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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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biological source

Escherichia coli

Quality Level



storage condition

OK to freeze

growth mode

adherent or suspension


rod shaped


microbiological culture: suitable

cell transformation

transformation efficiency: >2×106 cfu/μg

shipped in

dry ice

storage temp.


General description

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.


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


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

Legal Information

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

Storage Class

10 - Combustible liquids



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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
Shaheen A Farhadi et al.
Frontiers in chemistry, 7, 898-898 (2020-01-31)
Galectin-1 (G1) and galectin-3 (G3) are carbohydrate-binding proteins that can signal apoptosis in T cells. We recently reported that a synthetic tetramer with two G1 and two G3 domains ("G1/G3 Zipper") induces Jurkat T cell death more potently than G1.
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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