Western blot analysis of extracts from various cell lines using Paxillin (D9G12) Rabbit mAb. The 45 kDa band is a degradation product of full-length paxillin protein.
HeLa cells were detached with 0.04% trypsin and 0.03% EDTA, suspended in serum-free medium for one hour, and either processed in suspension (right) or plated on fibronectin-coated slides and allowed to adhere for an additional hour prior to fixation (left). Adherent cells were post-processed with λ-phosphatase to confirm phospho-specificity (center). Confocal immunofluorescent analysis was performed after staining with Phospho-Paxillin (Tyr118) (E9U9F) Rabbit mAb (green), DyLight™ 554 Phalloidin #13054 (red), and ProLong® Gold Antifade Reagent with DAPI #8961 (blue).
Immunoprecipitation of Phospho-Paxillin (Tyr118) protein from HeLa cells induced attachment to fibronectin-coated plate surface (10 μg/ml, 1 hr). Lane 1 is 10% input, lane 2 is Rabbit (DA1E) mAb IgG XP® Isotype Control #3900, and lane 3 is Phospho-Paxillin (Tyr118) (E9U9F) Rabbit mAb. Western blot analysis was performed using Phospho-Paxillin (Tyr118) (E9U9F) Rabbit mAb. Anti-rabbit IgG, HRP-linked Antibody #7074 was used as a secondary antibody.
Western blot analysis of extracts from HeLa cells in suspension, untreated (-) or induced attachment to fibronectin-coated plate surface (10 μg/ml, 1 hr; +), using Phospho-Paxillin (Tyr118) (E9U9F) Rabbit mAb (upper) and Paxillin (D9G12) Rabbit mAb #12065 (lower).
PhosphoPlus® Duets from Cell Signaling Technology (CST) provide a means to assess protein activation status. Each Duet contains an activation-state and total protein antibody to your target of interest. These antibodies have been selected from CST's product offering based upon superior performance in specified applications.
Paxillin is a multidomain protein that localizes primarily to focal adhesion sites in the extracellular matrix (1). Paxillin is one of the key components of integrin signaling, and tyrosine phosphorylation of paxillin is required for integrin-mediated cytoskeletal reorganization (2). Paxillin is phosphorylated by another focal adhesion component, focal adhesion kinase (FAK), at Tyr118 (3,4). Phospho-Paxillin (Tyr118) may provide a docking site for recruitment of other signaling molecules to focal adhesions. It has been shown that the SH2 domain of Crk binds to the phosphorylated Tyr118 of paxillin (5).
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