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SH2 Domain Histochemistry

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SH2 Domain Histochemistry. / Buhs, Sophia; Nollau, Peter.

In: Methods Mol Biol, Vol. 1555, 2017, p. 535-545.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Buhs, S & Nollau, P 2017, 'SH2 Domain Histochemistry', Methods Mol Biol, vol. 1555, pp. 535-545. https://doi.org/10.1007/978-1-4939-6762-9_31

APA

Buhs, S., & Nollau, P. (2017). SH2 Domain Histochemistry. Methods Mol Biol, 1555, 535-545. https://doi.org/10.1007/978-1-4939-6762-9_31

Vancouver

Buhs S, Nollau P. SH2 Domain Histochemistry. Methods Mol Biol. 2017;1555:535-545. https://doi.org/10.1007/978-1-4939-6762-9_31

Bibtex

@article{b7000066d2dd412d843904195b629d9f,
title = "SH2 Domain Histochemistry",
abstract = "Among posttranslational modifications, the phosphorylation of tyrosine residues is a key modification in cell signaling. Because of its biological importance, characterization of the cellular state of tyrosine phosphorylation is of great interest. Based on the unique properties of endogenously expressed SH2 domains recognizing tyrosine phosphorylated signaling proteins with high specificity we have developed an alternative approach, coined SH2 profiling, enabling us to decipher complex patterns of tyrosine phosphorylation in various normal and cancerous tissues. So far, SH2 profiling has largely been applied for the analysis of protein extracts with the limitation that information on spatial distribution and intensity of tyrosine phosphorylation within a tissue is lost. Here, we describe a novel SH2 domain based strategy for differential characterization of the state of tyrosine phosphorylation in formaldehyde-fixed and paraffin-embedded tissues. This approach demonstrates that SH2 domains may serve as very valuable tools for the analysis of the differential state of tyrosine phosphorylation in primary tissues fixed and processed under conditions frequently applied by routine pathology laboratories.",
author = "Sophia Buhs and Peter Nollau",
year = "2017",
doi = "10.1007/978-1-4939-6762-9_31",
language = "English",
volume = "1555",
pages = "535--545",
journal = "Methods Mol Biol",
issn = "1064-3745",
publisher = "Humana Press",

}

RIS

TY - JOUR

T1 - SH2 Domain Histochemistry

AU - Buhs, Sophia

AU - Nollau, Peter

PY - 2017

Y1 - 2017

N2 - Among posttranslational modifications, the phosphorylation of tyrosine residues is a key modification in cell signaling. Because of its biological importance, characterization of the cellular state of tyrosine phosphorylation is of great interest. Based on the unique properties of endogenously expressed SH2 domains recognizing tyrosine phosphorylated signaling proteins with high specificity we have developed an alternative approach, coined SH2 profiling, enabling us to decipher complex patterns of tyrosine phosphorylation in various normal and cancerous tissues. So far, SH2 profiling has largely been applied for the analysis of protein extracts with the limitation that information on spatial distribution and intensity of tyrosine phosphorylation within a tissue is lost. Here, we describe a novel SH2 domain based strategy for differential characterization of the state of tyrosine phosphorylation in formaldehyde-fixed and paraffin-embedded tissues. This approach demonstrates that SH2 domains may serve as very valuable tools for the analysis of the differential state of tyrosine phosphorylation in primary tissues fixed and processed under conditions frequently applied by routine pathology laboratories.

AB - Among posttranslational modifications, the phosphorylation of tyrosine residues is a key modification in cell signaling. Because of its biological importance, characterization of the cellular state of tyrosine phosphorylation is of great interest. Based on the unique properties of endogenously expressed SH2 domains recognizing tyrosine phosphorylated signaling proteins with high specificity we have developed an alternative approach, coined SH2 profiling, enabling us to decipher complex patterns of tyrosine phosphorylation in various normal and cancerous tissues. So far, SH2 profiling has largely been applied for the analysis of protein extracts with the limitation that information on spatial distribution and intensity of tyrosine phosphorylation within a tissue is lost. Here, we describe a novel SH2 domain based strategy for differential characterization of the state of tyrosine phosphorylation in formaldehyde-fixed and paraffin-embedded tissues. This approach demonstrates that SH2 domains may serve as very valuable tools for the analysis of the differential state of tyrosine phosphorylation in primary tissues fixed and processed under conditions frequently applied by routine pathology laboratories.

U2 - 10.1007/978-1-4939-6762-9_31

DO - 10.1007/978-1-4939-6762-9_31

M3 - SCORING: Journal article

C2 - 28092054

VL - 1555

SP - 535

EP - 545

JO - Methods Mol Biol

JF - Methods Mol Biol

SN - 1064-3745

ER -