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Recently, the simultaneous characterization of the glycoproteome and phosphoproteome of mouse brain membrane has been achieved with ERLIC [29].
They were characterized simultaneously from a digest of mouse brain membrane but under conditions where the unmodified peptides eluted in the flow-through [29].
As shown in Fig. 1A, 14-3-3 co-immunoprecipitated with L1 from mouse brain membrane fractions, indicating that L1 and 14-3-3 14-3-3 14-3-3ciate in the brain.
We have published two novel ERLIC based fractionation approaches for the simultaneous characterization of glyco- and phosphoproteomes of mouse brain membrane [29] and the comprehensive profiling of rat kidney proteome [30].
The L6/23 antibody detects bands of the predicted molecular weight in western blots of rat and wildtype mouse brain membrane preparations and detects no bands in blots of brain membrane preparations from BK channel (α subunit) knockout mice (Figure S2A).
Mouse brain membrane fractions containing 1.5 mg/ml protein in modified RIPA buffer (50 mM Tris-HCl pH 7.4, 150 mM NaCl, 2 mM EDTA, 1 mM NaF, 1 mM Na3VO4, 1% Nonidet P-40, 0.5% SDS, 100 µM PMSF, Complete Protease Inhibitor Cocktail EDTAfree, and Phosphatase Inhibitor Cocktail I) were precleared using 25 µl of Protein A Agarose beads (Santa Cruz).
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Native co-immunoprecipitation assays from mouse brain membranes imply that KCNE1 and KCNE3 interact with Kv12.2 simultaneously in vivo, suggesting the existence of novel KCNE1-KCNE3-Kv12.2 complexesripartite complexes.
One earlier study has reported the MPTP binding to σ protein in C57BL/6 mouse brain membranes.
The antibody recognized a single band of approximately 72 kDa in immunoblot analysis of both rat and mouse brain membranes (Dabrowska and Rainnie 2010; Rhodes et al. 2004).
To further determine in which sub-mitochondrial compartment the Pank2 protein was present, we further fractionated mitochondria derived from WT mouse brain, into membranes, inter-membrane space, and matrix, and we isolated mitoplasts.
The protein Norbin regulates the accumulation of a neurotransmitter receptor in mouse brain cell membranes.
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