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CelLytic MEM Protein Extraction Kit

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Membrane protein extraction kit

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General description

CelLytic MEM Protein Extraction Kit offers a fast and convenient method to isolate hydrophobic and raft microdomain associated proteins from cells. The method is based on phase separation and does not require cell membrane isolation. The separated proteins can be used for further experiments such as SDS-PAGE, Western blotting, dot blotting, and immunoprecipitation. The kit has been tested on, but not limited to, HeLa, HEK-293, NIH 3T3, COS and CHO cell lines.
Membrane proteins make up around 20-30% of an organism′s genome and serve as cellular gatekeepers, regulators, and sensors. They have diverse cellular functions, such as shielding the cell from external toxins, being the starting point of intracellular signaling cascades, and retaining critical ion concentrations.


CelLytic MEM Protein Extraction Kit has been used for de novo lipogenesis measurements using hepatocytes and to extract membrane proteins for western blotting.


Sufficient reagents supplied for 80 tests.

Legal Information

CelLytic is a trademark of Sigma-Aldrich Co. LLC

Kit Components Only

Product No.

  • Lysis and Separation Buffer 50 mL

  • Wash Buffer for CelLytic MEM 50 mL

  • Sodium Chloride, 4M Solution 1.5 mL

Kit Components Also Available Separately

Product No.

  • P8340Protease Inhibitor Cocktail, for use with mammalian cell and tissue extracts, DMSO solution 1 mLSDS


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Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Skin Irrit. 2

Storage Class Code

10 - Combustible liquids



Flash Point(F)

188.6 °F - closed cup

Flash Point(C)

87 °C - closed cup

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Amanda Y van Tilburg et al.
Microbial biotechnology, 15(5), 1633-1651 (2021-12-03)
A form of lateral membrane compartmentalization in bacteria is represented by functional membrane microdomains (FMMs). FMMs are important for various cellular processes and offer application possibilities in microbial biotechnology. We designed a lipidomics method to directly measure relative abundances of
Elisabeth P Carpenter et al.
Current opinion in structural biology, 18(5), 581-586 (2008-08-05)
Membrane protein structural biology is still a largely unconquered area, given that approximately 25% of all proteins are membrane proteins and yet less than 150 unique structures are available. Membrane proteins have proven to be difficult to study owing to
Tomoaki Furuta et al.
Cancer science, 112(9), 3722-3731 (2021-06-12)
The rBC2LCN lectin, known as a stem cell marker probe that binds to an H type 3 fucosylated trisaccharide motif, was recently revealed to also bind to pancreatic ductal adenocarcinoma (PDAC) cells. A lectin-drug conjugate was generated by fusing rBC2LCN
Marc Bramkamp et al.
Microbiology and molecular biology reviews : MMBR, 79(1), 81-100 (2015-02-06)
An interesting concept in the organization of cellular membranes is the proposed existence of lipid rafts. Membranes of eukaryotic cells organize signal transduction proteins into membrane rafts or lipid rafts that are enriched in particular lipids such as cholesterol and
Xiangquan Kong et al.
Molecular biology of the cell, 27(25), 3972-3979 (2016-11-01)
Hyaluronan (HA) in the endothelial glycocalyx serves as a mechanotransducer for high-shear-stress-stimulated endothelial nitric oxide synthase (eNOS) phosphorylation and nitric oxide (NO) production. Low shear stress (LSS) has been shown to contribute to endothelial inflammation and atherosclerosis by impairing the

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