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. 2010 Sep 21;300(2):E276–E286. doi: 10.1152/ajpendo.00262.2010

Fig. 6.

Fig. 6.

Binding interactions between Kir6.2 and α-synuclein demonstrated in mouse islets. Data from a representative coimmunoprecipitation experiment from mouse islet cells showing immunoblots reacted with an anti-α-synuclein antibody (610787; A and B, bottom) or anti-Kir6.2 antibody (sc-20809, H55; A and B, top). A: immunoblots showing Kir6.2 and α-synuclein in initial homogenate (Input), which was enriched in the coimmunoprecipitation using an anti-α-synuclein antibody (Syn-1, BD 610786; Syn IP). Specificity was confirmed using preadsorbed Syn-1 antibody for coimmunoprecipitation (Pre), which efficiently reduced the level of the proteins coimmunoprecipitated. B: immunoblots reveal the presence of Kir6.2 and α-synuclein in the initial homogenate (Input) as well as in the coimmunoprecipitation performed with anti-Kir6.2 antibody (sc-20809, H55; Kir6.2 IP), and specificity was demonstrated by coimmunoprecipitation using preimmune serum and beads (Pre). Molecular weights, determined from prestained standards, are shown on the left.