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. Author manuscript; available in PMC: 2008 Sep 22.
Published in final edited form as: J Invest Dermatol. 2007 Jul 26;127(12):2807–2817. doi: 10.1038/sj.jid.5700970

Figure 4.

Figure 4

IgG in the sera of Wt mice grafted with Tg skin specifically bound hBPAG2. a. IgG in the sera of Wt mice grafted with Tg skin specifically bound hBPAG2 in extracts of cultured HKs as well as recombinant NC16A-GST (lanes 1 and 4, respectively). While preadsorption of immune sera with recombinant NC16A-GST completely removed all reactivity to this fusion protein (lane 5), immunoadsorbed immune sera still bound hBPAG2 (lane 2), indicating that epitopes other than NC16A are also targeted by such IgG. Normal mouse serum did not show any reactivity to hBPAG2 or NC16A-GST (lanes 3 and 6, respectively). Results were confirmed in three separate experiments. Markers in the left margins indicate Mr × 10-3. b. Immunoprecipitation studies of biosynthetically radiolabeled HK extracts showed that sera from Wt mice grafted with Tg skin (representative example, lane 1) contained IgG that bound BPAG2 but not BPAG1 – the former identified as a 180 kD protein that comigrated with BPAG2 immunoprecipitated by serum from a patient with BP (lane 3). Serum from a Wt mouse grafted with Wt skin (lane 2) as well as serum from a normal volunteer (lane 4) bound no specific HK proteins in these immunoprecipitation studies. Markers in the right margin indicate Mr × 10-3.