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. 1999 Sep 20;190(6):793–802. doi: 10.1084/jem.190.6.793

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© 1999 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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Biochemical analysis of Z176-reactive molecules and their association with SHP-1 phosphatase. (a) A polyclonal NK population was surface labeled with ¹²⁵I and immunoprecipitated with anti-NKG2A (Z199 mAb, lanes A and B), anti-p70/NKB-1 (Z27 mAb, lanes C and D), and Z176 mAb (lanes E and F). Samples were analyzed in an 8% SDS-PAGE under reducing conditions either undigested (−) or digested (+) with N-glycosidase. Molecular weight markers (in kD) are indicated on the right. (b) 1% NP-40 cell lysates derived from a polyclonal NK cell population, untreated (−) or treated (+) with sodium pervanadate, were immunoprecipitated with Z176 mAb. Samples were analyzed in an 11% SDS-PAGE under reducing conditions, transferred to polyvinylidene difluoride membranes, and probed with either antiphosphotyrosine (anti-PTyr) or anti–SHP-1 mAb.

Biochemical analysis of Z176-reactive molecules and their association with SHP-1 phosphatase. (a) A polyclonal NK population was surface labeled with ¹²⁵I and immunoprecipitated with anti-NKG2A (Z199 mAb, lanes A and B), anti-p70/NKB-1 (Z27 mAb, lanes C and D), and Z176 mAb (lanes E and F). Samples were analyzed in an 8% SDS-PAGE under reducing conditions either undigested (−) or digested (+) with N-glycosidase. Molecular weight markers (in kD) are indicated on the right. (b) 1% NP-40 cell lysates derived from a polyclonal NK cell population, untreated (−) or treated (+) with sodium pervanadate, were immunoprecipitated with Z176 mAb. Samples were analyzed in an 11% SDS-PAGE under reducing conditions, transferred to polyvinylidene difluoride membranes, and probed with either antiphosphotyrosine (anti-PTyr) or anti–SHP-1 mAb.