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Origami B(DE3) Competent Cells - Novagen

Origami B host strains carry the same mutations as the original Origami strain, except that they are derived from a lacZY mutant of BL21 to enable precise control of expression levels using IPTG.

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About This Item

Code UNSPSC :
41106202

Source biologique

Escherichia coli

Niveau de qualité

Fabricant/nom de marque

Novagen®

Conditions de stockage

OK to freeze

Mode de croissance

adherent or suspension

Morphologie

rod shaped

Technique(s)

microbiological culture: suitable

Transformation cellulaire

transformation efficiency: >2×106 cfu/μg

Conditions d'expédition

dry ice

Température de stockage

−70°C

Description générale

Genotype: F-ompT hsdSB(rB- mB-) gal dcm lacY1 ahpC (DE3) gor522::Tn10 trxB (KanR, TetR)





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.
Origami B host strains carry the same mutationsin trxB and gor as the original Origami strains,except that they are derived from a lacZY mutantof BL21 to enable precise control of expressionlevels by adjusting the concentration of IPTG.Thus the Origami B strains combine the desirablecharacteristics of BL21, Tuner, and Origamistrains in one strain background. The mutationsin trxB and gor are selectable on kanamycin andtetracycline, respectively; therefore, these strainscannot be used with plasmids that can onlyselected with kanamycin or tetracycline. Thesestrains also include the lon and ompT deficiencesof BL21, which increase protein stability.

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.
Origami B host strains carry the same mutations as the original Origami strain, except that they are derived from a lacZY mutant of BL21 to enable precise control of expression levels using IPTG.

Composants

0.4 ml1 mlComponent

•2 × 0.2 ml5 × 0.2 mlOrigami B(DE3) Competent Cells

•2 × 2 ml4 × 2 mlSOC Medium

•2 ng2 ngTest Plasmid

Avertissement

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

Informations légales

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

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 2


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Marriah N Green et al.
Molecular cell, 81(15), 3216-3226 (2021-06-24)
Glutamate receptor-like channels (GLRs) play vital roles in various physiological processes in plants, such as wound response, stomatal aperture control, seed germination, root development, innate immune response, pollen tube growth, and morphogenesis. Despite the importance of GLRs, knowledge about their
Shanti Pal Gangwar et al.
Structure (London, England : 1993), 29(2), 161-169 (2020-10-08)
Glutamate receptor-like channels (GLRs) play important roles in numerous plant physiological processes. GLRs are homologous to ionotropic glutamate receptors (iGluRs) that mediate neurotransmission in vertebrates. Here we determine crystal structures of Arabidopsis thaliana GLR3.2 ligand-binding domain (LBD) in complex with
Miaomiao Li et al.
eLife, 11 (2022-02-10)
RAGE, a druggable inflammatory receptor, is known to function as an oligomer but the exact oligomerization mechanism remains poorly understood. Previously we have shown that heparan sulfate (HS) plays an active role in RAGE oligomerization. To understand the physiological significance
Niko Amin-Wetzel et al.
eLife, 8 (2019-12-25)
Coupling of endoplasmic reticulum (ER) stress to dimerisation-dependent activation of the UPR transducer IRE1 is incompletely understood. Whilst the luminal co-chaperone ERdj4 promotes a complex between the Hsp70 BiP and IRE1's stress-sensing luminal domain (IRE1LD) that favours the latter's monomeric
Niko Amin-Wetzel et al.
Cell, 171(7), 1625-1637 (2017-12-05)
When unfolded proteins accumulate in the endoplasmic reticulum (ER), the unfolded protein response (UPR) increases ER-protein-folding capacity to restore protein-folding homeostasis. Unfolded proteins activate UPR signaling across the ER membrane to the nucleus by promoting oligomerization of IRE1, a conserved transmembrane

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