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Citações e referências (16)
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 mammalianLeia mais
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| Número do catálogo | Quantity |
|---|---|
| 78501 | 250 mL |
| 78503 | 25 mL |
| 78505 | 1 L |
Número do catálogo 78501
Preço (BRL)
2.740,85
Each
Quantity:
250 mL
Preço (BRL)
2.740,85
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.
Especificações
FormatLiquid
Quantity250 mL
Volume (Metric)250 mL
Product LineM-PER
Product TypeProtein Extraction Reagent
Unit SizeEach
Conteúdo e armazenamento
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?
Citações e referências (16)
Citações e referências
Abstract
Journal:
PubMed ID:30761918
Supply of methionine and arginine alters phosphorylation of mechanistic target of rapamycin (mTOR), circadian clock proteins, and α-s1-casein abundance in bovine mammary epithelial cells.
Journal:Food & function
PubMed ID:31942894
Methionine (Met) and arginine (Arg) regulate casein protein abundance through alterations in activity of the mechanistic target of rapamycin complex 1 (mTORC1) signaling pathway. A potential role for the circadian clock network on the regulation of protein synthesis, partly via activity of mTORC1, has been highlighted in non-ruminants. The main
Proteomics of protein trafficking by in vivo tissue-specific labeling.
Journal:Nature communications
PubMed ID:33888706
Conventional approaches to identify secreted factors that regulate homeostasis are limited in their abilities to identify the tissues/cells of origin and destination. We established a platform to identify secreted protein trafficking between organs using an engineered biotin ligase (BirA*G3) that biotinylates, promiscuously, proteins in a subcellular compartment of one tissue.
Methods for Systematic Identification of Membrane Proteins for Specific Capture of Cancer-Derived Extracellular Vesicles.
Journal:Cell reports
PubMed ID:30943406
Analysis of cancer-derived extracellular vesicles (EVs) in biofluids potentially provides a source of disease biomarkers. At present there is no procedure to systematically identify which antigens should be targeted to differentiate cancer-derived from normal host cell-derived EVs. Here, we propose a computational framework that integrates information about membrane proteins in
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