Merck
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所有图片(3)

文件

安全信息

B11001

Sigma-Aldrich

EnPresso® B

Growth system for expressing protein in bacteria

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无菌性

sterile; γ-irradiated

形式

tablet

制造商/商品名称

(BioSilta Oy)

pH值(酸碱度)

6.8

运输

ambient

储存温度

room temp

一般描述

Enpresso B by BioSilta Oy

生化/生理作用

EnPresso® B是一种预灭菌生长体系,适合基于大肠杆菌的表达体系,提高功能性蛋白的表达水平。

EnPresso®生长体系可为微生物生长、代谢及蛋白表达提供最佳的培养条件。该体系可达到远超常规培养基的细胞密度,从而提高蛋白得率。通过控制生长速率及代谢环境,可大幅提高表达蛋白的正确折叠比例,提高蛋白产物的溶解率,最大限度降低包涵体的形成,确保蛋白产物的功能。

EnPresso®生长体系不仅可以维持稳定的pH,提供生长所需的充足矿物质元素、维生素及微量元素,而且可通过专利的EnBase 技术来确保多聚糖基质中的葡萄糖能够稳定、缓慢地释放。

了解EnPresso B 生长体系所有产品的订购信息。

外形

EnPresso® B 以试剂盒形式提供,足够进行4次50 ml 培养。试剂盒组分包括:
20包(白色),共40片
20包(黑色),共20片
1瓶(5 ml)Reagent A

法律信息

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

法规信息

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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
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

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