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Western blot analysis of WWP1 expression in adult mouse liver (lane 1) and human prostate adenocarcinoma (PC3) cells (lane 2). The blot was probed with anti-WWP1 (WP3931) at 1:1000.
Western blot of rat PC12 lysate. The blots were probed with anti-WAVE2 (Central region) in the presence (lane 2) or absence (lane 1) of WAVE2 (Central region) blocking peptide.Immunocytochemical labeling of WAVE2 in rat PC12 cells differentiated with NGF. The cells were labeled with rabbit polyclonal WAVE2 (Central) antibody, then detected using appropriate secondary antibody conjugated to Cy3. The antibody was used in the absence (left) or presence (right) of blocking peptide (WX1795).
Western blot of control and alkaline phosphatase-treated (AP) neonatal rat brain lysate (20 µg/lane). Blots were probed with anti-N-WASP (Lanes 1 & 2), anti-phospho-N-WASP (S484/S485) (Lanes 3 & 4), or anti-unphosphorylated-N-WASP (S484/S485) (Lanes 5 & 6).Immunocytochemical labeling of phospho- and unphospho-N-WASP in rabbit spleen fibroblasts. The cells were probed with N-WASP (Ser-484/Ser-485) phospho-specific and N-WASP (Ser-484/Ser-485) unphosphorylated antibodies, then the antibodies were detected using appropriate secondary antibodies conjugated to Cy3. The antibodies were used in the absence (left) or presence (right) of blocking peptide (WX2205 or WX2405).
Western blot analysis of control and alkaline phosphatase-treated (AP) neonatal rat brain lysate (20 µg/lane). Blots were probed with anti-N-WASP (Lanes 1 & 2), anti-phospho-N-WASP (S484/S485) (Lanes 3 & 4), or anti-unphosphorylated-N-WASP (S484/S485) (Lanes 5 & 6).
Western blot analysis of Jurkat (lane 1), A431 (lane 2), and HeLa (lane 3) cell lysates (20 µg/lane). Blots were probed with rabbit polyclonal anti-WASP/N-WASP (WP2101).Immunocytochemical labeling of N-WASP in control and pervanadate-treated A431 cells. The cells were labeled with rabbit polyclonal N-WASP/WASP (WP2101) or rabbit polyclonal N-WASP (Tyr-256) antibodies, then the antibodies were detected using appropriate secondary antibody conjugated to DyLight® 594.
Immunocytochemical labeling of Vimentin in paraformaldehyde fixed and NP-40 permeabilized A7r5 cells. The cells were labeled with a mouse monoclonal antibody to Vimentin (VM4341), then the antibody was detected using Goat anti-Mouse secondary antibody conjugated to DyLight® 594.Western blot image of cell structure markers in NCI-H1915 lung carcinoma cells. The blot was probed with anti-Vimentin intermediate
filament protein VM4341 (lane 1), anti-Nucleoporin p62 NM4361 (lane 2), anti-Hsp60 mitochondrial protein HM4381 (lane 3), and anti-Calnexin endoplasmic reticulum protein CM4371 (lane 4).
Left: Western blot image of human K-562 cells (lanes 1 & 2) and HUVEC (lanes 3 & 4). The blots were probed with rabbit polyclonal anti-VEGFR-3 (a.a. 1285-1298) in the absence (lanes 1 & 3) or presence of blocking peptide (VX2945) (lanes 2 & 4). Right: Western blot image of GST-recombinant human VEGFR-1 (89 kDa), VEGFR-2 (110 kDa), and VEGFR-3 (86 kDa) C-terminal regions. The blot was probed with anti-VEGFR-3 (a.a. 1285-1298).
Western blot image of GST-recombinant human VEGFR-1 (89 kDa), VEGFR-2 (110 kDa), and VEGFR-3 (86 kDa) C-terminal regions. The blots were probed with rabbit polyclonal anti-VEGFR-2 (a.a. 1304-1317), anti-VEGFR-2 (Tyr-801, conserved site), and anti-VEGFR-3 (a.a. 1285-1298).Left: Western blot image of HUVEC cells untreated (-) or treated with pervanadate (1 mM) for 30 min. (+). Right: Western blot image of GST-recombinant VEGFR-2 kinase without (-) or with (+) akaline phosphatase treatment. Both sets of blots were probed with rabbit polyclonal anti-VEGFR-2 (a.a. 1304-1317) or anti-VEGFR-2 (Tyr-801).
Western blot of human Jurkat (lanes 1 & 4), HUVEC (lanes 2 & 5), and A431 (lanes 3 & 6) cells. The blots were probed with anti-Vav2 (a.a. 309-322) at a dilution of 1:500 (lanes 1-3) and anti-Vav3 (a.a. 293-305) at 1:500 (lanes 4-6).
Western blot of human Jurkat (lanes 1 & 4), HUVEC (lanes 2 & 5), and A431 (lanes 3 & 6) cells. The blots were probed with anti-Vav2 (a.a. 309-322) at a dilution of 1:500 (lanes 1-3) and anti-Vav3 (a.a. 293-305) at 1:500 (lanes 4-6).
Western blot of human A431 cells treated with EGF (lanes 1, 3, & 5) then the blot was exposed to alkaline phosphatase (lanes 2, 4, & 6). The blots were probed with anti-Vav (a.a. 165-174) (lanes 1 & 2), anti-Vav2 (Tyr-142) (lanes 3 & 4), or anti-Vav2 (Tyr-172) (lanes 5 & 6).Immunocytochemical labeling of Vav in paraformaldehyde-fixed and NP-40-permeabilized rabbit spleen fibroblasts. The cells were labeled with rabbit polyclonal Vav (a.a. 165-174), and detected using appropriate secondary antibody conjugated to Cy3.
Western blot image of human A431 cells stimulated with calyculin A (100 nM) for 30 min. The blots were untreated (lanes 1 & 3) or treated with lambda phosphatase (lanes 2 & 4), then probed with mouse monoclonal VASP (C-term.) antibody (lanes 1 & 2) or rabbit polyclonal VASP (Thr-278) phospho-specific antibody (lanes 3 & 4).Immunocytochemical labeling of VASP in aldehyde-fixed and NP-40-permeabilized A431 cells. The cells were labeled with mouse monoclonal VASP (C-terminal region) antibody, then the antibody was detected using appropriate secondary antibody conjugated to DyLight® 594.
Western blot analysis of mouse brain. The blot was probed with anti-unphosphorylated βIII-Tubulin (Ser-444) (lanes 1-3) and anti-βIII-Tubulin (C-terminus) (lanes 4-6) polyclonal antibodies. Both antibodies were used in the presence of unphosphorylated βIII-Tublin (Ser-444) peptide (lanes 2 & 5; TX1815) and phospho-βIII-Tublin (Ser-444) peptide (lanes 3 & 6; TX1695).Immunocytochemical labeling of β-tubulin in aldehyde fixed and NP-40 permeabilized human NCI-H1299 lung carcinoma cells. The cells were labeled with rabbit polyclonal anti-unphosphorylated β-Tubulin (TP1811). The antibody was detected using goat anti-rabbit DyLight® 594.
Western blot analysis of mouse brain. The blot was probed with anti-unphosphorylated βIII-Tubulin (Ser-444) (lanes 1-3) and anti-βIII-Tubulin (C-terminus) (lanes 4-6) polyclonal antibodies. Both antibodies were used in the presence of unphosphorylated βIII-Tublin (Ser-444) peptide (lanes 2 & 5; TX1815) and phospho-βIII-Tublin (Ser-444) peptide (lanes 3 & 6; TX1695).Immunocytochemical labeling in chick dorsal root ganglion neurons using anti-Cofilin (N-terminus; CP1131), anti-Cofilin (Ser-3; CP1151), anti-βIII-Tubulin (C-terminus; TP1691) and anti-β-Tubulin (TM1541) antibodies. (Images provided by Dr. Diane Snow, Department of Anatomy & Neurobiology, University of Kentucky).
Western blot analysis of purified brain tubulin untreated (lanes 1,3,5) or treated with ERK2 kinase to phosphorylate Ser-172 (lanes 2,4,6). The blot was probed with anti-β-Tubulin (a.a. 168-177) (lanes 1 & 2), anti-β-Tubulin (Ser-172) (lanes 3 & 4), and anti-β-Tubulin (TM1541) (lanes 5 & 6).Immunocytochemical labeling of β-tubulin in aldehyde fixed and NP-40 permeabilized human NCI-H1299 lung carcinoma cells. The cells were labeled with rabbit polyclonal anti-β-Tubulin (TP1781). The antibody was detected using goat anti-rabbit DyLight® 594.

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