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Citations & References (12)
Thermo Scientific™
M-PER™ Mammalian Protein Extraction Reagent
Thermo Scientific M-PER Mammalian Protein Extraction Reagent is designed to provide highly efficient total soluble protein extraction from cultured mammalianRead more
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| Catalog Number | Quantity |
|---|---|
| 78505 | 1 L |
| 78501 | 250 mL |
| 78503 | 25 mL |
Catalog number 78505
Price (BRL)
8.019,64
Each
Quantity:
1 L
Price (BRL)
8.019,64
Each
Thermo Scientific M-PER Mammalian Protein Extraction Reagent is designed to provide highly efficient total soluble protein extraction from cultured mammalian cells.
Features of M-PER Mammalian Protein Extraction Reagent:
• Gentle—mild detergent lysis, yielding extracts that are immediately compatible with coomassie (Bradford) and BCA protein assays or SDS-PAGE
• Compatible—extracts soluble proteins in nondenatured state, enabling direct use in immunoprecipitation and other affinity purification procedures
• Amine-free and dialyzable—formulation ensures compatibility with subsequent assay systems
• Convenient—lyse adherent cells directly in plate or after scraping and washing in suspension
• Non-denaturing—maintain activity of luciferase, beta-galactosidase, CAT and other reporter genes as well or better than other suppliers' products and freeze/thaw methods
Product Details
The complete cell lysis reagent contains a mild, nondenaturing detergent that dissolves cell membranes to extract and solubilize total protein from most cellular compartments. Extraction is accomplished in only 5 minutes and requires little or no additional mechanical disruption. M-PER reagent is formulated for minimal interference with downstream biological applications. The reagent has been validated for use with several cell lines, including primary, suspension and adherent cell types; the resulting cell lysates are compatible with many downstream assays including immunoassays, enzyme assays and a variety of common reporter assays.
Cellular protein extraction—cell lysis to release the proteins of interest—is a key first step in many proteomics analysis procedures. M-PER reagent is designed to efficiently extract soluble protein from a variety of cell types, including primary cells and cells grown in suspension or adherent culture conditions. Performance of M-PER reagent was evaluated for yields of both total protein and specific target proteins from the various cellular compartments. Additionally, because M-PER reagent is formulated with dialyzable components that are devoid of primary amines, it is more compatible with certain downstream applications, such as luciferase, beta-galactosidase, and CAT assays, than other protein extraction methods.
Related Products
T-PER™ Tissue Protein Extraction Reagent
Features of M-PER Mammalian Protein Extraction Reagent:
• Gentle—mild detergent lysis, yielding extracts that are immediately compatible with coomassie (Bradford) and BCA protein assays or SDS-PAGE
• Compatible—extracts soluble proteins in nondenatured state, enabling direct use in immunoprecipitation and other affinity purification procedures
• Amine-free and dialyzable—formulation ensures compatibility with subsequent assay systems
• Convenient—lyse adherent cells directly in plate or after scraping and washing in suspension
• Non-denaturing—maintain activity of luciferase, beta-galactosidase, CAT and other reporter genes as well or better than other suppliers' products and freeze/thaw methods
Product Details
The complete cell lysis reagent contains a mild, nondenaturing detergent that dissolves cell membranes to extract and solubilize total protein from most cellular compartments. Extraction is accomplished in only 5 minutes and requires little or no additional mechanical disruption. M-PER reagent is formulated for minimal interference with downstream biological applications. The reagent has been validated for use with several cell lines, including primary, suspension and adherent cell types; the resulting cell lysates are compatible with many downstream assays including immunoassays, enzyme assays and a variety of common reporter assays.
Cellular protein extraction—cell lysis to release the proteins of interest—is a key first step in many proteomics analysis procedures. M-PER reagent is designed to efficiently extract soluble protein from a variety of cell types, including primary cells and cells grown in suspension or adherent culture conditions. Performance of M-PER reagent was evaluated for yields of both total protein and specific target proteins from the various cellular compartments. Additionally, because M-PER reagent is formulated with dialyzable components that are devoid of primary amines, it is more compatible with certain downstream applications, such as luciferase, beta-galactosidase, and CAT assays, than other protein extraction methods.
Related Products
T-PER™ Tissue Protein Extraction Reagent
For Research Use Only. Not for use in diagnostic procedures.
Specifications
FormatLiquid
Quantity1 L
Volume (Metric)1 L
Product LineM-PER
Product TypeProtein Extraction Reagent
Unit SizeEach
Contents & Storage
Upon receipt store product at room temperature.
Frequently asked questions (FAQs)
What are the standard lysis buffers used with mammalian cells for detection of protein expression by immunoprecipitation (IP) or Western blot analysis?
Is the M-PER Mammalian Protein Extraction Reagent (Cat. No. 78501, 78503, 78505) compatible with Mass spectrometry (MS)?
Can you provide the shelf-life for the M-PER Mammalian Protein Extraction Reagent?
Will M-PER Mammalian Protein Extraction Reagent extract membrane or cytoskeletal proteins?
When using the M-PER Mammalian Protein Extraction Reagent, is it necessary to remove cells from the plate? Should I use scraping or trypsinization to remove the cells from the plate?
Citations & References (12)
Citations & References
Abstract
Aromatase promoter I.f is regulated by progesterone receptor in mouse hypothalamic neuronal cell lines.
Journal:J Mol Endocrinol
PubMed ID:21628418
'Aromatase catalyzes the conversion of C(19) steroids to estrogens. Aromatase and progesterone, both of which function at different steps of steroidogenesis, are crucial for the sexually dimorphic development of the fetal brain and the regulation of gonadotropin secretion and sexual interest in adults. The aromatase gene (Cyp19a1) is selectively expressed
Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy.
Journal:J Virol
PubMed ID:21835792
'Autophagy has been shown to facilitate replication or production of hepatitis C virus (HCV); nevertheless, how HCV induces autophagy remains unclear. Here, we demonstrate that HCV nonstructural protein 4B (NS4B) alone can induce autophagy signaling; amino acid residues 1 to 190 of NS4B are sufficient for this induction. Further studies
Dual-modality gene reporter for in vivo imaging.
Journal:
PubMed ID:24347640
'The ability to track cells and their patterns of gene expression in living organisms can increase our understanding of tissue development and disease. Gene reporters for bioluminescence, fluorescence, radionuclide, and magnetic resonance imaging (MRI) have been described but these suffer variously from limited depth penetration, spatial resolution, and sensitivity. We
Exploitation of conserved eukaryotic host cell farnesylation machinery by an F-box effector of Legionella pneumophila.
Journal:J Exp Med
PubMed ID:20660614
'Farnesylation involves covalent linkage of eukaryotic proteins to a lipid moiety to anchor them into membranes, which is essential for the biological function of Ras and other proteins. A large cadre of bacterial effectors is injected into host cells by intravacuolar pathogens through elaborate type III-VII translocation machineries, and many
Intestinal GUCY2C prevents TGF-ß secretion coordinating desmoplasia and hyperproliferation in colorectal cancer.
Journal:
PubMed ID:24085786
Tumorigenesis is a multistep process that reflects intimate reciprocal interactions between epithelia and underlying stroma. However, tumor-initiating mechanisms coordinating transformation of both epithelial and stromal components are not defined. In humans and mice, initiation of colorectal cancer is universally associated with loss of guanylin and uroguanylin, the endogenous ligands for