B11001
EnPresso® B
Growth system for expressing protein in bacteria
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About This Item
UNSPSC Code:
12352200
Productos recomendados
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.
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
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
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Referencia del producto
Descripción
Precios
signalword
Danger
hcodes
Hazard Classifications
Aquatic Chronic 3 - Carc. 1B - Eye Irrit. 2 - Skin Sens. 1 - STOT RE 2
Storage Class
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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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
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.
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
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
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
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