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Merck

B11001

EnPresso® B

Growth system for expressing protein in bacteria

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UNSPSC Code:
12352200
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sterility

sterile; γ-irradiated

form

tablet

manufacturer/tradename

(BioSilta Oy)

pH

6.8

shipped in

ambient

storage temp.

room temp

General description

Enpresso B by BioSilta Oy

Biochem/physiol Actions

EnPresso® B is a pre-sterilized growth system designed to increase the yield of functional protein from E. coli-based expression systems.

EnPresso® growth systems provide optimal conditions for growth, metabolism and protein expression in microbial cultures. Protein yields are increased by enabling cultures to reach far higher cell densities than those achieved using conventional media. By controlling growth rate and metabolism, a greater proportion of expressed protein can be correctly folded to improve solubility, minimize the risk of inclusion body formation, and ensure functionality of the final product.

EnPresso® growth systems maintain pH, provide adequate minerals, vitamins and trace elements to support growth, and use proprietary EnBase technology to ensure a constant, slow release of glucose from a polysaccharide substrate.

See all available products from EnPresso B Growth Systems.

Physical form

EnPresso® B is supplied in a kit providing sufficient reagents for 20 separate 50 ml cultures. Included in the kit:
40 tablets in 20 white bags
20 tablets in 20 black bags
1 bottle (5 ml) Reagent A

Legal Information

EnBase is a trademark of BioSilta Oy
EnPresso is a registered trademark of BioSilta Oy


pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

Aquatic Chronic 3 - Carc. 1B - Eye Irrit. 2 - Skin Sens. 1 - STOT RE 2

保管分類

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects


適用法令

試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。

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pdsc

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prtr

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fsl

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Jian Li et al.
Journal of biotechnology, 193, 16-22 (2014-12-03)
Heterologous expression of secondary metabolite biosynthesis pathways in a surrogate host, e.g. Escherichia coli, has emerged in recent years as an effective way to produce complex natural products. The nonribosomal peptide (NRP) antibiotic valinomycin has been recombinantly produced in E.
Thomas Horn et al.
Redox biology, 1, 566-577 (2013-11-28)
Mammalian lipoxygenases play a role in normal cell development and differentiation but they have also been implicated in the pathogenesis of cardiovascular, hyperproliferative and neurodegenerative diseases. As lipid peroxidizing enzymes they are involved in the regulation of cellular redox homeostasis
Jennifer Jaitzig et al.
ACS synthetic biology, 3(7), 432-438 (2013-12-20)
The structural complexity of nonribosomal peptides (NRPs) impeding economic chemical synthesis and poor cultivability of source organisms limits the development of bioprocesses for novel bioactive compounds. Since nonribosomal peptide synthetases (NRPSs) assemble NRPs from simple amino acid building blocks, heterologous