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  • 99
    New England Biolabs e coli bl 21 de 3 cell culture
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    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.
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    Image Search Results


    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