PhosphoSolutions

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Western blot analysis of A431 cells treated with calyculin A (100 nM) for 30 min (lane 1 and 2) then treated with lambda phosphatase (lane 3). The blot was probed with anti-Phosphoserine/threonine mouse monoclonal at 1:250 (lane 1) or 1:1000 (lanes 2 & 3).Immunocytochemical labeling of phosphoserine and phosphothreonine in control and calyculin A-treated A431 cells. The cells were labeled with mouse monoclonal anti-Phosphoserine/threonine (PM3801) and rabbit polyclonal anti-Phosphoserine/threonine (PP2551), then the antibodies were detected using appropriate secondary antibodies conjugated to Cy3.
Western blot analysis of A431 cells treated with calyculin A (100 nM) for 30 min (lane 1) then treated with lambda phosphatase (lane 2). The blot was probed with anti-Phosphoserine/threonine rabbit polyclonal at 1:1000.Bar graph showing anti-Phosphoserine/threonine (PP2551) binding to a variety of phosphoserine and phosphothreonine peptides, but not control peptide containing unphosphorylated serine or phosphotyrosine.
Western blot of human A431 cells treated with Calyculin A (100 nM) for 30 min. The blot was untreated (lane 1) or treated with lambda phosphatase (lanes 2), then probed with anti-Phosphothreonine (PP4641) at 1:1000.Immunocytochemical labeling of phosphothreonine upregulation in control (left) or calyculin A-treated HeLa cells (right). The cells were labeled with rabbit polyclonal anti-Phosphothreonine (PP4641). The antibody was detected using goat anti-rabbit DyLight® 594.
Western blot of HeLa cells treated with pervanadate (1 mM) for 30 min. Phosphotyrosine containing proteins were immunoprecipitated with rabbit polyclonal anti-Phosphotyrosine:Agarose (Lane 1) or with no antibody agarose beads (Lane 2), and blots were made that included the whole lysate (Lane 3). The blots were probed with mouse monoclonal anti-Phosphotyrosine (PM3751) to detect phosphotyrosine containing proteins.Immunocytochemical labeling of phosphotyrosine in control and pervanadate-treated A431 cells. The cells were labeled with rabbit polyclonal anti-Phosphotyrosine (PP2221) and mouse monoclonal anti-Phosphotyrosine (PM3751), then the antibodies were detected using appropriate secondary antibodies conjugated to Cy3.
Bar graph showing rabbit polyclonal anti-Phosphotyrosine (PP2221) binding to a variety of phosphotyrosine containing peptides, but no binding to unphosphorylated peptide (beta-Catenin (a.a. 29-45).Immunocytochemical labeling of phosphotyrosine in control and pervanadate-treated A431 cells. The cells were labeled with rabbit polyclonal anti-Phosphotyrosine (PP2221) and mouse monoclonal anti-Phosphotyrosine (PM3751), then the antibodies were detected using appropriate secondary antibodies conjugated to Cy3.
Simple Western of HeLa lysate showing specific immunolabeling of the ~ 56 kDa PINK1 protein.  Western Blot of C-terminally V5His-tagged human PINK1 or N-terminally myc-tagged human PINK1 expressed in HEK293T cells showing specific immunolabeling of PINK1.
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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