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The anti-pS34 antibody recognized AATYK1 immunoprecipitated from a mouse brain extract at a molecular weight ∼200 KDa (Fig. 5A, lane 1).

The possibility that lipin-1α stimulates the transcriptional activity of MEF2 by a direct coactivator mechanism is supported by our finding that lipin-1α coimmunoprecipitated with endogenous MEF2C in mouse brain extract (Fig. S4A) and with ectopically expressed MEF2C in HEK293A cells (Fig. S4B).

Mouse brain extract in SDS/PAGE loading buffer was obtained from Sigma Aldrich.

A higher protein concentration (40 μg/μL) of WT mouse brain extract decreased the adhesion of cells by approximately 75%.

(Bottom) GST pulldowns from a mouse brain extract using GST alone or GST fusions of OCRL as baits.

Antibodies we generated against the mouse FLJ46154 protein recognize a protein of the predicted size for FLJ46154 in mouse brain extract (supplementary figure 6).

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To determine whether the endogenous Tmub1/HOPS is localized in the membranous compartment, we fractionated mouse brain extracts into cytosolic and membranous fractions (Figure 2F).

A more expansive huntingtin (htt) interactome subnetwork, comprising over 700 candidate proteins, was likewise identified in mouse brain extracts using AP-MS by Shirasaki et al. [ 58].

Using optimal conditions (5 μg mAb295/mg M270 beads; bead volume 10% of total extracts), we extracted β2∗ nAChRs from mouse brain extracts prepared from wild type (WT), heterozygous (HET) and homozygous (KO) mice lacking either α4 or β2 nAChR subunit.

The MS/MS spectra for the low-intensity peaks in the MALDI imaging spectra were acquired from the mouse brain extracted glycans to confirm their composition (Supporting Information S1).

To better understand the function of neuronal RTN1A, we searched for protein-binding partners using pull-down experiments from mouse brain extracts with a GST-His-tagged fusion protein comprising aa 1 523 of rat RTN1A GST-RTN15233) (Fig. 1A).

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