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無菌性
sterile; γ-irradiated
フォーム
tablet
メーカー／製品名
(BioSilta Oy)
pH
6.8
輸送温度
ambient
保管温度
room temp
詳細
Enpresso B by BioSilta Oy
生物化学的／生理学的作用
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.
物理的形状
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
法的情報
EnBase is a trademark of BioSilta Oy
EnPresso is a registered trademark of BioSilta Oy
シグナルワード
Danger
危険有害性情報
危険有害性の分類
Aquatic Chronic 3 - Carc. 1B - Eye Irrit. 2 - Skin Sens. 1 - STOT RE 2
保管分類コード
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。
毒物及び劇物取締法
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PRTR
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消防法
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労働安全衛生法名称等を表示すべき危険物及び有害物
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労働安全衛生法名称等を通知すべき危険物及び有害物
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カルタヘナ法
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Jan Code
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最新バージョンのいずれかを選択してください：
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
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
ライフサイエンス、有機合成、材料科学、クロマトグラフィー、分析など、あらゆる分野の研究に経験のあるメンバーがおります。.
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