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Merck
CN

B21200

Sigma-Aldrich

EnPresso® B Defined Nitrogen-free

Growth system for expressing protein in bacteria, Starter Pack

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UNSPSC Code:
12352200
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sterility

sterile; γ-irradiated

form

tablet

pH

6.8

shipped in

ambient

storage temp.

room temp

Biochem/physiol Actions

EnPresso® B Defined Nitrogen-free is a pre-sterilized, chemically-defined growth system designed to increase the yield of 15N-labelled proteins.

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 4 separate 50 ml cultures. Included in the kit:
8 tablets in 4 blue bags
1 bottle (1 ml) Reagent A

Other Notes

BioSilta performance guarantee for EnPresso Starter Packs:
For expression of recombinant proteins in E. coli, BioSilta guarantees a minimun 5-fold increase in protein yield from EnPresso B Defined nitrogen-free growth system when compared to yields from comercially available minimal media. Comparisons must be made using an EnPresso Starter Pack and a commercially-available growth media. Manufacturer′s protocols must be followed exactly. Cultures must be adequately aerated in shake flasks or 24 deepwell plates. Failure to achieve minimum 5-fold increase in yield must be reported to BioSilta (through Sigma Technical Services) within 21 days of product delivery and include quantitative data from the EnPresso growth system and the comparative growth media. Subject to data review, BioSilta/Sigma will refund the purchase price of the EnPresso Starter Pack. Please note this guarantee does not apply to membrane proteins and proteins expressed into the periplasm as performance data is not yet available.

Legal Information

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

Signal Word

Danger

Hazard Statements

Hazard Classifications

Aquatic Chronic 2 - Carc. 1A - Carc. 1B Inhalation - Skin Sens. 1 - STOT RE 2

Storage Class Code

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

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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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
F Mahboudi et al.
Journal of applied microbiology, 114(2), 364-372 (2012-11-07)
A novel chimeric-truncated form of tissue-type plasminogen activator (t-PA) with improved fibrin affinity and resistance to PAI was successfully produced in CHO expression system during our previous studies. Considering advantages of prokaryotic expression systems, the aim in this study was
Thomas Horn et al.
Biochimica et biophysica acta, 1831(12), 1702-1713 (2013-08-21)
Mammalian lipoxygenases belong to a family of lipid-peroxidizing enzymes, which have been implicated in cardiovascular, hyperproliferative and neurodegenerative diseases. Here we report that a naturally occurring mutation in the hALOX15 gene leads to expression of a catalytically near-null enzyme variant
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
Kristof Zarschler et al.
Microbial cell factories, 12, 97-97 (2013-10-29)
For their application in the area of diagnosis and therapy, single-domain antibodies (sdAbs) offer multiple advantages over conventional antibodies and fragments thereof in terms of size, stability, solubility, immunogenicity, production costs as well as tumor uptake and blood clearance. Thus

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