M-PER™ Mammalian Protein Extraction Reagent
M-PER™ Mammalian Protein Extraction Reagent
Thermo Scientific™

M-PER™ Mammalian Protein Extraction Reagent

Thermo Scientific M-PER Mammalian Protein Extraction Reagent은 배양된 포유류 세포에서 매우 효율적인 총 용해성 단백질을 추출해 줍니다.M-PER Mammalian Protein Extraction자세히 알아보기
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카탈로그 번호수량
785051 L
78501250 mL
7850325 mL
카탈로그 번호 78505
제품 가격(KRW)
1,350,000
Online offer
Ends: 31-Dec-2025
1,499,000
할인액 149,000 (10%)
Each
카트에 추가하기
수량:
1 L
대량 주문 또는 맞춤형 요청
제품 가격(KRW)
1,350,000
Online offer
Ends: 31-Dec-2025
1,499,000
할인액 149,000 (10%)
Each
카트에 추가하기
Thermo Scientific M-PER Mammalian Protein Extraction Reagent은 배양된 포유류 세포에서 매우 효율적인 총 용해성 단백질을 추출해 줍니다.

M-PER Mammalian Protein Extraction Reagent의 특징:

부드러움—약한 세척제 용해를 통해 coomassie(Bradford)와 BCA 단백질 분석이나 SDS-PAGE에서 즉시 사용할 수 있는 추출물 생성
호환성—비변성(nondenatured) 상태의 용해성 단백질을 추출하여 면역침강과 다른 친화 정제 절차에서 직접 사용 가능
아민 무함유 및 투석 가능—이 제형은 후속 분석 시스템에서 사용할 수 있도록 보장함
편의성—플레이트에서 직접 또는 현탁액에서 스크래핑(scraping)하고 세척한 후 부착 세포를 용해함
비변성(Non-denaturing)—luciferase, beta-galactosidase, CAT, 기타 리포터 유전자의 활성을 유지하거나 다른 공급업체의 제품과 동결/해동 방법보다 우수함

이 완전한 세포 용해 시약은 단 5분만에 세포막을 용해하고 총 용해성 단백질을 추출하는 비변성(nondenaturing) 세척제 제형입니다. M-PER Reagent은 기계적 분해가 거의 또는 전혀 필요하지 않고 반복적 동결/해동과 초음파 분해(sonication)보다 더 많은 단백질을 회수합니다. 이 포유류 세포 용해 시약은 매우 효율적이어서 부착 세포를 배양 접시에서 스크래핑하지 않아도 되고, 24-well과 96-well 플레이트에서 성장한 세포를 쉽게 직접 용해하고 분석할 수 있습니다. 그 결과 생성된 부착 및 현탁 세포의 세포 용해물은 면역분석, 효소 분석, 다양한 일반 리포터 분석을 포함한 다양한 후속 분석에서 사용할 수 있습니다.

단백질 추출은 일반적으로 단백질체학(proteomics) 분석 절차에서 첫 번째 주요 단계이므로, 세포는 먼저 용해되어 세포를 개방하고 관심 단백질을 방출해야 합니다. 기계적 분해, 액체 균질화, 초음파 분해(sonication), 반복적 동결/해동, 수동 분쇄를 포함한 여러 방법이 세포를 물리적으로 용해하는 데 일반적으로 사용됩니다.

관련 자료:
세포 용해 및 단백질 추출 검토

관련 제품:
세포 용해 및 단백질 추출 시약 전체 찾아보기
Protease and Phosphatase Inhibitor Cocktails and Tablets
For Research Use Only. Not for use in diagnostic procedures.
사양
형식Liquid
수량1 L
부피(미터법)1 L
제품라인M-PER
제품 유형Protein Extraction Reagent
Unit SizeEach
구성 및 보관
Upon receipt store product at room temperature.

자주 묻는 질문(FAQ)

What are the standard lysis buffers used with mammalian cells for detection of protein expression by immunoprecipitation (IP) or Western blot analysis?

The most commonly used buffer is RIPA Buffer with SDS. We offer RIPA Buffer (Cat. Nos. 89900 and 89901). We also offer the Pierce IP Lysis buffer (Cat. Nos. 87787 and 87788) as well as M-PER (Cat. Nos. 78501, 78503, and 78505).

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

Is the M-PER Mammalian Protein Extraction Reagent (Cat. No. 78501, 78503, 78505) compatible with Mass spectrometry (MS)?

As any other lysis reagent, M-PER has detergent and salts in its composition, and both type of components need to be removed before the MS analysis, as they will interfere with the analysis. According to the workflow used in the MS analysis, those might be removed before the MS analysis. We recommend removing detergents at the protein level. Both detergent and salts can be removed by dialysis.

Find additional tips, troubleshooting help, and resources within our Mass Spectrometry Support Center.

Can you provide the shelf-life for the M-PER Mammalian Protein Extraction Reagent?

The M-PER Mammalian Protein Extraction Reagent is covered under our general 1-year warranty and is guaranteed to be fully functional for 12 months from the date of shipment, if stored as recommended (room temperature). Please see section 8.1 of our Terms & Conditions of Sale (https://www.thermofisher.com/content/dam/LifeTech/Documents/PDFs/Terms-and-Conditions-of-Sale.pdf) for more details.

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.

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?

M-PER reagent works very well with adherent and suspension cells, making it unnecessary to separate the cells from the plate. However, if cell removal is desired, scraping is the recommended procedure for removing cells from the plate. Trypsinization is not recommended as the free trypsin left behind in the lysis solution can damage lysed proteins.

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

인용 및 참조 문헌 (12)

인용 및 참조 문헌
Abstract
Aromatase promoter I.f is regulated by progesterone receptor in mouse hypothalamic neuronal cell lines.
Authors:Yilmaz MB, Wolfe A, Zhao H, Brooks DC, Bulun SE,
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 ... More
Rab5 and class III phosphoinositide 3-kinase Vps34 are involved in hepatitis C virus NS4B-induced autophagy.
Authors:Su WC, Chao TC, Huang YL, Weng SC, Jeng KS, Lai MM,
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 ... More
Dual-modality gene reporter for in vivo imaging.
Authors:Patrick PS, Hammersley J, Loizou L, Kettunen MI, Rodrigues TB, Hu DE, Tee SS, Hesketh R, Lyons SK, Soloviev D, Lewis DY, Aime S, Fulton SM, Brindle KM,
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 ... More
Exploitation of conserved eukaryotic host cell farnesylation machinery by an F-box effector of Legionella pneumophila.
Authors:Price CT, Al-Quadan T, Santic M, Jones SC, Abu Kwaik Y,
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 ... More
Intestinal GUCY2C prevents TGF-ß secretion coordinating desmoplasia and hyperproliferation in colorectal cancer.
Authors:Gibbons AV, Lin JE, Kim GW, Marszalowicz GP, Li P, Stoecker BA, Blomain ES, Rattan S, Snook AE, Schulz S, Waldman SA,
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 ... More