M-PER™ Mammalian Protein Extraction Reagent

Citations & References (12)

Thermo Scientific™

M-PER™ Mammalian Protein Extraction Reagent

Name: M-PER™ Mammalian Protein Extraction Reagent
SKU: 78503

Thermo Scientific M-PER Mammalian Protein Extraction Reagentは、培養哺乳類細胞から総可溶性タンパク質を効率的に抽出できるよう設計されています。M-PER Mammalian詳細を見る

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製品番号（カタログ番号）	数量
78503	25 mL
78501	250 mL
78505	1 L

3 オプション

製品番号（カタログ番号） 78503

価格（JPY）

21,600

Each

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数量:

25 mL

一括またはカスタム形式をリクエストする

Thermo Scientific M-PER Mammalian Protein Extraction Reagentは、培養哺乳類細胞から総可溶性タンパク質を効率的に抽出できるよう設計されています。

M-PER Mammalian Protein Extraction Reagentの特長：

•穏やか—穏やかな界面活性剤により溶解し、抽出物はcoomassie（Bradford）およびBCAタンパク質アッセイ、またはSDS-PAGEにすぐに使用可能
• 適合性—可溶性タンパク質を非変性状態で抽出するため、免疫沈降やその他のアフィニティー精製に直接使用可能
• アミノ不含有で透析可能—以降のアッセイシステムとの適合性を確保する組成
• 利便性—接着細胞をプレート上で直接、または剥離して懸濁液で洗浄した後に溶解可能
• 非変性—ルシフェラーゼ、β-ガラクトシダーゼ、CAT、およびその他のレポーター遺伝子活性を他社製品やその他の凍結融解方法と同等、またはより良好に維持

製品の詳細

この完全な細胞溶解試薬は穏やかな非変性界面活性剤を含有し、わずか5分で細胞膜を溶解して総可溶性細胞タンパク質を抽出します。抽出はわずか5分で完了し、機械的破壊はまったく、またはほとんど必要ありません。M-PER試薬は、ダウンストリームの生物学的アプリケーションへの干渉を最小限に抑えるように調製されています。この試薬は、初代細胞、懸濁細胞、および接着細胞などのさまざまな細胞株で使用できることが検証済みです；得られる細胞ライセートは、イムノアッセイ、酵素アッセイ、およびさまざまな一般的なレポーターアッセイなどの多くのダウンストリームアッセイで使用できます。

細胞タンパク質の抽出—目的のタンパク質を分離するための細胞溶解—は多くのプロテオミクス解析手順で重要な最初のスッテプです。M-PER試薬は、初代細胞や、懸濁または接着培養条件下で培養した細胞など、さまざまな細胞タイプから可溶性タンパク質を効率的に抽出するよう設計されています。M-PER試薬の性能は、さまざまな細胞内コンパートメントから総タンパク質および特定の目的タンパク質を回収できることが評価済みです。さらに、M-PER試薬は一級アミンを含有しない透析可能な成分で調製されているため、ルシフェラーゼ、β-ガラクトシダーゼ、およびCATアッセイなどの特定のダウンストリームアプリケーションで、他のタンパク質抽出法よりも優れた適合性を有します。

関連製品
T-PER™ Tissue Protein Extraction Reagent

研究用途にのみご使用ください。診断目的には使用できません。

仕様

フォーマット液体

数量25 mL

容量（メートル法）25 mL

製品ラインM-PER

製品タイプタンパク質抽出試薬

Unit SizeEach

組成および保存条件

製品を受け取り後、室温で保存。

よくあるご質問（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.

View all M-PER™ Mammalian Protein Extraction Reagent, 25 mL FAQs

引用および参考文献 (12)

引用および参考文献

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

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