Identifying the heterotrimeric complex stoichiometry of AMPK in skeletal muscle by immunoprecipitation

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Standard

Identifying the heterotrimeric complex stoichiometry of AMPK in skeletal muscle by immunoprecipitation. / Birk, Jesper Bratz; Wojtaszewski, Jørgen.

AMPK: Methods and Protecols. ed. / Dietbert Neumann; Benoit Viollet. New York : Humana Press, 2018. p. 203-213 (Methods in Molecular Biology; No. 1732).

Research output: Chapter in Book/Report/Conference proceeding › Book chapter › Research › peer-review

Harvard

Birk, JB & Wojtaszewski, J 2018, Identifying the heterotrimeric complex stoichiometry of AMPK in skeletal muscle by immunoprecipitation. in D Neumann & B Viollet (eds), AMPK: Methods and Protecols. Humana Press, New York, Methods in Molecular Biology, no. 1732, pp. 203-213. https://doi.org/10.1007/978-1-4939-7598-3_13

APA

Birk, J. B., & Wojtaszewski, J. (2018). Identifying the heterotrimeric complex stoichiometry of AMPK in skeletal muscle by immunoprecipitation. In D. Neumann, & B. Viollet (Eds.), AMPK: Methods and Protecols (pp. 203-213). Humana Press. Methods in Molecular Biology No. 1732 https://doi.org/10.1007/978-1-4939-7598-3_13

Vancouver

Birk JB, Wojtaszewski J. Identifying the heterotrimeric complex stoichiometry of AMPK in skeletal muscle by immunoprecipitation. In Neumann D, Viollet B, editors, AMPK: Methods and Protecols. New York: Humana Press. 2018. p. 203-213. (Methods in Molecular Biology; No. 1732). https://doi.org/10.1007/978-1-4939-7598-3_13

Author

Birk, Jesper Bratz ; Wojtaszewski, Jørgen. / Identifying the heterotrimeric complex stoichiometry of AMPK in skeletal muscle by immunoprecipitation. AMPK: Methods and Protecols. editor / Dietbert Neumann ; Benoit Viollet. New York : Humana Press, 2018. pp. 203-213 (Methods in Molecular Biology; No. 1732).

Bibtex

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title = "Identifying the heterotrimeric complex stoichiometry of AMPK in skeletal muscle by immunoprecipitation",
abstract = "The 5'-AMP-activated protein kinase is a complicated enzyme consisting of three different subunits, each of which is expressed as two or three isoforms. This gives the possibility of 12 different heterotrimeric complexes, which could have diverse functions within the cell. To map out which of these complexes are present and to what extent in skeletal muscle, we have used the immunoprecipitation technique and analyzed both the precipitates and the remaining supernatants for coprecipitation of complex partners. We have fine-tuned this method to give the best results on lysates from the skeletal muscle, liver, and heart muscle from mouse to man.",
keywords = "Faculty of Science, AMPK, Homogenization, Protein interaction, Immunoprecipitation, Western blot, In vitro setting, Antibody specificity",
author = "Birk, {Jesper Bratz} and J{\o}rgen Wojtaszewski",
note = "CURIS 2018 NEXS 079",
year = "2018",
doi = "10.1007/978-1-4939-7598-3_13",
language = "English",
isbn = "978-1-4939-7597-6",
series = "Methods in Molecular Biology",
publisher = "Humana Press",
number = "1732",
pages = "203--213",
editor = "Dietbert Neumann and Benoit Viollet",
booktitle = "AMPK",
address = "United States",

}

RIS

TY - CHAP

T1 - Identifying the heterotrimeric complex stoichiometry of AMPK in skeletal muscle by immunoprecipitation

AU - Birk, Jesper Bratz

AU - Wojtaszewski, Jørgen

N1 - CURIS 2018 NEXS 079

PY - 2018

Y1 - 2018

N2 - The 5'-AMP-activated protein kinase is a complicated enzyme consisting of three different subunits, each of which is expressed as two or three isoforms. This gives the possibility of 12 different heterotrimeric complexes, which could have diverse functions within the cell. To map out which of these complexes are present and to what extent in skeletal muscle, we have used the immunoprecipitation technique and analyzed both the precipitates and the remaining supernatants for coprecipitation of complex partners. We have fine-tuned this method to give the best results on lysates from the skeletal muscle, liver, and heart muscle from mouse to man.

AB - The 5'-AMP-activated protein kinase is a complicated enzyme consisting of three different subunits, each of which is expressed as two or three isoforms. This gives the possibility of 12 different heterotrimeric complexes, which could have diverse functions within the cell. To map out which of these complexes are present and to what extent in skeletal muscle, we have used the immunoprecipitation technique and analyzed both the precipitates and the remaining supernatants for coprecipitation of complex partners. We have fine-tuned this method to give the best results on lysates from the skeletal muscle, liver, and heart muscle from mouse to man.

KW - Faculty of Science

KW - AMPK

KW - Homogenization

KW - Protein interaction

KW - Immunoprecipitation

KW - Western blot

KW - In vitro setting

KW - Antibody specificity

U2 - 10.1007/978-1-4939-7598-3_13

DO - 10.1007/978-1-4939-7598-3_13

M3 - Book chapter

C2 - 29480477

SN - 978-1-4939-7597-6

T3 - Methods in Molecular Biology

SP - 203

EP - 213

BT - AMPK

A2 - Neumann, Dietbert

A2 - Viollet, Benoit

PB - Humana Press

CY - New York

ER -

ID: 191293422