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Western blot analysis of PKC isoforms in adult mouse brain lysate. The blot was probed with mouse monoclonal anti-PKC (α,β,γ) clone M499 at 1:250 (lane 1) and 1:1000 (lane 2).
Western blot analysis of immunoprecipitates from neonatal rat brain lysate using anti-PKCα antibody. Control and alkaline phosphatase treated precipitates were probed with anti-PKCα (Central region) or anti-phospho-PKCα (Ser-657/Tyr-658). The latter shows no detection of PKCα after phosphatase treatment.Formalin fixed, citric acid treated parafin sections of adult mouse brain. Sections were probed with anti-PKCα (PM2371) then anti-mouse:HRP before detection using DAB. (Image provided by Carl Hobbs and Dr. Pat Doherty at Wolfson Centre for Age-Related Diseases, King's College London).
Western blot analysis of adult mouse brain tissue lysate. The blot was probed with mouse monoclonal anti-PKCδ (N-terminal region) at 1:125 (lane 1) and 1:500 (lane 2).Immunocytochemical labeling of PKCδ in rat PC12 cells differentiated with NGF. The cells were labeled with mouse monoclonal PKCδ (N-terminal region) antibody, then detected using appropriate secondary antibody conjugated to Cy3.
Western blot analysis of  PKCθ in human Jurkat cell lysate. The blot was probed with anti-PKCθ at 1:250 (lane 1) and 1:1000 (lane 2).Immunocytochemical labeling of PKCθ in rat PC12 cells differentiated with NGF. The cells were labeled with mouse monoclonal PKCθ (N-terminal region) antibody, then detected using appropriate secondary antibody conjugated to Cy3.
Western blot analysis of PLCγ1 immunoprecipitates from human jurkat cells untreated (lanes 1 & 3) or treated with pervanadate (1 mM) for 30 min (lanes 2,4,5,6). Immunoprecipitation was performed with anti-PLCγ1 (PM1561). The blots were probed with anti-PLCγ1 (lanes 1 & 2) and anti-PLCγ1 (Tyr-775) (lanes 3-6). The latter antibody was used in the presence of phospho- PLCγ1 (Tyr-775) peptide (lane 5), or unrelated phosphotyrosine peptide (lane 6).Immunocytochemical labeling of PLCγ1 in adelhyde-fixed and NP-40 permeabilized human MDA-MB-231 breast carcinoma cells. The cells were labeled with mouse monoclonal anti-PLCγ1 (PM1561) antibody. The antibody was detected using appropriate secondary antibody conjugated to DyLight® 594.
Western blots showing Cos-7 cells transfected with mouse Myc-tagged Plexin-A1 (lanes 1 & 3), neonatal rat brain (lane 2), or Plexin-A1 immunoprecipitated from Myc-tagged Plexin-A1 transfected cells using anti-Myc (lane 4) or anti-Plexin-A1 (PP1301; lane 5). These blots were probed with either the affinity purified anti-Plexin-A1 (PP1301; lanes 1 & 2) or with mouse monoclonal anti-Myc (lanes 3-5).Immunocytochemical double labeling using anti-Myc mouse monoclonal and anti-Plexin-A1 rabbit polyclonal (PP1301) antibodies in Cos-7 cells mock transfected (A,D) or transfected with Myc-tagged mouse Plexin-A1 construct (B,E). The specificity of the binding in E was demonstrated by using Plexin-A1 peptide (PX1305) in the presence of this anti-Plexin-A1 antibody (C,F).
Western blots showing mouse recombinant Plexin-A1 extracellular domain (lanes 1-4). These blots were probed with rabbit polyclonal anti-Plexin-A1 (PP1301) at 1:250 (lane 1) and 1:1000 (lane 2) or with mouse monoclonal anti-Plexin A1 (PM5351) at 1:250 (lane 3) and 1:1000 (lane 4).Immunocytochemical labeling of Plexin A1 in aldehyde fixed and NP-40 permeabilized human NCI-H1299 lung carcinoma cells. The cells were labeled with mouse monoclonal anti-Plexin A1 (PM5351). The antibody was detected using goat anti-mouse DyLight® 594.
Western blots showing mouse brain (lanes 1 & 4), and Cos-7 cells untransfected (lanes 2 & 5) or transfected with mouse myc-tagged Plexin-A1 (lanes 3 & 6). The blots were probed with either affinity purified anti-Plexin-A1 (PP1471); lanes 1-3) or with mouse monoclonal anti-Myc (lanes 4-6).Immunocytochemical double labeling using anti-Myc mouse monoclonal and anti-Plexin-A1 rabbit polyclonal (PP1471) antibodies in Cos-7 cells mock transfected (A,D) or transfected with Myc-tagged mouse Plexin-A1 construct (B,E). The specificity of the binding in E was demonstrated by using Plexin-A1 peptide (PX1475) in the presence of this anti-Plexin-A1 antibody (C,F).
Western blot analysis of Plexin D1 expression in human endothelial cells (HUVEC) (lanes 1-6). The blots were probed with rabbit polyclonals anti-Plexin D1 (Sema domain) (lanes 1 & 2), anti-Plexin D1 (Cytoplasmic domain) (lanes 3 & 4), and anti-Plexin D1 (a.a. 1635-1647) (lanes 5 & 6). Each antibody was used in the presence of their respective blocking peptide (lanes 2, 4 & 6).

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