabbit mAb (upper), or α-Actinin (D6F6) XP® Rabbit mAb #6487 (lower).

Background

Phosphoinositide-specific phospholipase C (PLC) plays a significant role in transmembrane signaling. In response to extracellular stimuli such as hormones, growth factors and neurotransmitters, PLC hydrolyzes phosphatidylinositol 4,5-bisphosphate (PIP2) to generate two secondary messengers: inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG) (1). At least four families of PLCs have been identified: PLCβ, PLCγ, PLCδ and PLCε. The PLCβ subfamily includes four members, PLCβ1-4. All four members of the subfamily are activated by α- or β-γ-subunits of the heterotrimeric G-proteins (2,3).

Phosphorylation is one of the key mechanisms that regulates the activity of PLC. Phosphorylation of Ser1105 by PKA or PKC inhibits PLCβ3 activity (4,5). Ser537 of PLCβ3 is phosphorylated by CaMKII, and this phosphorylation may contribute to the basal activity of PLCβ3. PLCγ is activated by both receptor and nonreceptor tyrosine kinases (6).

PLCγ forms a complex with EGF and PDGF receptors, which leads to the phosphorylation of PLCγ at Tyr771, 783 and 1245 (7). Phosphorylation by Syk at Tyr783 activates the enzymatic activity of PLCγ1 (8).

  1. Singer, W.D. et al. (1997) Annu Rev Biochem 66, 475-509.
  2. Smrcka, A.V. et al. (1991) Science 251, 804-7.
  3. Taylor, S.J. et al. (1991) Nature 350, 516-8.
  4. Yue, C. et al. (1998) J Biol Chem 273, 18023-7.
  5. Yue, C. et al. (2000) J Biol Chem 275, 30220-5.
  6. Margolis, B. et al. (1989) Cell 57, 1101-7.
  7. Kim, H.K. et al. (1991) Cell 65, 435-41.
  8. Wang, Z. et al. (1998) Mol Cell Biol 18, 590-7.

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