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Lambda protein phosphatase

Manufactured by Merck Group
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Lambda protein phosphatase is an enzyme that can remove phosphate groups from proteins. It is commonly used in biochemical and molecular biology research applications to study protein phosphorylation and dephosphorylation processes.

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Lab products found in correlation

Protein g sepharose 4 fast flow, by GE Healthcare (1 mentions) Dnase 1, by Merck Group (1 mentions)

Close spelling variants of this product

Phosphatases (7 citations) Lambda phosphatase (4 citations) Lambda Protein phosphatase (λPPase) (2 citations)

2 protocols using lambda protein phosphatase

1

Dephosphorylation and PARP Activity

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Dephosphorylation was performed with 100 µg of Rin-5F nuclear lysates that were incubated for 20 min at 30°C with 400 units of lambda protein phosphatase (Sigma, Saint Louis, MO, USA) in reaction buffer supplemented with 1× MnCl2, all provided by the manufacturer. After the incubation, the dephosphorylated nuclear lysates were immediately used for measuring PARP activity.
Grdović N., Dinić S., Mihailović M., Uskoković A., Jovanović J.A., Poznanović G., Wagner L, & Vidaković M. (2014). CXC Chemokine Ligand 12 Protects Pancreatic β-Cells from Necrosis through Akt Kinase-Mediated Modulation of Poly(ADP-ribose) Polymerase-1 Activity. PLoS ONE, 9(7), e101172.
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2

MED1-BRCA1 Complex Formation in U2OS Cells

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The formation of a MED1–BRCA1 complex in U2OS cells was analyzed by IP. Whole-cell extracts of U2OS cells using RIPA buffer were used for IP with anti-BRCA1 and anti-MED1 antibodies or preimmune IgG. The immunoprecipitate was subjected to 30 ml of protein G Sepharose 4 Fast Flow (GE Healthcare) and subsequently immunoblotted with anti-BRCA1, anti-MED1, or anti-IgG antibodies. Immunoprecipitation samples were treated with lambda protein phosphatase (Sigma Aldrich), DNase I (Sigma Aldrich), or RNase (Sigma Aldrich) according to the manufacturer’s protocol.
Honjoh H., Tanikawa M., Wada-Hiraike O., Oda K., Inaba H., Kukita A., Kawata Y., Kusakabe M., Tsuchimochi S., Taguchi A., Miyamoto Y., Sone K., Tsuruga T., Mori-Uchino M., Matsumoto Y, & Osuga Y. (2022). MED1, a novel binding partner of BRCA1, regulates homologous recombination and R-loop processing. Scientific Reports, 12, 17140.
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