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  • 99
    New England Biolabs e coli bl21de3 competent cells
    E Coli Bl21de3 Competent Cells, supplied by New England Biolabs, used in various techniques. Bioz Stars score: 99/100, based on 86 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    e coli bl21de3 competent cells - by Bioz Stars, 2020-03
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    99
    Millipore bl 21 de3 cells
    mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami <t>DE3</t> and <t>BL21</t> DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.
    Bl 21 De3 Cells, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 50 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Stratagene bl 21 de3
    mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami <t>DE3</t> and <t>BL21</t> DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.
    Bl 21 De3, supplied by Stratagene, used in various techniques. Bioz Stars score: 78/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bl 21 de3 - by Bioz Stars, 2020-03
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    84
    Agilent technologies bl 21 de3
    mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami <t>DE3</t> and <t>BL21</t> DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.
    Bl 21 De3, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 84/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    78
    Stratagene bl 21 de3 plyss
    mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami <t>DE3</t> and <t>BL21</t> DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.
    Bl 21 De3 Plyss, supplied by Stratagene, used in various techniques. Bioz Stars score: 78/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Thermo Fisher bl 21 de3 star
    mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami <t>DE3</t> and <t>BL21</t> DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.
    Bl 21 De3 Star, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 80/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bl 21 de3 star - by Bioz Stars, 2020-03
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    78
    Promega bl 21 de3 cells
    mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami <t>DE3</t> and <t>BL21</t> DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.
    Bl 21 De3 Cells, supplied by Promega, used in various techniques. Bioz Stars score: 78/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Agilent technologies competent bl 21 de3 ril
    mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami <t>DE3</t> and <t>BL21</t> DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.
    Competent Bl 21 De3 Ril, supplied by Agilent technologies, used in various techniques. Bioz Stars score: 80/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    80
    Stratagene escherchia coli bl 21 de3
    mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami <t>DE3</t> and <t>BL21</t> DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.
    Escherchia Coli Bl 21 De3, supplied by Stratagene, used in various techniques. Bioz Stars score: 80/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Promega bl 21 de3 plyss
    mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami <t>DE3</t> and <t>BL21</t> DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.
    Bl 21 De3 Plyss, supplied by Promega, used in various techniques. Bioz Stars score: 99/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bl 21 de3 plyss - by Bioz Stars, 2020-03
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    79
    Stratagene bl 21 de3 cells
    mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami <t>DE3</t> and <t>BL21</t> DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.
    Bl 21 De3 Cells, supplied by Stratagene, used in various techniques. Bioz Stars score: 79/100, based on 17 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    88
    TaKaRa e coli bl 21 de 3 ril
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
    E Coli Bl 21 De 3 Ril, supplied by TaKaRa, used in various techniques. Bioz Stars score: 88/100, based on 21 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    77
    Stratagene bl 21 de3 competent cells
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
    Bl 21 De3 Competent Cells, supplied by Stratagene, used in various techniques. Bioz Stars score: 77/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bl 21 de3 competent cells - by Bioz Stars, 2020-03
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    80
    Promega escherichia coli bl 21 de3
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
    Escherichia Coli Bl 21 De3, supplied by Promega, used in various techniques. Bioz Stars score: 80/100, based on 9 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    escherichia coli bl 21 de3 - by Bioz Stars, 2020-03
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    79
    Stratagene bl 21 de3 codon ril
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
    Bl 21 De3 Codon Ril, supplied by Stratagene, used in various techniques. Bioz Stars score: 79/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    bl 21 de3 codon ril - by Bioz Stars, 2020-03
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    87
    Agilent technologies bl 21 de3 ripl cells
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
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    79
    Bio-Rad bl 21 de3 e coli
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
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    76
    Stratagene bl 21 de3 plyss bacteria
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
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    80
    Thermo Fisher bl 21 de3 plys
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
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    79
    Millipore bl 21 de3 star e coli
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
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    79
    Thermo Fisher enzyme purification bl 21 de3 cells
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
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    87
    Agilent technologies bl 21 de3 ril codon plus
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
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    86
    Agilent technologies bl 21 de3 competent e coli
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
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    85
    Stratagene coli bl 21 de3 gold
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
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    79
    Stratagene bl 21 de3 codonplus rp
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
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    89
    Sangon Biotech bl21 de3
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
    Bl21 De3, supplied by Sangon Biotech, used in various techniques. Bioz Stars score: 89/100, based on 6 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Thermo Fisher bl21 de3
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
    Bl21 De3, supplied by Thermo Fisher, used in various techniques. Bioz Stars score: 99/100, based on 761 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    94
    GE Healthcare bl21 de3
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
    Bl21 De3, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 94/100, based on 120 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Pasteur Institute bl21 de3
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
    Bl21 De3, supplied by Pasteur Institute, used in various techniques. Bioz Stars score: 91/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Merck & Co bl21 de3
    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - <t>BL</t> 21 (DE 3 <t>)-RIL</t> , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.
    Bl21 De3, supplied by Merck & Co, used in various techniques. Bioz Stars score: 93/100, based on 33 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami DE3 and BL21 DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.

    Journal: PLoS ONE

    Article Title: The Quiescin Sulfhydryl Oxidase (hQSOX1b) Tunes the Expression of Resistin-Like Molecule Alpha (RELM-? or mFIZZ1) in a Wheat Germ Cell-Free Extract

    doi: 10.1371/journal.pone.0055621

    Figure Lengend Snippet: mFIZZ1 soluble expressed using wheat germ extract. ( A ) The expression of mFIZZ1 in SHuffle™ T7, Origami DE3 and BL21 DE3 analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( B ) Strip of the immunoblot from the SDS-PAGE in ( A ) developed with anti-His antibody is shown. ( C ) The expression of mFIZZ1′ with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( D ) Strip of the respective immunoblot of ( C ) developed with anti-His antibody is shown. ( E ) The expression of mFIZZ1 with wheat germ extract analysed on non-reducing 15% SDS-PAGE stained with Coomassie Brilliant Blue. ( F ) Strip of the respective immunoblot of ( E ) developed with anti-His antibody is shown. As marker (M) the PageRuler™ pre-stained Protein Ladder (Fermentas) is used. P = pellet, S = soluble fraction and T = total. The corresponding bands are indicated with an asterisk.

    Article Snippet: Plasmid DNA of mFIZZ1 was transformed into E. coli SHuffle™ T7 Express (BioLabs), Origami™ DE3 and BL21 DE3 (Novagen), grown in LB medium supplemented with 25 µg/ml ampicillin, induced at a cell density (OD600 nm ) of 0.7 with 1 mM isopropyl-b-D-thiogalactopyranoside (IPTG), and cultured for 6 h at 37°C except for SHuffle™ T7 cells, the expression done at 30°C.

    Techniques: Expressing, SDS Page, Staining, Stripping Membranes, Marker

    The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.

    Journal: Virology Journal

    Article Title: The development and application of new crystallization method for tobacco mosaic virus coat protein

    doi: 10.1186/1743-422X-9-279

    Figure Lengend Snippet: The generation of expression and purification of target protein that was analyzed using 12% SDS-PAGE. ( A ) Protein molecular weight standards are shown in lane 1. Numbers on the left are the MW of the standards in kDa. Lanes 1, 2, and 3 show the controls without induction by IPTG that were 20 μL aliquots of whole cell lysates from 10 mL PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL , pET28a-His-TMV-CP 12 - BL 21 (DE 3 )-RIL , and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures, respectively. Lanes 4, 5, and 6 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L PGEX-6P-1-WT-GST-TMV-CP 32 - BL 21 (DE 3 )-RIL cultures with IPTG. A new protein band at 43.5 kDa corresponds to the target protein GST-TMV-CP. Lanes 7 and 8 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 12 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 68 - BL 21 (DE 3 )-RIL culture with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. Lanes 9 and 10 correspond to the cultures after expression that were from 20 μL aliquots of whole cell lysates from 1 L pET28a-TR-His-TMV-CP 62 - BL 21 (DE 3 )-RIL and pET28a-TR-His-TMV-CP 19 - BL 21 (DE 3 )-RIL cultures with IPTG, respectively. A new protein band at position 18.5 kDa corresponds to the target protein. ( B ) WT-GST-TMV-CP 32 protein is shown in lanes 1 and 2 purified using nickel-nitrilotriacetic acid (Ni-NTA) column. ( C ) WT-His-TMV-CP 12 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( D ) TR-His-TMV-CP 19 protein is shown in Lanes 1 and 2 purified using Ni-NTA column. ( E ) WT-TMV-CP 32 protein cleaved GST-tags is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( F ) WT-His-MV-CP 12 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column. ( G ) TR-His-MV-CP 19 protein is shown in 12% SDS-PAGE gel filtration purified using HiLoad 16/60 Superdex 200 pg column.

    Article Snippet: These correct proteins were successfully cloned to the expression host, E.coli BL 21 (DE 3 )-RIL (TakaRa), for protein expression.

    Techniques: Expressing, Purification, SDS Page, Molecular Weight, Filtration