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. 2011 May 6;286(26):22991–23002. doi: 10.1074/jbc.M110.204271

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© 2011 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 4. — Western blot analysis for wild-type and glycosylation-deficient mutant hPAR₁. A, immunoprecipitates from KNRK cell lines expressing HA.11-tagged hPAR₁ with the potential N-linked glycosylation sequons removed were analyzed by SDS-PAGE (10% gel) and immunoblotted using HA.11 monoclonal antibody. Lane 1, EV; lane 2, WT hPAR₁E; lane 3, N62QhPAR₁E; lane 4, N62Q/N75QhPAR₁E; lane 5, N35Q/N62Q/N75QhPAR₁E; lane 6, N250Q/N259QhPAR₁E; lane 7, N35–259QhPAR₁E. B, protein samples of hPAR₁E-transfected CHO (Pro5 and Lec2) cell lines were immunoprecipitated by HA.11 immunoprecipitation and were analyzed by SDS-PAGE (10% gel) and immunoblotted using a monoclonal HA.11 antibody. Lane 1, Pro5; lane 2, Pro5-PAR₁E; lane 3, Lec2; lane 4, Lec2-PAR₁E. GD, glycosylated dimer; NGD, nonglycosylated dimer; GM, glycosylated monomer; NGM, nonglycosylated or minimally glycosylated monomer; M, nonglycosylated or minimally glycosylated monomer; D, PAR₁ dimer; M.M., molecular mass. Results are representative of three separate experiments.