Mem-PER™ Plus Membrane Protein Extraction Kit
Mem-PER™ Plus Membrane Protein Extraction Kit
Thermo Scientific™

Mem-PER™ Plus Membrane Protein Extraction Kit

The Thermo Scientific Mem-PER Plus Membrane Protein Extraction Kit enables small-scale solubilization and enrichment of integral membrane proteins and membrane-associatedRead more
Have Questions?
Catalog NumberQuantity
89842300 mL
Catalog number 89842
Price (HKD)
4,081.00
Each
Add to cart
Quantity:
300 mL
Request bulk or custom format
Price (HKD)
4,081.00
Each
Add to cart
The Thermo Scientific Mem-PER Plus Membrane Protein Extraction Kit enables small-scale solubilization and enrichment of integral membrane proteins and membrane-associated proteins in a simple reagent-based procedure.

Features of the Mem-PER Plus Kit:

Extraction and isolation—produces minimal cross-contamination (typically less than 10%) of cytosolic protein into the membrane protein fraction
Cells or tissues—effective for extraction from cultured mammalian cells and mammalian tissues
Downstream compatibility—analyze membrane protein extracts by SDS-PAGE, western blotting, immunoprecipitation and protein assays
Fast and simple—isolation of membrane proteins in approximately one hour
No special equipment required—only a benchtop microcentrifuge, tubes, homogenizers, and pipettors are needed

The Mem-PER Plus Kit effectively isolates membrane proteins from cultured cells and tissues using a simple benchtop microcentrifuge procedure. Integral membrane proteins having one or two membrane-spanning domains are effectively solubilized and isolated from cytosolic proteins. The kit makes possible the extraction and selective enrichment of integral and attached membrane proteins from cultured mammalian cells, as well as from hard and soft mammalian tissues. The Mem-PER Plus Kit has many advantages compared to our original Mem-PER Kit. The protocol is simpler, and the fractions are directly compatible with many downstream applications such as SDS-PAGE, Western Blotting, BCA, immunoprecipitation, and amine-reactive protein labeling techniques.

Includes:
Kit contains a cell wash solution, permeabilization buffer, and solubilization buffer.

Traditional methods for isolation of membrane protein are tedious and time-consuming, and they require gradient separation and expensive ultracentrifugation equipment. The Mem-PER Plus Membrane Protein Extraction Kit is for the enrichment of integral membrane proteins and membrane associated proteins from cultured mammalian cells or tissue using a mild detergent-based selective extraction protocol. The use of selective detergent extraction eliminates the hassle of phase separation based on hydrophobicity, allowing better reproducibility and higher throughput.

The cells are first permeabilized with a mild detergent, allowing the release of soluble cytosolic proteins, after which a second detergent solubilizes membrane proteins. Extraction efficiencies and yields will vary depending on cell type as well as the number of times the integral membrane protein spans the lipid bilayer. Membrane proteins with one or two transmembrane domains are typically extracted with an efficiency of up to 90%. Cross-contamination of cytosolic proteins into the membrane fraction is usually less than 10%.

More Product Data
Efficient mammalian membrane protein extraction

Related Products
Subcellular Protein Fractionation Kit for Cultured Cells
Subcellular Protein Fractionation Kit for Tissues
Benchtop Centrifuges
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Quantity300 mL
Reagent TypeCell Lysis Buffer, Detergent Solution, Subcellular Fractionation
Sufficient For50 Samples
FormLiquid
Product LineMem-PER
Product TypeProtein Extraction Kit
Unit SizeEach
Contents & Storage
Upon receipt store Cell Wash Solution and Solubilization Buffer at 4°C. Aliquot and store Permeabilization Buffer at -20°C to avoid freeze/thaws. Product is shipped on ice.

Frequently asked questions (FAQs)

I am using the Mem-PER Plus Membrane Protein Extraction Kit with less than 5 X 10E6 cells. Should I scale down the amount of reagents accordingly?

The kit reagents can be scaled up or down as long as the ratio of reagents to cells is maintained. However, we don't have specific guidelines for the range of cell numbers that can be used because protein yields can vary depending on the cell line. It is important to note that the process of scaling the kit reagents up or down and determining the appropriate cell numbers for optimal protein yield will require empirical optimization by the investigator.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

What kind of detergent does the Permeabilization Buffer from the Mem-PER Plus Membrane Protein Extraction Kit (Cat. No 89842) contain?

The composition of the Permeabilization Buffer, including the identity and concentration of any detergent therein, is proprietary. However, the Permeabilization Buffer contains a very small amount of a weak non-ionic detergent to facilitate the permeabilization of the cells and release of the cytosolic proteins.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center

Will the Mem-PER Plus Membrane Protein Extraction Kit (Cat. No. 89842) extract membrane proteins from the plasma membrane only or also from other intra-cellular membranes (e.g., nuclear, mitochondrial, endoplasmic reticulum)?

The Permeabilization buffer in the Mem-PER Plus Membrane Protein Extraction Kit (Cat. No. 89842) creates pores in the plasma membrane of cells that releases cytosolic proteins. The permeabilized cells are centrifuged, and the supernatant contains the cytosolic protein fraction. The pellet is then resuspended in the Solubilization buffer containing a proprietary detergent that solubilizes plasma, mitochondrial, and ER membrane proteins. Subsequent centrifugation yields a supernatant containing solubilized membrane and membrane-associated proteins.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center

Can microalgae be processed with the Mem-PER Plus Membrane Protein Extraction Kit (Cat. No. 89842)?

The Mem-PER Plus Membrane Protein Extraction Kit is not suitable for any organism that has a cell wall, including algae, plants, yeast, or bacteria.

Find additional tips, troubleshooting help, and resources within our Protein Purification and Isolation Support Center.

Will M-PER Mammalian Protein Extraction Reagent extract membrane or cytoskeletal proteins?

M-PER Mammalian Protein Extraction Reagent can extract some membrane or cytoskeletal proteins, but the extraction efficiency is not consistent. The reagent was not intended to specifically extract these proteins. We recommend using Mem-PER Plus Membrane Protein Extraction Kit (Cat. No. 89842) for membrane protein extraction or Subcellular Protein Fractionation Kit for Cultured Cells (Cat. No. 78840) for compartmental extraction.

Find additional tips, troubleshooting help, and resources within our Cell Lysis and Fractionation Support Center.

Citations & References (7)

Citations & References
Abstract
P-Rex1 Mediates Glucose-Stimulated Rac1 Activation and Insulin Secretion in Pancreatic β-Cells.
Authors:Thamilselvan V,Gamage S,Harajli A,Chundru SA,Kowluru A
Journal:Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology
PubMed ID:33347743
BACKGROUND/AIMS: Despite the published evidence implicating phosphoinositide 3-kinase (PI3-kinase) in the regulation of islet function, limited information is available on the putative contributory roles of its downstream signaling steps, including the phosphatidylinositol-3,4,5-trisphosphate-dependent Rac exchange factor 1 (P-Rex1) signaling pathway in the islet β-cell. Therefore, we investigated potential roles for P-Rex1 ... More
Baicalein promotes KDM4E to induce BICD1 and inhibit triple-negative breast cancer progression by blocking PAR1 signaling.
Authors:Dong Y,He G,Chen K,He X,Pan M,Huang X,Yu X,Xia J
Journal:Molecular carcinogenesis
PubMed ID:38607237
Baicalein has been implicated in the chemotherapy overcoming triple-negative breast cancer (TNBC). However, many unanswered questions remain regarding its role in treating TNBC. Here, we sought to demonstrate the molecular pathway mediated by baicalein in TNBC. Lysine-specific demethylase 4E (KDM4E), reduced in TNBC cells, was identified as a target protein ... More
Exposure to Hypoxic Conditions Up-regulates HER2 in Breast Cancer Cell Lines.
Authors:Suganuma N,Saito N,Yasukawa M,Yamanaka T,Yamashita T,Miyagi Y,Saito A,Hoshino D
Journal:Anticancer research
PubMed ID:39626936
BACKGROUND/AIM: Tissue specimen quality is becoming increasingly important for basic research and routine clinical results. Warm ischemia time (WIT) affects human epidermal growth factor receptor 2 (HER2) immunohistochemistry (IHC) scores. However, the role of WIT on HER2 modulation remains unclear. We hypothesized that the WIT-mediated increase in HER2 IHC scores ... More
Selective Enrichment of Membrane Proteins by Partition Phase Separation for Proteomic Studies.
Authors:Qoronfleh MW, Benton B, Ignacio R, Kaboord B
Journal:J Biomed Biotechnol
PubMed ID:14615633
'The human proteome project will demand faster, easier, and more reliable methods to isolate and purify protein targets. Membrane proteins are the most valuable group of proteins since they are the target for 70-80% of all drugs. Perbio Science has developed a protocol for the quick, easy, and reproducible isolation ... More
Ubl4A is required for insulin-induced Akt plasma membrane translocation through promotion of Arp2/3-dependent actin branching.
Authors:Zhao Y, Lin Y, Zhang H, Mañas A, Tang W, Zhang Y, Wu D, Lin A, Xiang J
Journal:
PubMed ID:26195787
'The serine-threonine kinase Akt is a key regulator of cell proliferation and survival, glucose metabolism, cell mobility, and tumorigenesis. Activation of Akt by extracellular stimuli such as insulin centers on the interaction of Akt with PIP3 on the plasma membrane, where it is subsequently phosphorylated and activated by upstream protein ... More