e coli strains Search Results


ldehyde re duction  (Addgene inc)
93
Addgene inc ldehyde re duction
Ldehyde Re Duction, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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escherichia coli s17 1 λpir  (Addgene inc)
90
Addgene inc escherichia coli s17 1 λpir
Escherichia Coli S17 1 λpir, supplied by Addgene inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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chromosomal terminus  (Addgene inc)
91
Addgene inc chromosomal terminus
Chromosomal Terminus, supplied by Addgene inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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d escherichia coli  (Bio-Rad)
93
Bio-Rad d escherichia coli
Fig. 6: E. coli colonies on the different samples after 16h. N=3. *p<0.005 versus control, **p<0.01 versus control.
D Escherichia Coli, supplied by Bio-Rad, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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e coli dh10b  (Addgene inc)
92
Addgene inc e coli dh10b
Incorporation of nitroTyr into CaM expressed in <t>E.</t> <t>coli.</t> A, the human CaM construct with C-terminal His6 tag bearing either the native Tyr codon or an amber stop codon at amino acid position 99 or position 138 was co-transformed with a plasmid expressing an Methanocaldococcus jannaschii tyrosyl-tRNA synthetase/tRNACUA pair engineered to efficiently incorporate nitroTyr. B, WT– and nitroTyr–CaM was expressed in autoinduction medium with or without nitroTyr supplementation, purified using the C-terminal His6 tag, and analyzed by 15% SDS-PAGE gel. C, nitroTyr incorporation into CaM was determined here by Western blotting with a primary antibody against nitroTyr. D, electrospray ionization mass spectrometry confirms the quantitative incorporation of nitroTyr into CaM because all measured pure protein masses match their expected molecular masses.
E Coli Dh10b, supplied by Addgene inc, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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midreplichore  (Addgene inc)
91
Addgene inc midreplichore
Incorporation of nitroTyr into CaM expressed in <t>E.</t> <t>coli.</t> A, the human CaM construct with C-terminal His6 tag bearing either the native Tyr codon or an amber stop codon at amino acid position 99 or position 138 was co-transformed with a plasmid expressing an Methanocaldococcus jannaschii tyrosyl-tRNA synthetase/tRNACUA pair engineered to efficiently incorporate nitroTyr. B, WT– and nitroTyr–CaM was expressed in autoinduction medium with or without nitroTyr supplementation, purified using the C-terminal His6 tag, and analyzed by 15% SDS-PAGE gel. C, nitroTyr incorporation into CaM was determined here by Western blotting with a primary antibody against nitroTyr. D, electrospray ionization mass spectrometry confirms the quantitative incorporation of nitroTyr into CaM because all measured pure protein masses match their expected molecular masses.
Midreplichore, supplied by Addgene inc, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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e. coli strain jm109  (Amersham Life Sciences Inc)
90
Amersham Life Sciences Inc e. coli strain jm109
Incorporation of nitroTyr into CaM expressed in <t>E.</t> <t>coli.</t> A, the human CaM construct with C-terminal His6 tag bearing either the native Tyr codon or an amber stop codon at amino acid position 99 or position 138 was co-transformed with a plasmid expressing an Methanocaldococcus jannaschii tyrosyl-tRNA synthetase/tRNACUA pair engineered to efficiently incorporate nitroTyr. B, WT– and nitroTyr–CaM was expressed in autoinduction medium with or without nitroTyr supplementation, purified using the C-terminal His6 tag, and analyzed by 15% SDS-PAGE gel. C, nitroTyr incorporation into CaM was determined here by Western blotting with a primary antibody against nitroTyr. D, electrospray ionization mass spectrometry confirms the quantitative incorporation of nitroTyr into CaM because all measured pure protein masses match their expected molecular masses.
E. Coli Strain Jm109, supplied by Amersham Life Sciences Inc, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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recombinant bucky ball expressed in e. coli strain bl21 (de3)  (GERBU Biotechnik GmbH)
90
GERBU Biotechnik GmbH recombinant bucky ball expressed in e. coli strain bl21 (de3)
Incorporation of nitroTyr into CaM expressed in <t>E.</t> <t>coli.</t> A, the human CaM construct with C-terminal His6 tag bearing either the native Tyr codon or an amber stop codon at amino acid position 99 or position 138 was co-transformed with a plasmid expressing an Methanocaldococcus jannaschii tyrosyl-tRNA synthetase/tRNACUA pair engineered to efficiently incorporate nitroTyr. B, WT– and nitroTyr–CaM was expressed in autoinduction medium with or without nitroTyr supplementation, purified using the C-terminal His6 tag, and analyzed by 15% SDS-PAGE gel. C, nitroTyr incorporation into CaM was determined here by Western blotting with a primary antibody against nitroTyr. D, electrospray ionization mass spectrometry confirms the quantitative incorporation of nitroTyr into CaM because all measured pure protein masses match their expected molecular masses.
Recombinant Bucky Ball Expressed In E. Coli Strain Bl21 (De3), supplied by GERBU Biotechnik GmbH, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ccd operons e. coli strain o157:h7  (GenScript corporation)
90
GenScript corporation ccd operons e. coli strain o157:h7
Incorporation of nitroTyr into CaM expressed in <t>E.</t> <t>coli.</t> A, the human CaM construct with C-terminal His6 tag bearing either the native Tyr codon or an amber stop codon at amino acid position 99 or position 138 was co-transformed with a plasmid expressing an Methanocaldococcus jannaschii tyrosyl-tRNA synthetase/tRNACUA pair engineered to efficiently incorporate nitroTyr. B, WT– and nitroTyr–CaM was expressed in autoinduction medium with or without nitroTyr supplementation, purified using the C-terminal His6 tag, and analyzed by 15% SDS-PAGE gel. C, nitroTyr incorporation into CaM was determined here by Western blotting with a primary antibody against nitroTyr. D, electrospray ionization mass spectrometry confirms the quantitative incorporation of nitroTyr into CaM because all measured pure protein masses match their expected molecular masses.
Ccd Operons E. Coli Strain O157:H7, supplied by GenScript corporation, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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e. coli o157:h7 strains  (Bilthoven Biologicals)
90
Bilthoven Biologicals e. coli o157:h7 strains
Incorporation of nitroTyr into CaM expressed in <t>E.</t> <t>coli.</t> A, the human CaM construct with C-terminal His6 tag bearing either the native Tyr codon or an amber stop codon at amino acid position 99 or position 138 was co-transformed with a plasmid expressing an Methanocaldococcus jannaschii tyrosyl-tRNA synthetase/tRNACUA pair engineered to efficiently incorporate nitroTyr. B, WT– and nitroTyr–CaM was expressed in autoinduction medium with or without nitroTyr supplementation, purified using the C-terminal His6 tag, and analyzed by 15% SDS-PAGE gel. C, nitroTyr incorporation into CaM was determined here by Western blotting with a primary antibody against nitroTyr. D, electrospray ionization mass spectrometry confirms the quantitative incorporation of nitroTyr into CaM because all measured pure protein masses match their expected molecular masses.
E. Coli O157:H7 Strains, supplied by Bilthoven Biologicals, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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rnase iii-deficient escherichia coli bacteria strain ht115 (de3)  (Geneservice ltd)
90
Geneservice ltd rnase iii-deficient escherichia coli bacteria strain ht115 (de3)
Incorporation of nitroTyr into CaM expressed in <t>E.</t> <t>coli.</t> A, the human CaM construct with C-terminal His6 tag bearing either the native Tyr codon or an amber stop codon at amino acid position 99 or position 138 was co-transformed with a plasmid expressing an Methanocaldococcus jannaschii tyrosyl-tRNA synthetase/tRNACUA pair engineered to efficiently incorporate nitroTyr. B, WT– and nitroTyr–CaM was expressed in autoinduction medium with or without nitroTyr supplementation, purified using the C-terminal His6 tag, and analyzed by 15% SDS-PAGE gel. C, nitroTyr incorporation into CaM was determined here by Western blotting with a primary antibody against nitroTyr. D, electrospray ionization mass spectrometry confirms the quantitative incorporation of nitroTyr into CaM because all measured pure protein masses match their expected molecular masses.
Rnase Iii Deficient Escherichia Coli Bacteria Strain Ht115 (De3), supplied by Geneservice ltd, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Fig. 6: E. coli colonies on the different samples after 16h. N=3. *p<0.005 versus control, **p<0.01 versus control.

Journal: Nanomedicine : nanotechnology, biology, and medicine

Article Title: Synergic antibacterial coatings combining titanium nanocolumns and tellurium nanorods.

doi: 10.1016/j.nano.2018.12.009

Figure Lengend Snippet: Fig. 6: E. coli colonies on the different samples after 16h. N=3. *p<0.005 versus control, **p<0.01 versus control.

Article Snippet: For the sake of comparison, the sputtered Ti thin films as well as commercial Ti disks from Goodfellow (thickness: 0.5 mm, code: 303-115-36) were also used: no significant differences between them were observed, so their results were averaged and jointly labeled D. Escherichia coli (strain K-12 HB101; Bio-Rad, Hercules, CA) and Staphylococcus aureus (subsp. aureus Rosenbach, ATCC® 12600TM; ATCC, Manassas, VA) bacteria were used.

Techniques: Control

Incorporation of nitroTyr into CaM expressed in E. coli. A, the human CaM construct with C-terminal His6 tag bearing either the native Tyr codon or an amber stop codon at amino acid position 99 or position 138 was co-transformed with a plasmid expressing an Methanocaldococcus jannaschii tyrosyl-tRNA synthetase/tRNACUA pair engineered to efficiently incorporate nitroTyr. B, WT– and nitroTyr–CaM was expressed in autoinduction medium with or without nitroTyr supplementation, purified using the C-terminal His6 tag, and analyzed by 15% SDS-PAGE gel. C, nitroTyr incorporation into CaM was determined here by Western blotting with a primary antibody against nitroTyr. D, electrospray ionization mass spectrometry confirms the quantitative incorporation of nitroTyr into CaM because all measured pure protein masses match their expected molecular masses.

Journal: The Journal of Biological Chemistry

Article Title: Tyrosine nitration on calmodulin enhances calcium-dependent association and activation of nitric-oxide synthase

doi: 10.1074/jbc.RA119.010999

Figure Lengend Snippet: Incorporation of nitroTyr into CaM expressed in E. coli. A, the human CaM construct with C-terminal His6 tag bearing either the native Tyr codon or an amber stop codon at amino acid position 99 or position 138 was co-transformed with a plasmid expressing an Methanocaldococcus jannaschii tyrosyl-tRNA synthetase/tRNACUA pair engineered to efficiently incorporate nitroTyr. B, WT– and nitroTyr–CaM was expressed in autoinduction medium with or without nitroTyr supplementation, purified using the C-terminal His6 tag, and analyzed by 15% SDS-PAGE gel. C, nitroTyr incorporation into CaM was determined here by Western blotting with a primary antibody against nitroTyr. D, electrospray ionization mass spectrometry confirms the quantitative incorporation of nitroTyr into CaM because all measured pure protein masses match their expected molecular masses.

Article Snippet: E. coli DH10B was transformed with pBad–CaM–(99 or 138 TAG) and pDule–nitroTyr–5B (Addgene plasmid no. 85498) ( 30 ).

Techniques: Construct, Transformation Assay, Plasmid Preparation, Expressing, Purification, SDS Page, Western Blot, Mass Spectrometry