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Western blot of human Jurkat cells treated with calyculin A (100 nM) for 30 min. The blots were untreated (lanes 1 & 3) or treated (lanes 2 & 4) with lambda phosphatase and probed with anti-B-Raf (N-terminus) (lanes 1 & 2) or anti-B-Raf (Ser-446) (lanes 3 & 4).
Western blot of human Jurkat cell lysate. The blot was probed with mouse monoclonal anti-A-Raf (N-terminal region) antibody at 1:500 (lane 1) and 1:2000 (lane 2).
Western blot analysis of mouse brain. The blot was probed with anti-PYK2 (C-terminal region) antibody at 1:250 (lane 1), 1:500 (lane 2), 1:1000 (lane 3), and 1:2000 (lane 4).
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.

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