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. 2000 Aug 7;192(3):337–346. doi: 10.1084/jem.192.3.337

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© 2000 The Rockefeller University Press

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).

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graphic file with name JEM000434.f5a.jpg — Biochemical characterization of 2B4-associated molecules in normal and XLP-NK cells. (a) NK or XLP-NK cell populations, either untreated (−) or treated (+) with sodium pervanadate, were immunoprecipitated with anti-2B4 (S39 mAb), anti-IRp60 (P192 mAb, isotype-matched negative control), or anti-SH2D1A antiserum. Samples were analyzed in a 14% SDS-PAGE under reducing conditions and probed with anti-SH2D1A antiserum. (b) 2B4, IRp60 (positive control), and NKp46 (BAB281 mAb, negative control) molecules were sequentially immunoprecipitated from normal polyclonal NK cell populations either untreated (−) or treated (+) with sodium pervanadate. Identical samples were divided, analyzed in 7% SDS-PAGE under reducing conditions, and probed with either anti–SHP-2 (left) or anti–SHP-1 (right) mAbs. Sepharose-PA preclearing on treated cells (/) is also shown. (c) Anti-2B4, anti–SHP-2, or anti–SHP-1 immunoprecipitates were derived from XLP-NK cell populations either untreated (−) or treated (+) with sodium pervanadate. Identical samples were divided, analyzed in 7% SDS-PAGE under reducing conditions, and probed with either anti–SHP-2 (left) or anti–SHP-1 (right) mAbs. Molecular mass markers (kD) are indicated. Arrows indicate SH2D1A, SHP-2, and SHP-1 molecules. The first lanes in b and c were loaded with the S39 (2B4-specific) mAb alone as control.

graphic file with name JEM000434.f5c.jpg — Biochemical characterization of 2B4-associated molecules in normal and XLP-NK cells. (a) NK or XLP-NK cell populations, either untreated (−) or treated (+) with sodium pervanadate, were immunoprecipitated with anti-2B4 (S39 mAb), anti-IRp60 (P192 mAb, isotype-matched negative control), or anti-SH2D1A antiserum. Samples were analyzed in a 14% SDS-PAGE under reducing conditions and probed with anti-SH2D1A antiserum. (b) 2B4, IRp60 (positive control), and NKp46 (BAB281 mAb, negative control) molecules were sequentially immunoprecipitated from normal polyclonal NK cell populations either untreated (−) or treated (+) with sodium pervanadate. Identical samples were divided, analyzed in 7% SDS-PAGE under reducing conditions, and probed with either anti–SHP-2 (left) or anti–SHP-1 (right) mAbs. Sepharose-PA preclearing on treated cells (/) is also shown. (c) Anti-2B4, anti–SHP-2, or anti–SHP-1 immunoprecipitates were derived from XLP-NK cell populations either untreated (−) or treated (+) with sodium pervanadate. Identical samples were divided, analyzed in 7% SDS-PAGE under reducing conditions, and probed with either anti–SHP-2 (left) or anti–SHP-1 (right) mAbs. Molecular mass markers (kD) are indicated. Arrows indicate SH2D1A, SHP-2, and SHP-1 molecules. The first lanes in b and c were loaded with the S39 (2B4-specific) mAb alone as control.