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Western blot image of mouse SYF cSrc-transformed cells untreated (lanes 1 & 3) or treated (lanes 2 & 4) with pervanadate (1 mM for 30 min.). The blots were probed with rabbit polyclonal anti-PTP1B (a.a. 146-157) (lanes 1 & 2) or anti-PTP1B (Tyr-152) (lanes 3 & 4).Immunocytochemical labeling of PTP1B in aldehyde-fixed and NP-40 permeabilized human NCI-H1915 lung carcinoma cells. The cells were labeled with rabbit polyclonal anti-PTP1B (PP2351) antibody. The antibody was detected using appropriate secondary antibody
conjugated to DyLight® 594.
Western blot image of human Jurkat cells untreated (lanes 1 & 3) or treated (lanes 2 & 4) with calyculin A (100 nM for 30 min.). The blots were probed with mouse monoclonal anti-PTP1B (lanes 1 & 2) or rabbit polyclonal anti-PTP1B (Ser-50) (lanes 3 & 4).Immunocytochemical labeling of PTP1B in methanol and acetone fixed human NCI-H1915 lung carcinoma cells. The cells were labeled with mouse monclonal anti-PTP1B (PM2341) antibody. The antibody was detected using appropriate secondary antibody conjugated to DyLight® 594.
Western blot of GST recombinant human full-length prion protein that was untreated (lanes 1 and 3) or phosphorylated with Cdk5/p25 (lanes 2 & 4). Endogenous prion phosphorylation was examined in human PC3 cells untreated (lanes 5 & 7) or treated with Calyculin A (100 nM) for 30 min (lanes 6 & 8). The blots were probed with anti-Prion protein (3F4) (lanes 1, 2, 5, & 6) or anti-Prion protein (Ser-43) (lanes 3, 4, 7, & 8).
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).
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 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 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 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 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 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 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).

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