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Western blot of human K562 cells stimulated with pervanadate (1 mM) for 30 min. (lanes 1-4). The blot was treated with alkaline phosphatase to dephosphorylate CrkL (lanes 2 & 4), then the blot was probed with rabbit polyclonals CrkL (C-terminus) CP3081 (lanes 1 & 2) and CrkL (Tyr-207) phospho-specific CP4671 (lanes 3 & 4).
Western blot image of mouse brain untreated (lanes 1 & 3) or treated with lambda phosphatase (lanes 2 & 4). The blot was probed with anti-CRMP2 (C-terminal Region) (lanes 1 & 2) or anti-CRMP2 (Ser-522) (lanes 3 & 4).Immunocytochemical labeling of phosphorylated CRMP2 in mouse C2C12 cells. The cells were probed with CRMP2 (C-terminal region) and CRMP2 (Thr-555) rabbit polyclonal 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 their respective blocking peptide (CX2165 or CX2255).
Western blot analysis of human Jurkat cells treated with 100 nM calyculin A for 30 min.  then the blots were untreated (-) or treated (+) with lambda phosphatase. The blots were probed with rabbit polyclonals anti-CXCR4 (Ser-324/Ser-325) (left panel) or anti-CXCR4 (a.a. 322-329) (right panel).Immunocytochemical labeling of CXCR4 in chick pluripotent cells. The cells were labeled with rabbit polyclonal CXCR4 (a.a. 322-329) antibody (CP4211), then detected using appropriate secondary antibody (Red). (Image provided by Dr. Yangqing Lu at the Regenerative Bioscience Center, University of Georgia).
Western blot analysis of human Jurkat cells treated with 100 nM calyculin A for 30 min.  then the blots were untreated (-) or treated (+) with lambda phosphatase. The blots were probed with rabbit polyclonal anti-CXCR4 (Ser-324/Ser-325) (left panel), or anti-CXCR4 (a.a. 328-338) (right panel).Immunocytochemical labeling of CXCR4 in chick pluripotent cells. The cells were labeled with rabbit polyclonal CXCR4 (a.a. 328-338) antibody (CP4231), then detected using appropriate secondary antibody (Red). (Image provided by Dr. Yangqing Lu at the Regenerative Bioscience Center, University of Georgia).
Western blot analysis of human LNCaP (lane 1), MCF7 (lane 2), MDA-MB-231 (lane 3), and MeWo (lane 4) cell lysates, as well as human recombinant full-length cyclophilin B (lane 5) and cyclophilin A (lane 6). The blot was probed with mouse monoclonal anti-cyclophilin B (CM0191) at 1:500.Immunocytochemical labeling of cyclophilin B in methanol:acetone (1:1) fixed human A549 lung cancer cells. The cells were labeled with mouse monoclonal anti-cyclophilin B (CM0191). The antibody was detected using goat anti-mouse DyLight® 594.
Immunocytochemical labeling of DAAM1 in aldehyde-fixed and NP-40-permeabilized A431 cells. The cells were labeled with mouse monoclonal DAAM1 (N-terminal region) antibody, then the antibody was detected using appropriate secondary antibody conjugated to DyLight® 594. The corresponding phase image is shown to the right.
Western blot of DISC1 in mouse brain (lanes 1 & 3) and rat PC12 cells (lanes 2 & 4). The blots were probed with DP3021 anti-DISC1 (a.a. 740-753) (lanes 1 & 2) and DP3041 anti-DISC1 (a.a. 740-753) (lanes 3 & 4).
Western blot of DISC1 in mouse brain (lanes 1 & 3) and rat PC12 cells (lanes 2 & 4). The blots were probed with DP3021 anti-DISC1 (a.a. 740-753) (lanes 1 & 2) and DP3041 anti-DISC1 (a.a. 740-753) (lanes 3 & 4).
Western blot analysis of draxin expression in rat PC12 cells (lane 1), rat P1 brain (lane 2), adult mouse brain (lane 3), and chick E9 brain (lane 4). The blot was probed with rabbit polyclonal anti-Draxin (C-terminal region) at 1:1000.Immunocytochemical labeling of Draxin in rat PC12 cells differentiated with NGF. The cells were probed with Draxin (C-terminal region) rabbit polyclonal antibody, then the antibody was detected using appropriate secondary antibody conjugated to Cy3. The antibody was used in the absence (left) or presence (right) of blocking peptide (DX3675). Lower images show corresponding phase images.
Western blot image of human A431 cells  treated with pervanadate (1 mM) for 30 min (lanes 1 & 3) then treated with akaline phosphatase (lanes 2 & 4). Blots were probed with anti-E-Cadherin (Cytoplasmic) and anti-N-Cadherin (Tyr-860)/E-Cadherin (Tyr-835) conserved site.Formalin fixed, citric acid treated parafin sections of embryonic Rat E16 intestines. Sections were probed with anti-E-Cadherin (CM1681) then anti-mouse:HRP before detection using DAB. (Images provided by Carl Hobbs and Dr. Pat Doherty at Wolfson Centre for Age-Related Diseases, King's College London).
Western blot of EB proteins in mouse brain (lanes 1-5). The blot was probed with rat monoclonals EM5041 anti-EB1 (lane 1), EM5061 anti-EB1/2/3 (lane 2), EM5081 anti-EB2 (lane 3), EM5101 anti-EB3 (lane 4), and EM5091 anti-EB3 (lane 5). Then the antibodies were detected using goat anti-Rat IgG Light Chain specific:HRP (RS3121).Immunocytochemical labeling of EB1 in paraformaldehyde-fixed and NP40-permeabilized A431 cells. The cells were dual labeled with mouse monoclonal anti-α-Tubulin (TM4111) (left)  and rat monoclonal anti-EB1 (EM5041) (middle). The antibodies were detected using either goat anti-mouse:DyLight® 488 (MS3011) or goat anti-Rat:DyLight® 594 (RS3111).
Western blot of EB proteins in mouse brain (lanes 1-5). The blot was probed with rat monoclonals EM5041 anti-EB1 (lane 1), EM5061 anti-EB1/2/3 (lane 2), EM5081 anti-EB2 (lane 3), EM5101 anti-EB3 (lane 4), and EM5091 anti-EB3 (lane 5). Then the antibodies were detected using goat anti-Rat IgG Light Chain specific:HRP (RS3121).Immunocytochemical labeling of EB2 in paraformaldehyde-fixed and NP40-permeabilized A431 cells. The cells were dual labeled with mouse monoclonal anti-α-Tubulin (TM4111) (left)  and rat monoclonal anti-EB2 (EM5081) (right). The antibodies were detected using either goat anti-mouse:DyLight® 488 (MS3011) or goat anti-Rat:DyLight® 594 (RS3111).

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