FITC-labeled bovine serum albumin

There are several recent examples of the switching of nonspecific protein binding on polymer surfaces by application of an external stimulus. Alexander and coworkers demonstrated that protein adhesion can be controlled on PNIPAM surface brushes [14, 181]. For instance, it was reported that the adsorption of FITC-labeled bovine serum albumin (FITC-BSA) on PNIPAM/hexadecanethiol micropatterned surfaces could be tuned by LCST. However, this effect was found to be less pronounced after prolonged incubation times or repeated heating/cooling cycles. The authors suggested that this behavior could be due to unspecific PNIPAM-protein interactions [14],... 

The binding constant between FITC-labeled bovine serum albumin and its monoclonal antibody was determined using ACE with LIF [14], Interaction of the enzyme cyclophilin with the immunosuppressive drug cyclosporine A was quantitatively assessed by CE with UV detection [15]. In the latter case the authors showed in particular how the difference between the sensitivity of the detector and KD of the studied system can severely hamper the correct determination of binding constants. 

Confocal laser scanning microscopy images of patterned poly(poly(ethylene glycol) methyl ether methacrylate) (PPEGMA) brushes on (a) poly(ethylene terephthalate) (PET) after the treatment with fluorescein isothiocyanate (FITC)-labeled bovine serum albumin (BSA). (Reprinted with permission from Ohno, K., et al., Macromolecides, 43, 5569-5574, 2010, copyright (2010) American Chemical Society.)... 

Figure 9 On-chip electropherograms of fluorescein isothiocyanate-labeled bovine serum albumin (FlTC-labeled BSA) (bottom) and of a mixture containing FITC-labeled BSA and monoclonal anti-BSA in diluted mouse ascites fluid. (From Ref. 95.)...

Figure 13 Molecular-mass analysis of phosphorylase B (panel B) and the separation of the noncovalently (Sypro Red) labeled protein markers (panel A ALA, a-lactalbumin CBA, carbonic anhydrase OVA, ovalbumin BSA, bovine serum albumin BGA, (f-galactosidase) and the covalently (FITC) labeled protein markers (panel C TRI, tripsin inhibitor CAH, carbonic anhydrase ADH, alcohol dehydrogenase BSA, bovine serum albumin BGA, P-galactosidase). Separation conditions gel, 1% agarose, 2% linear polyacrylamide (LPA, MW 700,000-1,000,000) in 50 mM Tris, 50 mM TAPS, 0.05% SDS (pH 8.4) separation buffer, 50 mM Tris, 50 mM TAPS, 0.05% SDS (pH 8.4) separation voltage, 420 V, current, 5 mA gel thickness, 190 pm effective separation length, 3.5 cm temperature, 25°C sample loading, 0.2 pL into 2.5 x 4 x 0.19-mm injection wells. Sample buffer contained 0.05% SDS and 1 x Sypro Red. (Reproduced with permission from Ref. 141.)...

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