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Rosetta(DE3) Competent Cells - Novagen

Escherichia coli, rod shaped

Sinônimo(s):

BL21 derivatives

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About This Item

Código UNSPSC:
41106202
NACRES:
NA.81

product name

Rosetta(DE3) Competent Cells - Novagen, Rosetta host strains are BL21 derivatives designed to enhance the expression of eukaryotic proteins that contain codons rarely used in E. coli.

fonte biológica

Escherichia coli

Nível de qualidade

fabricante/nome comercial

Novagen®

condição de armazenamento

OK to freeze

modo de crescimento

adherent or suspension

morfologia

rod shaped

técnica(s)

microbiological culture: suitable

Condições de expedição

wet ice

temperatura de armazenamento

−70°C

Descrição geral

Genotype: F-ompT hsdSB(rB- mB-) gal dcm (DE3) pRARE (CamR)





This product contains genetically modified organisms (GMO). Within the EU GMOs are regulated by Directives 2001/18/EC and 2009/41/EC of the European Parliament and of the Council and their national implementation in the member States respectively. This legislation obliges us to request certain information about you and the establishment where the GMOs are being handled. Click here for Enduser Declaration (EUD) Form.
Rosetta host strains are BL21 derivatives designed to enhance the expression of eukaryotic proteins that contain codons rarely used in E. coli. These strains supply tRNAs for AGG, AGA, AUA, CUA, CCC, GGA codons on a compatible chloramphenicol-resistant plasmid. Thus the Rosetta strains provide for “universal” translation which is otherwise limited by the codon usage of E. coli. The tRNA genes are driven by their native promoters. In Rosetta(DE3)pLysS, the rare tRNA genes are present on the same plasmids that carries the T7 lysozyme gene.

DE3 indicates that the host is a lysogen of λDE3, and therefore carries a chromosomal copy of the T7 RNA polymerase gene under control of the lacUV5 promoter. Such strains are suitable for production of protein from target genes cloned in pET vectors by induction with IPTG.
Rosetta host strains are BL21 derivatives designed to enhance the expression of eukaryotic proteins that contain codons rarely used in E. coli.

Componentes

0.4 ml1 mlComponent

•2 × 0.2 ml5 × 0.2 mlRosetta(DE3) Competent Cells

•2 × 2 ml4 × 2 mlSOC Medium

•2 ng2 ngTest Plasmid

Advertência

Toxicity: Multiple Toxicity Values, refer to MSDS (O)

Informações legais

NOVAGEN is a registered trademark of Merck KGaA, Darmstadt, Germany

Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 2


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Shuo Jiang et al.
Developmental cell, 49(5), 711-730 (2019-04-30)
The correct localization of Hedgehog effectors to the tip of primary cilia is critical for proper signal transduction. The conserved non-motile kinesin Kif7 defines a "cilium-tip compartment" by localizing to the distal ends of axonemal microtubules. How Kif7 recognizes microtubule ends
Naomichi Takemata et al.
Cell, 179(1), 165-179 (2019-09-21)
The three-dimensional organization of chromosomes can have a profound impact on their replication and expression. The chromosomes of higher eukaryotes possess discrete compartments that are characterized by differing transcriptional activities. Contrastingly, most bacterial chromosomes have simpler organization with local domains
Caitlin I Stoddard et al.
Molecular cell, 73(1), 73-83 (2018-11-13)
DNA methylation and H3K9me are hallmarks of heterochromatin in plants and mammals, and are successfully maintained across generations. The biochemical and structural basis for this maintenance is poorly understood. The maintenance DNA methyltransferase from Zea mays, ZMET2, recognizes dimethylation of
Emily Anne Scarborough et al.
eLife, 8 (2019-05-03)
Regulation of the outer kinetochore complex Ndc80 is essential to ensure correct kinetochore-microtubule attachments during mitosis. Here, we present a novel mechanism of regulation that is intrinsic to its structure; tight bending of the Ndc80 complex inhibits its microtubule binding.
Koning Shen et al.
Molecular cell, 74(4), 729-741 (2019-04-16)
The nascent polypeptide-associated complex (NAC) is a conserved ribosome-associated protein biogenesis factor. Whether NAC exerts chaperone activity and whether this function is restricted to de novo protein synthesis is unknown. Here, we demonstrate that NAC directly exerts chaperone activity toward

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