Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2011 Feb 16;6(2):e17037. doi: 10.1371/journal.pone.0017037

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Riemer et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

PMC Copyright notice

(A) Immunoprecipitation of ERFAD-HA. Cells stably expressing ERFAD-HA (A11) and control cells (FRT) not overexpressing the protein were [³⁵S] pulse-labeled for 16 hours, treated as indicated, Triton X-100 lysates immunoprecipitated with anti-HA, and samples separated by reducing SDS-PAGE. CHO, N-glycans. The arrowhead indicates the novel protein that was coimmunoprecipitated with ERFAD-HA. (B) The approach from (A) was upscaled and analysed by mass spectrometry. The positions of ERFAD-HA as well as of the identified protein – ERp90 – are indicated. (C) Immunoprecipitations on lysates of A11 cells that were [³⁵S] pulse-labeled to steady state were performed with anti-HA. The immunoprecipitate was either analyzed directly (lane 1) or reimmunoprecipitated using HA- (lane 2), SEL1L- (lane 3) or ERp90- (lane 4) antibodies. The positions of the individual proteins are indicated and the glycosylated 90 kDa band coprecipitating with ERFAD-HA can thereby be attributed to ERp90. The hairline indicates that one lane has been removed.