histrap ff crude column  (GE Healthcare)

 
  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 97
    Name:
    HisTrap FF
    Description:

    Catalog Number:
    17525501
    Price:
    None
    Category:
    HisTrap FF
    Buy from Supplier


    Structured Review

    GE Healthcare histrap ff crude column
    Purified trKMO. (A) Chromatogram produced during NiNTA affinity purification of truncate KMO. (B) SDS-PAGE protein gel stained with simplyblue showing <t>HisTrap</t> purification of truncated human KMO protein, (a) Cell-free extract prior to affinity chromatography, (b) flowthrough proteins which did not bind to the column, (c) first column wash, (d) second column wash, (e) third column wash, (f) pure truncated human KMO protein (44 kDa) from the fractions under the chromatogram. (C) Cartoon illustrating the trKMO construct. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    https://www.bioz.com/result/histrap ff crude column/product/GE Healthcare
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    histrap ff crude column - by Bioz Stars, 2021-04
    97/100 stars

    Images

    1) Product Images from "Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification"

    Article Title: Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification

    Journal: Protein Expression and Purification

    doi: 10.1016/j.pep.2013.11.015

    Purified trKMO. (A) Chromatogram produced during NiNTA affinity purification of truncate KMO. (B) SDS-PAGE protein gel stained with simplyblue showing HisTrap purification of truncated human KMO protein, (a) Cell-free extract prior to affinity chromatography, (b) flowthrough proteins which did not bind to the column, (c) first column wash, (d) second column wash, (e) third column wash, (f) pure truncated human KMO protein (44 kDa) from the fractions under the chromatogram. (C) Cartoon illustrating the trKMO construct. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)
    Figure Legend Snippet: Purified trKMO. (A) Chromatogram produced during NiNTA affinity purification of truncate KMO. (B) SDS-PAGE protein gel stained with simplyblue showing HisTrap purification of truncated human KMO protein, (a) Cell-free extract prior to affinity chromatography, (b) flowthrough proteins which did not bind to the column, (c) first column wash, (d) second column wash, (e) third column wash, (f) pure truncated human KMO protein (44 kDa) from the fractions under the chromatogram. (C) Cartoon illustrating the trKMO construct. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Techniques Used: Purification, Produced, Affinity Purification, SDS Page, Staining, Affinity Chromatography, Construct

    Related Articles

    Purification:

    Article Title: Large-scale seroprevalence analysis of human metapneumovirus and human respiratory syncytial virus infections in Beijing, China
    Article Snippet: Cells expressing the hRSV N protein were harvested by centrifugation at 2,500 × g for 15 minutes at 4°C, resuspended in lysis buffer (20 mM phosphate at pH7.4), and then sonicated at 4°C. .. The supernatant was purified using a HisTrap Q FF 5 ml column (GE Healthcare) followed by a HisTrap HP 1 ml column (GE Healthcare). .. The purification of N proteins was evaluated by 12% SDS-PAGE and optical density scanning using the Gene Genius Bio-imaging System (Syngene, Synoptics Ltd. Cambridge.

    Article Title: Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification
    Article Snippet: Cells were lysed by sonication and centrifuged to pellet cell debris as above. .. The soluble supernatant fraction was purified on a 5 ml HisTrap ff crude column (GE Healthcare, 17-5286-01) using the AKTA protein purification system (GE Healthcare). .. The column was washed with ten column volumes of 20 mM HEPES pH7, 200 mM NaCl and 25 mM imidazole (Sigma Aldrich, I5513).

    Article Title: The Rice Pentatricopeptide Repeat Protein RF5 Restores Fertility in Hong-Lian Cytoplasmic Male-Sterile Lines via a Complex with the Glycine-Rich Protein GRP162 [C]The Rice Pentatricopeptide Repeat Protein RF5 Restores Fertility in Hong-Lian Cytoplasmic Male-Sterile Lines via a Complex with the Glycine-Rich Protein GRP162 [C] [W]
    Article Snippet: These fragments were inserted into pET32a for expression (Novagen). .. The His-GRP162, His-RRM, and His-tag recombinant proteins were purified with a HisTrap FF column (GE Healthcare). .. The concentrations of the proteins were determined with a modified Lowry protein assay kit (Thermo Scientific).

    Protein Purification:

    Article Title: Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification
    Article Snippet: Cells were lysed by sonication and centrifuged to pellet cell debris as above. .. The soluble supernatant fraction was purified on a 5 ml HisTrap ff crude column (GE Healthcare, 17-5286-01) using the AKTA protein purification system (GE Healthcare). .. The column was washed with ten column volumes of 20 mM HEPES pH7, 200 mM NaCl and 25 mM imidazole (Sigma Aldrich, I5513).

    Recombinant:

    Article Title: The Rice Pentatricopeptide Repeat Protein RF5 Restores Fertility in Hong-Lian Cytoplasmic Male-Sterile Lines via a Complex with the Glycine-Rich Protein GRP162 [C]The Rice Pentatricopeptide Repeat Protein RF5 Restores Fertility in Hong-Lian Cytoplasmic Male-Sterile Lines via a Complex with the Glycine-Rich Protein GRP162 [C] [W]
    Article Snippet: These fragments were inserted into pET32a for expression (Novagen). .. The His-GRP162, His-RRM, and His-tag recombinant proteins were purified with a HisTrap FF column (GE Healthcare). .. The concentrations of the proteins were determined with a modified Lowry protein assay kit (Thermo Scientific).

    Centrifugation:

    Article Title: Engineering of monobody conjugates for human EphA2-specific optical imaging
    Article Snippet: The pellet was resuspended in 30 mL of Dulbecco’s phosphate buffered saline (DPBS) and lysed by sonication for 30 min at 4°C. .. Supernatants were obtained by centrifugation at 10,000 rpm at 4°C and applied to a HisTrap FF column (GE Healthcare Biosciences, PA) in an AKTA FPLC system (GE Healthcare Biosciences). ..

    Fast Protein Liquid Chromatography:

    Article Title: Engineering of monobody conjugates for human EphA2-specific optical imaging
    Article Snippet: The pellet was resuspended in 30 mL of Dulbecco’s phosphate buffered saline (DPBS) and lysed by sonication for 30 min at 4°C. .. Supernatants were obtained by centrifugation at 10,000 rpm at 4°C and applied to a HisTrap FF column (GE Healthcare Biosciences, PA) in an AKTA FPLC system (GE Healthcare Biosciences). ..

    Flow Cytometry:

    Article Title: Computational redesign of the Escherichia coli ribose-binding protein ligand binding pocket for 1,3-cyclohexanediol and cyclohexanol
    Article Snippet: .. The clean lysate was next loaded onto a HisTrap HP column (HisTrap FF crude 1 ml, GE Healthcare) at 4 °C and flow rate of 0.5 ml min−1 , followed by washes of, consecutively, 10 column volumes (cv, equal to 1 ml) of buffer A with 20 mM imidazole, 1.5 cv of buffer A with 40 mM imidazole and 1.5 cv of buffer A with 80 mM imidazole. ..

    Similar Products

  • Logo
  • About
  • News
  • Press Release
  • Team
  • Advisors
  • Partners
  • Contact
  • Bioz Stars
  • Bioz vStars
  • 97
    GE Healthcare crude histrap column
    PKA phosphorylates GPKOW at S27 and T316 in vitro . A . Recombinant GPKOW proteins were expressed in bacteria and purified on a <t>HisTrap</t> column followed by an ion exchange column. GPKOW wt (lane 1), GPKOW S27A (lane 2), GPKOW T316A (lane 3) and GPKOW S27A+T316A (lane 4) were all recognized by anti-GPKOW B01 after separation on SDS-PAGE and immunoblotting. One representative immunoblot is shown. B . Purified GPKOW wt (lanes 1 and 2), single- (lanes 3-6) or double-mutated GPKOW (lanes 7 and 8) were incubated with active (+) or heat inactivated (-) PKA Cα1 (7.4 ng) and γ- 32 P-ATP in a reaction buffer. The samples were analyzed by SDS-PAGE and autoradiography. The CBB staining in the lower panel shows the amount of the different proteins. C . Unsaturated images from Syngene G-box and Typhoon 9400 phosphoimager were quantified by Genetools (Syngene) and the statistical analysis was performed with paired students T-test in GraphPad Prism. The asterisk indicates a significant difference between the columns with a p-value
    Crude Histrap Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/crude histrap column/product/GE Healthcare
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    crude histrap column - by Bioz Stars, 2021-04
    97/100 stars
      Buy from Supplier

    97
    GE Healthcare histrap ff crude column
    Purification and oligomeric state of CdFic SE/AA . ( a ) Coomassie-stained 4–15% gradient SDS–PAGE of purified CdFic SE/AA . Lane M , molecular-weight marker (labelled in kDa). Lane 1, elution from the <t>HisTrap</t> affinity column, 1.8 µg
    Histrap Ff Crude Column, supplied by GE Healthcare, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/histrap ff crude column/product/GE Healthcare
    Average 97 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    histrap ff crude column - by Bioz Stars, 2021-04
    97/100 stars
      Buy from Supplier

    Image Search Results


    PKA phosphorylates GPKOW at S27 and T316 in vitro . A . Recombinant GPKOW proteins were expressed in bacteria and purified on a HisTrap column followed by an ion exchange column. GPKOW wt (lane 1), GPKOW S27A (lane 2), GPKOW T316A (lane 3) and GPKOW S27A+T316A (lane 4) were all recognized by anti-GPKOW B01 after separation on SDS-PAGE and immunoblotting. One representative immunoblot is shown. B . Purified GPKOW wt (lanes 1 and 2), single- (lanes 3-6) or double-mutated GPKOW (lanes 7 and 8) were incubated with active (+) or heat inactivated (-) PKA Cα1 (7.4 ng) and γ- 32 P-ATP in a reaction buffer. The samples were analyzed by SDS-PAGE and autoradiography. The CBB staining in the lower panel shows the amount of the different proteins. C . Unsaturated images from Syngene G-box and Typhoon 9400 phosphoimager were quantified by Genetools (Syngene) and the statistical analysis was performed with paired students T-test in GraphPad Prism. The asterisk indicates a significant difference between the columns with a p-value

    Journal: Journal of Molecular Signaling

    Article Title: G-patch domain and KOW motifs-containing protein, GPKOW; a nuclear RNA-binding protein regulated by protein kinase A

    doi: 10.1186/1750-2187-6-10

    Figure Lengend Snippet: PKA phosphorylates GPKOW at S27 and T316 in vitro . A . Recombinant GPKOW proteins were expressed in bacteria and purified on a HisTrap column followed by an ion exchange column. GPKOW wt (lane 1), GPKOW S27A (lane 2), GPKOW T316A (lane 3) and GPKOW S27A+T316A (lane 4) were all recognized by anti-GPKOW B01 after separation on SDS-PAGE and immunoblotting. One representative immunoblot is shown. B . Purified GPKOW wt (lanes 1 and 2), single- (lanes 3-6) or double-mutated GPKOW (lanes 7 and 8) were incubated with active (+) or heat inactivated (-) PKA Cα1 (7.4 ng) and γ- 32 P-ATP in a reaction buffer. The samples were analyzed by SDS-PAGE and autoradiography. The CBB staining in the lower panel shows the amount of the different proteins. C . Unsaturated images from Syngene G-box and Typhoon 9400 phosphoimager were quantified by Genetools (Syngene) and the statistical analysis was performed with paired students T-test in GraphPad Prism. The asterisk indicates a significant difference between the columns with a p-value

    Article Snippet: The bacteria were lysed in Buffer A (50 mM sodium dihydrogen phosphate pH 7.5, 0.2 M NaCl, 5 mM Imidazole, 1 × EDTA free protease inhibitor cocktail (Roche 04693132001) and 0.4 mM betamercaptoetanol) and purified on a crude HisTrap column (GE Healthcare 11-0004-58) using Buffer A and Buffer B (50 mM sodium dihydrogen phosphate pH 7.5, 0.2 M NaCl, 500 mM Imidazole, 1 × EDTA free protease inhibitor cocktail (Roche 04693132001) and 0.4 mM betamercaptoetanol).

    Techniques: In Vitro, Recombinant, Purification, SDS Page, Incubation, Autoradiography, Staining

    A , expression and purification of recombinant proteins. Proteins were expressed in E. coli BL21(DE3) strain. All proteins were expressed in fusion with the His 6 tag. Expressed recombinant proteins were purified using HisTrap FF crude columns (GE Healthcare).

    Journal: The Journal of Biological Chemistry

    Article Title: Biochemical Characterization and Substrate Specificity of Autophagin-2 from the Parasite Trypanosoma cruzi *

    doi: 10.1074/jbc.M115.687764

    Figure Lengend Snippet: A , expression and purification of recombinant proteins. Proteins were expressed in E. coli BL21(DE3) strain. All proteins were expressed in fusion with the His 6 tag. Expressed recombinant proteins were purified using HisTrap FF crude columns (GE Healthcare).

    Article Snippet: All proteins were expressed as fusion protein with a His6 tag and were allowed to bind to HisTrap FF crude columns (GE Healthcare) and eluted with buffer containing 250 m m imidazole.

    Techniques: Expressing, Purification, Recombinant

    Purification and oligomeric state of CdFic SE/AA . ( a ) Coomassie-stained 4–15% gradient SDS–PAGE of purified CdFic SE/AA . Lane M , molecular-weight marker (labelled in kDa). Lane 1, elution from the HisTrap affinity column, 1.8 µg

    Journal: Acta Crystallographica. Section F, Structural Biology Communications

    Article Title: Protein expression, characterization, crystallization and preliminary X-ray crystallographic analysis of a Fic protein from Clostridium difficile

    doi: 10.1107/S2053230X1400987X

    Figure Lengend Snippet: Purification and oligomeric state of CdFic SE/AA . ( a ) Coomassie-stained 4–15% gradient SDS–PAGE of purified CdFic SE/AA . Lane M , molecular-weight marker (labelled in kDa). Lane 1, elution from the HisTrap affinity column, 1.8 µg

    Article Snippet: The resulting supernatant was filtered with a 0.45 µm syringe filter before application onto a pre-packed 1 ml HisTrap FF Crude column (GE Healthcare) charged with Ni2+ and washed with 20 column volumes of 50 m M Tris pH 7.4, 300 m M NaCl, 5 m M β-mercaptoethanol, 5%( v / v ) glycerol, 20 m M imidazole.

    Techniques: Purification, Staining, SDS Page, Molecular Weight, Marker, Affinity Column

    Purified trKMO. (A) Chromatogram produced during NiNTA affinity purification of truncate KMO. (B) SDS-PAGE protein gel stained with simplyblue showing HisTrap purification of truncated human KMO protein, (a) Cell-free extract prior to affinity chromatography, (b) flowthrough proteins which did not bind to the column, (c) first column wash, (d) second column wash, (e) third column wash, (f) pure truncated human KMO protein (44 kDa) from the fractions under the chromatogram. (C) Cartoon illustrating the trKMO construct. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Journal: Protein Expression and Purification

    Article Title: Bacterial expression of human kynurenine 3-monooxygenase: Solubility, activity, purification

    doi: 10.1016/j.pep.2013.11.015

    Figure Lengend Snippet: Purified trKMO. (A) Chromatogram produced during NiNTA affinity purification of truncate KMO. (B) SDS-PAGE protein gel stained with simplyblue showing HisTrap purification of truncated human KMO protein, (a) Cell-free extract prior to affinity chromatography, (b) flowthrough proteins which did not bind to the column, (c) first column wash, (d) second column wash, (e) third column wash, (f) pure truncated human KMO protein (44 kDa) from the fractions under the chromatogram. (C) Cartoon illustrating the trKMO construct. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)

    Article Snippet: The soluble supernatant fraction was purified on a 5 ml HisTrap ff crude column (GE Healthcare, 17-5286-01) using the AKTA protein purification system (GE Healthcare).

    Techniques: Purification, Produced, Affinity Purification, SDS Page, Staining, Affinity Chromatography, Construct