Proteoextract membrane purification kit

Manufactured by Merck Group

The ProteoExtract membrane purification kit is a laboratory tool designed for the isolation and purification of membrane proteins from various biological samples. The kit utilizes a specialized extraction procedure to selectively extract and concentrate membrane proteins, facilitating their subsequent analysis and characterization.

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Lab products found in correlation

Protease phosphatase inhibitor, by Merck Group (2 mentions) Sypro ruby, by Thermo Fisher Scientific (2 mentions)

Close spelling variants of this product

ProteoExtract (5 citations)

2 protocols using proteoextract membrane purification kit

C. elegans Membrane Protein Isolation

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Synchronized day-3 C. elegans adults were collected after washing in S buffer, drained of excess liquid, and flash frozen in liquid nitrogen. The worm pellets were pulverized with a dry-ice-cooled mortar and pestle, and suspended in buffer with nonionic detergent (20-mM Hepes pH 7.4, 300-mM NaCl, 2-mM MgCl₂, 1% NP40), and protease/phosphatase inhibitors (MilliporeSigma, Darmstadt, Germany) at 0°C. Worm or cell debris was removed by brief centrifugation of lysate (5 min. at 3000 rpm). Native membrane-associated proteins were isolated from lysates with ProteoExtract membrane purification kit (MilliporeSigma) following the manufacturer's protocol, and either (a.) used for PIP₃ binding (see next section), or (b.) suspended in Laemmli buffer containing 2% SDS (w/v) and 0.3-M β-mercaptoethanol, heated 5 min at 95°C to dissolve proteins, and electro-phoresed on 4–20% polyacrylamide gels (SDS-PAGE). Gels were stained with SYPRO Ruby (ThermoFisher) to visualize total protein.

Ayyadevara S., Balasubramaniam M., Johnson J., Alla R., Mackintosh S.G, & Shmookler Reis R.J. (2016). PIP3-binding proteins promote age-dependent protein aggregation and limit survival in C. elegans. Oncotarget, 7(31), 48870-48886.

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Isolation and Analysis of Mouse Brain Proteins

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Frozen mouse brain samples (3 per group) were individually pulverized with a dry-ice-cooled mortar and pestle and suspended in buffer with nonionic detergent (20 mM HEPES pH 7.4, 0.3 M NaCl, 2 mM MgCl2, 1% [v/v] NP40) and protease/phosphatase inhibitors (Millipore-Sigma; Darmstadt, Germany) at 0 °C. Large debris was removed from lysate by brief centrifugation (5 min at 800 rpm). Native membrane-associated proteins were isolated from homogenates with ProteoExtract membrane purification kit (Millipore-Sigma) following the manufacturer’s protocol. Supernatants from these preparations were stored as soluble proteins. Pellets containing membrane-associated proteins were solubilized in either “Buffer 2”—for use in PIP₃ binding as described in the next section—or Laemmli buffer [2% SDS (w/v) and 0.3 M β-mercaptoethanol]. The latter were heated 5 min at 95 °C, and electrophoresed on 4–20% polyacrylamide, 1% SDS gels (SDS-PAGE). Gels were stained with SYPRO Ruby (ThermoFisher) to visualize total protein.

Ayyadevara S., Ganne A., Hendrix R.D., Balasubramaniam M., Shmookler Reis R.J, & Barger S.W. (2018). Functional assessments through novel proteomics approaches: Application to insulin/IGF signaling in neurodegenerative disease. Journal of neuroscience methods, 319, 40-46.

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