推荐产品
特点
for bacteria and yeasts
制造商/商品名称
Eppendorf® 4309000027
一般描述
The Eppendorf Eporator is the perfect fit for you and your lab. Ask the specialists – your bacteria and yeast – they will confirm that the product features and performance of the Eppendorf Eporator make it very easy for you to carry out your experiments and obtain excellent results. Electroporation can be used for the transformation of electrocompetent bacteria and yeast with DNA. Compared to chemical methods, electroporation yields a much higher transformation efficiency. It also gives more reproducible results than other methods, is very simple to perform, and saves you valuable time. Treat your bacteria and yeast with something special – let them experience the Eppendorf Eporator!
应用
Eppendorf Eporator® is suitable:
- for the electroporation of various yeast and bacterial strains
- to transform electro-competent E. coli BL21(DE3) cells with pETM-20/LIC-g6pdh for overexpression
- to transform ElectroMAX DH5α-E cells
- to introduce DNA into Escherichia coli by electroporation
特点和优势
- Faster sample handling – simple one-button operation: just set the voltage or choose a preset parameter and insert a cuvette
- Intuitive use – the status information on the colored display minimizes errors
- Fast and freely programmable – two program buttons allow storage and recall of most commonly used parameters, default setting: P1 1,700 V and P2 2,500 V
- Safe electronics and integrated electroporation chamber eliminate voltage leaks and misuse
- Easy, GLP-compliant documentation via USB port – data from your experiments can be exported for documentation and analysis
法律信息
Eppendorf is a registered trademark of Eppendorf AG
Eppendorf Eporator is a registered trademark of Eppendorf AG
法规信息
新产品
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This study shows the effect of site-directed enzyme immobilization upon the enzyme activity of covalently bound glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides. Immobilization points were introduced at sterically accessible sites in order to control the protein's orientation and twice as much
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A CotA multicopper oxidase (MCO) from Bacillus pumilus, previously identified as a laccase, has been studied and characterized as a new bacterial bilirubin oxidase (BOD). The 59 kDa protein containing four coppers, was successfully over-expressed in Escherichia coli and purified
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