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. 2006 Oct 9;26(24):9508–9516. doi: 10.1128/MCB.01136-06

FIG. 1.

FIG. 1.

Imp is coimmunoprecipitated with Sqd and Hrp48. (A) Western blot of immunoprecipitation (IP) from ovary extract with anti-Imp antibodies or preimmune serum (Pre) with (+) or without (−) RNase A/T1 treatment. Proteins on the blot were detected with anti-Imp and anti-Sqd. An amount of ovary extract equal to 5% of that used for the immunoprecipitations was loaded in lane WCL. (B) Western blot of immunoprecipitation from ovary extract with Hrp48 or Nanos (Nos) antibodies with or without RNase A/T1 treatment. The blot was probed with anti-Imp. (C) Western blot analysis of Imp protein. Similar amounts of ovarian protein from w1118 or ImpG0072/Df(1)HC133 mutant females were probed for Imp and for α-tubulin as a loading control. The ImpG0072 hemizygous mutant has dramatically reduced levels of the two immunoreactive bands of Imp protein (one prominent and indicated as Imp, the other less abundant and slightly larger). The identities of the bands were confirmed in blots probed separately for Imp or Tubulin. wt, wild type.