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SDS‐PAGE gets another life: Quantitative affinity electrophoresis pp. 1371–1382 Some old dogs never stop hunting. You've heard of Schrödinger's cat, now we have Laemmli's dog – it brings home any stick you throw. Originally published in the 1970s as an improved protein electrophoresis method, it is now the basis for an affinity separation protocol for phosphoproteins. In the new (age 5) method, phosphoproteins are separated in a Laemmli Tris‐based SDS gel into which a phosphate‐chelating agent has been polymerized. The chelator retards proteins in proportion to the number of exposed phosphates. Messer et al. used the procedure of Kinoshita et al. [Ref. 18] to evaluate the phosphorlyation status of pathological heart tissue and potential donor hearts and valves. The procedure is much simpler than those based on mass spectrometry.Geography reaches new dimensions by FRETting pp. 1383–1388 Geography was once a subject unto itself, the study of the earth, but, now too big to teach in one term, it has been broken up into a variety of topics and sub‐topics. As we learn here, it is not even linked to the earth. Kang et al. describe a new method of exploring the geography of molecules within a cell using fluorescent resonance energy transfer (FRET). In FRET, the overlap of the emission spectrum of one molecule with the excitation spectrum of a second returns a signal dependent on the distance between the two molecules. A quantum dot, conjugated to a high‐affinity peptide (RGD), overlapped spectra with fluorescent dye Cy3 which was linked to a synthetic antibody (aptamer). Staining cancer cells with the two agents revealed an interaction between potential biomarkers not seen with conventional reagents.All roads lead (eventually) to or from insulin pp. 1440–1450 The word for insulin is “pleiotropic” or, roughly, “fingers in a lot of pies.” Two pies of current major interest are insulin resistance and type 2 diabetes. Insulin resistance is due in part to activation of several protein kinases (including IκB kinase, PKC, JNK) and inhibition of insulin receptor substrate 1 and Akt. Most of these are regulated by the degree of site‐specific phosphorylation which, in turn, is regulated by poorly or unknown mechanisms. A more facile means of evaluating these levels has been developed by He et al. in the form of antibody arrays. The monoclonal antibodies in the arrays are specific for particular phosphorylated amino acids in selected proteins. They circumvented antibody stability issues by applying mAbs to glass slides in a three‐dimensional matrix material. The array was validated by a multiplexed bead test and a Western blot test.