Primary Antibodies

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Western blot image of human endothelial cells untreated (lanes 1 & 3) or treated with pervanadate (1 mM) for 30 min (lanes 2, 4, 5 & 6). The blots were probed with anti-N-Cadherin (Cytoplasmic) (lanes 1 & 2) and anti-N-cadherin (Tyr-820) (lanes 3-6). The latter antibody was used in the presence of no peptide (lane 4), phospho-N-cadherin (Tyr-820) peptide (lane 5), or phospho-N-cadherin (Tyr-860) peptide (lane 6).Immunocytochemical labeling of phosphorylated N-Cadherin in pervanadate-treated mouse C2C12. The cells were labeled with mouse monoclonal N-Cadherin (Cytoplasmic) and rabbit polyclonal N-Cadherin(Tyr-860) antibodies, then the antibodies were detected using appropriate secondary antibodies conjugated to Cy3.
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 293 cells mock transfected (lane 1) or transiently transfected with pLenti6/TR lentiviral vector (lanes 2 & 3). Blots were probed with anti-Bsd (lanes 1-3). Molecular weight (MW) standards show that Bsd is expressed as a 13 kDa band in only the transfected cells.Immunocytochemical labeling of Blasticidin S Deaminase (Bsd) in 293 cells mock transfected (left) and transiently transfected with pLenti6/TR lentiviral vector (right). The cells were labeled with anti-Bsd (BP1231) and detected using appropriate secondary antibody conjugated to Texas Red. (Images provided by Charles Mashburn and Dr. George Smith at the University of Kentucky, Spinal Cord and Brain Injury Research Center).
Western blot image of mouse gastrocnemius (lanes 1 & 3) and mouse diaphragm tissue lysate (lanes 2 & 4). The blot was probed with anti-Atrogin-1 (AP2041; lanes 1-4) in the presence (lanes 3 & 4) or absence (lanes 1 & 2) of Atrogin-1 peptide (AX2045).Formalin fixed, citric acid treated paraffin sections of E16 mouse skeletal muscle. Sections were probed with anti-Atrogin-1 (AP2041) then anti-Rabbit: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 image of human recombinant Atrogin 1 (lanes 1-6). The blot was probed with rabbit polyclonal Atrogin-1 (lanes 1-3) and rat monoclonal Atrogin-1 (lanes 4-6) at 1:1000 (lanes 1 & 4), 1:2000 (lanes 2 & 5), and 1:4000 (lanes 3 & 6).
Western blot of human A431 cells treated with Calyculin A (100 nM) for 30 min. Blot lanes were untreated (lanes 1, 3, & 5) or treated with lambda phosphatase (lanes 2, 4, & 6) then probed with anti-ATM (Ser-794) (lanes 1 & 2), anti-ATM (C-Terminal) (lanes 3 & 4), or anti-ATM (Ser-1981) (lanes 5 & 6).Immunocytochemical labeling of ATM phosphorylation in control (Top row) or calyculin A-treated A431 cells (Bottom row). The cells were labeled with mouse monoclonal ATM (C-terminal region) (AM3611) and ATM (Ser-1981) (AM3661). The antibodies were detected using goat anti-mouse-DyLight® 594.
Western blot of human A431 (lane 1), Jurkat (lane 2), and HeLa (lane 3) cells. The blots were probed with rabbit polyclonal anti-Arp3 (C-terminal region) antibody at 1:1000 (lanes 1-3).Immunocytochemical labeling of Arp3 in aldehyde-fixed and NP-40-permeabilized rat PC12 cells differentiated with NGF. The cells were labeled with rabbit polyclonal anti-Arp3 (C-terminal region) (AP4581) in the absence (left) or presence (right) of blocking peptide (AX4585). The antibody was detected using appropriate secondary antibody conjugated to DyLight® 594.
Immunocytochemical labeling of Arp2 phosphorylation in rat PC12 cells differentiated with NGF. The cells were probed with Arp2 (C-terminal region) and Arp2 (Thr-237/Thr-238) rabbit polyclonal antibodies, then the antibodies were detected using appropriate secondary antibody conjugated to Cy3.
Western blot analysis of mouse recombinant Ago2 full length protein (lanes 1-4). The blot was treated with lambda phosphatase (lanes 2 & 4) then probed with rabbit polyclonal anti-Ago2 (AP5281) (lanes 1 & 2) and rabbit polyclonal anti-Ago2 (Ser-387) phospho-specific antibody (lanes 3 & 4).
Western blot analysis of human A431 cells treated with EGF (100 ng/ml for 60 min.) (lanes 1-4). The blot was treated with lambda phosphatase (lanes 2 & 4) then probed with rat monoclonal anti-Ago2 (AM5271) (lanes 1 & 2) and rabbit polyclonal anti-Ago2 (Tyr-393) phospho-specific antibody (lanes 3 & 4).

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