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B-PER™ Bacterial Protein Extraction Reagent
B-PER™ Bacterial Protein Extraction Reagent
Thermo Scientific™

B-PER™ Bacterial Protein Extraction Reagent

Thermo Scientific B-PER Reagent (in Phosphate Buffer) is an easy-to-use cell lysis reagent is a nonionic detergent-based solutions that effectively深入閱讀
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產品號碼Quantity
78243Promo Image165 mL
78248Promo Image500 mL
90084Promo Image250 mL
產品號碼 78243
價格 (HKD)
2,227.00
Each
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165 mL
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價格 (HKD)
2,227.00
Each
新增至購物車
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Thermo Scientific B-PER Reagent (in Phosphate Buffer) is an easy-to-use cell lysis reagent is a nonionic detergent-based solutions that effectively disrupt cells and solubilize native or recombinant proteins without denaturation. All B-PER Reagents are compatible with downstream applications, such as affinity chromatography (e.g., immobilized metal affinity chromatography, glutathione chromatography), SDS-PAGE, and protein quantification (e.g., Pierce BCA Protein Assay, Pierce 660nm Protein Assay). Depending on the particular application, protease inhibitors, salts, reducing agents, denaturants, and chelating agents may be added to the reagent.

Features of the B-PER Bacterial Protein Extraction Reagent:

• Detergent in sodium phosphate buffer; no enzyme components
• Amine-free formulation for direct compatibility of lysate with amine-reactive labeling and crosslinking

All Thermo Scientific B-PER Protein Extraction Reagents are:
Ready to use—one-step cell lysis of gram-positive and gram-negative bacteria using a mild, nonionic detergent (proprietary) in Tris or phosphate buffer formulations
Fast and simple—just add B-PER Reagent to a bacterial pellet, incubate with mixing for 10 to 15 minutes and recover soluble proteins after pelleting the cell debris
Convenient B-PER Complete Reagent contains lysozyme and a universal nuclease in a single formulation with 4°C storage
Excellent yields—recover recombinant proteins from bacterial lysates or purify inclusion bodies to near-homogeneous levels
Flexible—B-PER Reagents are suitable for any scale of protein extraction and are available in phosphate and 1X and 2X Tris formulations, with and without enzymes
Compatible—completely compatible with addition of protease inhibitors, and the resulting protein extract can be used in protein assays, typical affinity purification methods (e.g., GST, 6xHis) and other applications

Convenient, Ready-to-use Formats
B-PER Bacterial Extraction Reagents are more effective than traditional sonication and typical homemade lysis buffers, many of which include detergents and components that interfere with downstream applications. B-PER Reagents are formulated in Tris or phosphate buffer at physiological pH. They extract native and soluble recombinant proteins and yield lysates that are directly compatible with most downstream workflows such as electrophoresis, affinity purification, immunoprecipitation, protein interaction analysis, crosslinking and protein labeling.

More Product Data
Improved, all-in-one B-PER Reagent for bacterial protein extraction

Related Products
B-PER™ Bacterial Protein Extraction Reagent
B-PER™ Complete Bacterial Protein Extraction Reagent
B-PER™ II Bacterial Protein Extraction Reagent (2X)
For Research Use Only. Not for use in diagnostic procedures.
規格
DescriptionB-PER Bacterial Protein Extraction Reagent
Quantity165 mL
Volume (Metric)165 mL
Product LineB-PER™
Product TypeBacterial Protein Extraction Reagent
Unit SizeEach
內容物與存放
Store at room temperature.
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批號Certificate TypeDateCatalog Number(s)
3214968Certificate of AnalysisJun 18, 202590084
3213944Certificate of AnalysisJun 10, 202578243
3212528Certificate of AnalysisMay 06, 202578248
AB408940Certificate of AnalysisMar 14, 202578243
AB405513Certificate of AnalysisFeb 18, 202578248
顯示 5 個結果, 在上方搜尋特定憑證

安全資料表

常見問答集 (常見問題)

B-PER II Reagent contains more detergent making it ideal for extracting proteins from small bacterial cultures with less than 20 mL in volume.

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

B-PER Reagent utilizes a proprietary, mild nonionic detergent in a 20 mM Tris HCl, pH 7.5 buffer. No enzymatic components are present in the B-PER solution itself (B-PER Complete Bacterial Protein Extraction Reagent, Cat. No. 89821, 89822 does contain enzymes). Depending on your particular protein, you may need to add components such as salt, lysozyme, protease inhibitors, reducing agents and chelating agents. Other ready-to-use formats include B-PER II Bacterial Protein Extraction Reagent (2X), B-PER Reagent (in Phosphate Buffer), and B-PER with Enzymes Bacterial Protein Extraction Kit.

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

For 1 gram of cells add 4 mL of B-PER Reagent.

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

While this is protein-dependent, many proteins have been successfully tested in downstream applications (reporter assays, immunoprecipitation and beta-Gal assays), including GST and 6xHis proteins. Otherwise, samples can be diluted or dialyzed to remove any interfering substances.

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

This is often an indication of the presence of large amounts of DNA in the extract. This viscosity will be greatly decreased upon addition of DNase I (Cat. No. 90083).

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

引用資料與參考文獻 (4)

引用資料與參考文獻
Abstract
Evasion of Toll-like receptor 5 by flagellated bacteria.
Authors:Andersen-Nissen E, Smith KD, Strobe KL, Barrett SL, Cookson BT, Logan SM, Aderem A
Journal:Proc Natl Acad Sci U S A
PubMed ID:15956202
'Toll-like receptor 5 (TLR5) recognizes an evolutionarily conserved site on bacterial flagellin that is required for flagellar filament assembly and motility. The alpha and epsilon Proteobacteria, including the important human pathogens Campylobacter jejuni, Helicobacter pylori, and Bartonella bacilliformis, require flagellar motility to efficiently infect mammalian hosts. In this study, we ... More
Metaproteomics: Evaluation of protein extraction from activated sludge.
Authors:Hansen SH, Stensballe A, Nielsen PH, Herbst FA
Journal:
PubMed ID:25116144
Metaproteomic studies of full-scale activated sludge systems require reproducible protein extraction methods. A systematic evaluation of three different extractions protocols, each in combination with three different methods of cell lysis, and a commercial kit were evaluated. Criteria used for comparison of each method included the extracted protein concentration and the ... More
Mutations of the gene encoding the protein kinase A type I-alpha regulatory subunit in patients with the Carney complex.
Authors: Kirschner L S; Carney J A; Pack S D; Taymans S E; Giatzakis C; Cho Y S; Cho-Chung Y S; Stratakis C A;
Journal:Nat Genet
PubMed ID:10973256
Carney complex (CNC) is a multiple neoplasia syndrome characterized by spotty skin pigmentation, cardiac and other myxomas, endocrine tumours and psammomatous melanotic schwannomas. CNC is inherited as an autosomal dominant trait and the genes responsible have been mapped to 2p16 and 17q22-24 (refs 6, 7). Because of its similarities to ... More
Identification, expression, and substrate specificity of a mammalian beta-carotene 15,15'-dioxygenase.
Authors:Redmond TM, Gentleman S, Duncan T, Yu S, Wiggert B, Gantt E, Cunningham FX
Journal:J Biol Chem
PubMed ID:11092891
We have identified from mouse the first mammalian beta-carotene 15,15'-dioxygenase (beta-CD), a crucial enzyme in development and metabolism that governs the de novo entry of vitamin A from plant-derived precursors. beta-CD is related to the retinal pigment epithelium-expressed protein RPE65 and belongs to a diverse family that includes the plant ... More
4 total citations

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