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. 1997 Jun 16;137(6):1393–1401. doi: 10.1083/jcb.137.6.1393

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Multiple banding pattern and detergent solubility of occludin. (A) Immunoblots of the isolated junctional fraction from the chick liver (Chicken JF) and the whole cell lysate of MDCK I cells (MDCK I) with anti–chicken occludin mAb (Oc-2) and anti–mouse occludin pAb (F4), respectively. The apparent molecular masses of chicken and dog occludin were distributed between 58 and 66 kD and 62 and 82 kD, respectively. (B) Anti-occludin pAb (F4) immunoblots of the total (T), NP-40–soluble (S), and NP-40–insoluble (I) fractions of confluent MDCK I cells (see Materials and Methods). (C) Anti-occludin mAb (MOC37) immunoblots of the anti-occludin pAb (F4 + F5) immunoprecipitates from the total (T), NP-40–soluble (S), and NP-40–insoluble (I) fractions of confluent MDCK I cells. Since the amount of occludin in each fraction was fairly small (B), both NP-40–soluble and -insoluble occludins were recovered by immunoprecipitation, electrophoresed, and immunoblotted (C). Comparison between B and C revealed that the efficiency of immunoprecipitation from NP-40–soluble fraction is almost the same as that from NP40–insoluble fraction. Higher M _r bands of occludin were selectively recovered in the NP-40–insoluble fraction.