nickel nitrilotriacetic agarose ni nta resin wash buffer  (Millipore)

 
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    Millipore nickel nitrilotriacetic agarose ni nta resin wash buffer
    Nickel Nitrilotriacetic Agarose Ni Nta Resin Wash Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    nickel nitrilotriacetic agarose ni nta resin wash buffer  (Millipore)

     
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    Millipore nickel nitrilotriacetic agarose ni nta resin wash buffer
    (A) <t>Ni-NTA</t> purification. The 10,000g supernatant was mixed with Ni-NTA affinity beads. The beads were washed five times. Proteins bound to the beads were eluted by imidazole solution containing 50, 100, 150, 200, 250, 1000 mM (Elutions 1–6). Proteins were separated by 4–20% SDSPAGE and stained with Coomassie brilliant blue (A, top) or transferred onto nitrocellulose membranes for immunoblotting with anti-MBP-hTTP antibodies (A, bottom). The full-length rDGAT2, MBP, and the potential dimer of the full-length rDGAT2 are marked with arrows. H, homogenate, S2, 2,000g supernatant, S10, 10,000g supernatant, U, unbound fraction, B, Ni-NTA beads after 6 imidazole elutions. (B) The fractions purified by Ni-NTA affinity beads as shown in A were mixed with amylose resin affinity beads. The beads were washed five times. Proteins bound to the beads were eluted by amylase resin elution buffer containing 20 mM maltose (lanes 1–5) and three times with 0.5 M NaOH (lanes 6–8). Proteins were separated by 4–20% SDS-PAGE and stained with silver reagent (B, top) or transferred onto a nitrocellulose membrane for immunoblotting with anti-MBP-hTTP antibodies (B, bottom). The full length rDGAT2 and the potential dimer of the full-length rDGAT2 are marked with arrows. E4, proteins eluted with 200 mM imidazole solution from Ni-NTA beads (Figure 5).
    Nickel Nitrilotriacetic Agarose Ni Nta Resin Wash Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Expression and purification of recombinant tung tree diacylglycerol acyltransferase 2"

    Article Title: Expression and purification of recombinant tung tree diacylglycerol acyltransferase 2

    Journal: Applied microbiology and biotechnology

    doi: 10.1007/s00253-012-3869-7

    (A) Ni-NTA purification. The 10,000g supernatant was mixed with Ni-NTA affinity beads. The beads were washed five times. Proteins bound to the beads were eluted by imidazole solution containing 50, 100, 150, 200, 250, 1000 mM (Elutions 1–6). Proteins were separated by 4–20% SDSPAGE and stained with Coomassie brilliant blue (A, top) or transferred onto nitrocellulose membranes for immunoblotting with anti-MBP-hTTP antibodies (A, bottom). The full-length rDGAT2, MBP, and the potential dimer of the full-length rDGAT2 are marked with arrows. H, homogenate, S2, 2,000g supernatant, S10, 10,000g supernatant, U, unbound fraction, B, Ni-NTA beads after 6 imidazole elutions. (B) The fractions purified by Ni-NTA affinity beads as shown in A were mixed with amylose resin affinity beads. The beads were washed five times. Proteins bound to the beads were eluted by amylase resin elution buffer containing 20 mM maltose (lanes 1–5) and three times with 0.5 M NaOH (lanes 6–8). Proteins were separated by 4–20% SDS-PAGE and stained with silver reagent (B, top) or transferred onto a nitrocellulose membrane for immunoblotting with anti-MBP-hTTP antibodies (B, bottom). The full length rDGAT2 and the potential dimer of the full-length rDGAT2 are marked with arrows. E4, proteins eluted with 200 mM imidazole solution from Ni-NTA beads (Figure 5).
    Figure Legend Snippet: (A) Ni-NTA purification. The 10,000g supernatant was mixed with Ni-NTA affinity beads. The beads were washed five times. Proteins bound to the beads were eluted by imidazole solution containing 50, 100, 150, 200, 250, 1000 mM (Elutions 1–6). Proteins were separated by 4–20% SDSPAGE and stained with Coomassie brilliant blue (A, top) or transferred onto nitrocellulose membranes for immunoblotting with anti-MBP-hTTP antibodies (A, bottom). The full-length rDGAT2, MBP, and the potential dimer of the full-length rDGAT2 are marked with arrows. H, homogenate, S2, 2,000g supernatant, S10, 10,000g supernatant, U, unbound fraction, B, Ni-NTA beads after 6 imidazole elutions. (B) The fractions purified by Ni-NTA affinity beads as shown in A were mixed with amylose resin affinity beads. The beads were washed five times. Proteins bound to the beads were eluted by amylase resin elution buffer containing 20 mM maltose (lanes 1–5) and three times with 0.5 M NaOH (lanes 6–8). Proteins were separated by 4–20% SDS-PAGE and stained with silver reagent (B, top) or transferred onto a nitrocellulose membrane for immunoblotting with anti-MBP-hTTP antibodies (B, bottom). The full length rDGAT2 and the potential dimer of the full-length rDGAT2 are marked with arrows. E4, proteins eluted with 200 mM imidazole solution from Ni-NTA beads (Figure 5).

    Techniques Used: Purification, Staining, Western Blot, SDS Page, Membrane

    (A) The chromatogram for the protein size standards. The protein standards were vitamin B12, horse myoglobin, chicken ovalbumin, bovine γ-globulin, and bovine thyroglobulin. (B). Part of the chromatogram for rDGAT2. Recombinant DGAT2 fraction purified from Ni-NTA affinity beads was centrifuged at 10,000g before being loaded onto a Superose 12 HR 10/30 column and eluted with identical procedure for the size standards. (C). Immunoblotting detection of rDGAT2 using anti-MBP-hTTP serum (4–20% SDS-PAGE). The full-length rDGAT2 and the potential dimer of the protein are marked with arrows.
    Figure Legend Snippet: (A) The chromatogram for the protein size standards. The protein standards were vitamin B12, horse myoglobin, chicken ovalbumin, bovine γ-globulin, and bovine thyroglobulin. (B). Part of the chromatogram for rDGAT2. Recombinant DGAT2 fraction purified from Ni-NTA affinity beads was centrifuged at 10,000g before being loaded onto a Superose 12 HR 10/30 column and eluted with identical procedure for the size standards. (C). Immunoblotting detection of rDGAT2 using anti-MBP-hTTP serum (4–20% SDS-PAGE). The full-length rDGAT2 and the potential dimer of the protein are marked with arrows.

    Techniques Used: Recombinant, Purification, Western Blot, SDS Page

    The insoluble fraction from 30,000g pellet of E. coli was solubilizd with 0.5% detergents at 4°C for 1 h followed by centrifugation at 50,000g for 30 min. The 50,000g supernatant was used for affinity purification with Ni-NTA beads. Various fractions were used for immunoblotting analysis with anti-MBP-hTTP antiserum. A, 50,000g supernatant, B, 200 mM imidazole elution, C, washes, D, unbound fractions. Lane 1, Brij 35, lane 2, CHAPS, lane 3, NP-40, lane 4, SDS, lane 5, Triton X-100, lane 6, Tween 20 and lane 7, Tween 80. Each lane was loaded with 20 μL of each fraction.
    Figure Legend Snippet: The insoluble fraction from 30,000g pellet of E. coli was solubilizd with 0.5% detergents at 4°C for 1 h followed by centrifugation at 50,000g for 30 min. The 50,000g supernatant was used for affinity purification with Ni-NTA beads. Various fractions were used for immunoblotting analysis with anti-MBP-hTTP antiserum. A, 50,000g supernatant, B, 200 mM imidazole elution, C, washes, D, unbound fractions. Lane 1, Brij 35, lane 2, CHAPS, lane 3, NP-40, lane 4, SDS, lane 5, Triton X-100, lane 6, Tween 20 and lane 7, Tween 80. Each lane was loaded with 20 μL of each fraction.

    Techniques Used: Centrifugation, Affinity Purification, Western Blot

    The insoluble fraction from 30,000g pellet of E. coli was solubilizd with various concentrations of SDS at different temperatures for 1 h followed by centrifugation at 50,000g for 30 min. The 50,000g supernatant was used for affinity purification with Ni-NTA beads. Various fractions were used for SDS-PAGE followed by staining with silver reagent and immunoblotting analysis with anti-MBP-hTTP antiserum. A, 4°C, B, 25°C, C, 37°C, D, 80°C, E, 37°C, F, 80°C. Lane 1, 0% SDS, lane 2, 0.1% SDS, lane 3, 0.3% SDS, lane 4, 0.5% SDS, lane 5, 1% SDS. Each lane was loaded with 10 μL of each fraction.
    Figure Legend Snippet: The insoluble fraction from 30,000g pellet of E. coli was solubilizd with various concentrations of SDS at different temperatures for 1 h followed by centrifugation at 50,000g for 30 min. The 50,000g supernatant was used for affinity purification with Ni-NTA beads. Various fractions were used for SDS-PAGE followed by staining with silver reagent and immunoblotting analysis with anti-MBP-hTTP antiserum. A, 4°C, B, 25°C, C, 37°C, D, 80°C, E, 37°C, F, 80°C. Lane 1, 0% SDS, lane 2, 0.1% SDS, lane 3, 0.3% SDS, lane 4, 0.5% SDS, lane 5, 1% SDS. Each lane was loaded with 10 μL of each fraction.

    Techniques Used: Centrifugation, Affinity Purification, SDS Page, Staining, Western Blot

    The proteins purified by Ni-NTA affinity chromatography following SDS extraction were separated by SDSPAGE and stained with Coomassie brilliant blue. The protein bands corresponding to the sizes of the monomer and dimer of rDGAT2 were excised and digested with trypsin. The in-gel digested peptides were analyzed by LC-ESI-MS. (A) The protein bands corresponding to monomer and dimer sizes on SDS-PAGE were used for MS analysis, (B) Immunoblotting identification of both protein bands cross30 reacted with anti-MBP-hTTP antibodies, (C) Sequence of rDGAT2 with amino acids observed by LC/MS/MS in the lower molecular weight band highlighted in red, (D) MS/MS data of the triply charged ion of m/z 754.4 corresponding in mass to amino acid residues 89–107 of rDGAT2.
    Figure Legend Snippet: The proteins purified by Ni-NTA affinity chromatography following SDS extraction were separated by SDSPAGE and stained with Coomassie brilliant blue. The protein bands corresponding to the sizes of the monomer and dimer of rDGAT2 were excised and digested with trypsin. The in-gel digested peptides were analyzed by LC-ESI-MS. (A) The protein bands corresponding to monomer and dimer sizes on SDS-PAGE were used for MS analysis, (B) Immunoblotting identification of both protein bands cross30 reacted with anti-MBP-hTTP antibodies, (C) Sequence of rDGAT2 with amino acids observed by LC/MS/MS in the lower molecular weight band highlighted in red, (D) MS/MS data of the triply charged ion of m/z 754.4 corresponding in mass to amino acid residues 89–107 of rDGAT2.

    Techniques Used: Purification, Affinity Chromatography, Extraction, Staining, SDS Page, Western Blot, Sequencing, Liquid Chromatography with Mass Spectroscopy, Molecular Weight, Tandem Mass Spectroscopy

    nickel nta agarose resin  (Qiagen)


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    Qiagen nickel nta agarose resin
    Nickel Nta Agarose Resin, supplied by Qiagen, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    nickel nta agarose resin  (Qiagen)


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    Qiagen nickel nta agarose resin
    Nickel Nta Agarose Resin, supplied by Qiagen, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    nickel nitrilotriacetic acid agarose ni nta resin  (Qiagen)


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    Qiagen nickel nitrilotriacetic acid agarose ni nta resin
    Nickel Nitrilotriacetic Acid Agarose Ni Nta Resin, supplied by Qiagen, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    nickel nitrilotriacetic acid ni nta agarose resin  (Beyotime)

     
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    Beyotime nickel nitrilotriacetic acid ni nta agarose resin
    Nickel Nitrilotriacetic Acid Ni Nta Agarose Resin, supplied by Beyotime, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    nickel nitrilotriacetic acid agarose ni nta resin  (Qiagen)


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    Qiagen nickel nitrilotriacetic acid agarose ni nta resin
    Nickel Nitrilotriacetic Acid Agarose Ni Nta Resin, supplied by Qiagen, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    nickel nitrilotriacetic acid agarose ni nta resin  (Qiagen)


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    Qiagen nickel nitrilotriacetic acid agarose ni nta resin
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    nickel nta agarose resin  (Qiagen)


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    packed nickel nta agarose resin bed  (Gold Biotechnology Inc)


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    Gold Biotechnology Inc packed nickel nta agarose resin bed
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    Millipore nickel nitrilotriacetic agarose ni nta resin wash buffer
    Nickel Nitrilotriacetic Agarose Ni Nta Resin Wash Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    nickel nta agarose resin  (Qiagen)
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    Qiagen nickel nta agarose resin
    Nickel Nta Agarose Resin, supplied by Qiagen, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    nickel nitrilotriacetic acid agarose ni nta resin  (Qiagen)
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    Qiagen nickel nitrilotriacetic acid agarose ni nta resin
    Nickel Nitrilotriacetic Acid Agarose Ni Nta Resin, supplied by Qiagen, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    nickel nitrilotriacetic acid ni nta agarose resin  (Beyotime)
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    Beyotime nickel nitrilotriacetic acid ni nta agarose resin
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