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d7324 tags  (Biosynth Carbosynth)


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    Biosynth Carbosynth d7324 tags
    Characterization of BG505 SOS.664-dPG and related Env proteins. ( A ). <t>D7324-capture</t> ELISA with unpurified D7324-tagged BG505 SOS.664, SOS.664-dPG, and BG505 SOSIP.664 trimers expressed in the supernatant of HEK293T cells. ( B ) Top: SEC curve of BG505 SOS.664-dPG produced in suspension 293S cells and purified using 2G12 affinity chromatography. Bottom: BN-PAGE analysis of the SEC fractions depicted above. ( C ) NS-EM analysis on 2G12/SEC-purified BG505 SOS.664-dPG.
    D7324 Tags, supplied by Biosynth Carbosynth, used in various techniques. Bioz Stars score: 93/100, based on 50 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/d7324+tags/pmc12455988-246-7-24?v=Biosynth+Carbosynth
    Average 93 stars, based on 50 article reviews
    d7324 tags - by Bioz Stars, 2026-07
    93/100 stars

    Images

    1) Product Images from "A modification to heptad repeat 1 of gp41 improves yield and/or quality of soluble pre-fusion HIV-1 envelope glycoprotein trimers"

    Article Title: A modification to heptad repeat 1 of gp41 improves yield and/or quality of soluble pre-fusion HIV-1 envelope glycoprotein trimers

    Journal: Journal of Virology

    doi: 10.1128/jvi.00913-25

    Characterization of BG505 SOS.664-dPG and related Env proteins. ( A ). D7324-capture ELISA with unpurified D7324-tagged BG505 SOS.664, SOS.664-dPG, and BG505 SOSIP.664 trimers expressed in the supernatant of HEK293T cells. ( B ) Top: SEC curve of BG505 SOS.664-dPG produced in suspension 293S cells and purified using 2G12 affinity chromatography. Bottom: BN-PAGE analysis of the SEC fractions depicted above. ( C ) NS-EM analysis on 2G12/SEC-purified BG505 SOS.664-dPG.
    Figure Legend Snippet: Characterization of BG505 SOS.664-dPG and related Env proteins. ( A ). D7324-capture ELISA with unpurified D7324-tagged BG505 SOS.664, SOS.664-dPG, and BG505 SOSIP.664 trimers expressed in the supernatant of HEK293T cells. ( B ) Top: SEC curve of BG505 SOS.664-dPG produced in suspension 293S cells and purified using 2G12 affinity chromatography. Bottom: BN-PAGE analysis of the SEC fractions depicted above. ( C ) NS-EM analysis on 2G12/SEC-purified BG505 SOS.664-dPG.

    Techniques Used: Enzyme-linked Immunosorbent Assay, Produced, Suspension, Purification, Affinity Chromatography



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    Characterization of BG505 SOS.664-dPG and related Env proteins. ( A ). <t>D7324-capture</t> ELISA with unpurified D7324-tagged BG505 SOS.664, SOS.664-dPG, and BG505 SOSIP.664 trimers expressed in the supernatant of HEK293T cells. ( B ) Top: SEC curve of BG505 SOS.664-dPG produced in suspension 293S cells and purified using 2G12 affinity chromatography. Bottom: BN-PAGE analysis of the SEC fractions depicted above. ( C ) NS-EM analysis on 2G12/SEC-purified BG505 SOS.664-dPG.
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    Image Search Results


    Characterization of BG505 SOS.664-dPG and related Env proteins. ( A ). D7324-capture ELISA with unpurified D7324-tagged BG505 SOS.664, SOS.664-dPG, and BG505 SOSIP.664 trimers expressed in the supernatant of HEK293T cells. ( B ) Top: SEC curve of BG505 SOS.664-dPG produced in suspension 293S cells and purified using 2G12 affinity chromatography. Bottom: BN-PAGE analysis of the SEC fractions depicted above. ( C ) NS-EM analysis on 2G12/SEC-purified BG505 SOS.664-dPG.

    Journal: Journal of Virology

    Article Title: A modification to heptad repeat 1 of gp41 improves yield and/or quality of soluble pre-fusion HIV-1 envelope glycoprotein trimers

    doi: 10.1128/jvi.00913-25

    Figure Lengend Snippet: Characterization of BG505 SOS.664-dPG and related Env proteins. ( A ). D7324-capture ELISA with unpurified D7324-tagged BG505 SOS.664, SOS.664-dPG, and BG505 SOSIP.664 trimers expressed in the supernatant of HEK293T cells. ( B ) Top: SEC curve of BG505 SOS.664-dPG produced in suspension 293S cells and purified using 2G12 affinity chromatography. Bottom: BN-PAGE analysis of the SEC fractions depicted above. ( C ) NS-EM analysis on 2G12/SEC-purified BG505 SOS.664-dPG.

    Article Snippet: The trimers were then immobilized via their D7324 tags for 2 h at room temperature on half-well 96-well plates (Greiner) precoated with Ab D7324 (Aalto Bioreagents) at 10 μg/mL in 0.1 M NaHCO3, pH 8.6 overnight ( ).

    Techniques: Enzyme-linked Immunosorbent Assay, Produced, Suspension, Purification, Affinity Chromatography

    Figure 7. Comparison in Biophysical and Antigenic Properties between CNE40 SOSIP.664 gp140 Trimers Bearing the Wild- Type E658 and Mutant K658 Residue (A) Linear representation of CNE40 SOSIP.664 gp140 Env with D7324 tag, bearing the wild-type E658 or mutant K658 residue. (B) Size exclusion chromatography (SEC) pro- files of 293F-expressed, GNL-purified CNE40 SOSIP.664 gp140 trimers with wild-type E658 or mutant K658 residue. The y axis shows the absorbance at UV280. Peaks of protein aggrega- tion, trimer, and dimer and monomer complex are indicated with dotted line for trimer. Data shown are representative of three independent experiments. (C) Thermal stability of CNE40 SOSIP.664 gp140 Env with wild-type E658 or mutant K658 residue measured by DSC. Tm, thermal denaturation midpoint temperature. Data shown are represen- tative of two independent experiments. (D) Comparison of trimer content between CNE40 SOSIP.664 gp140 Env bearing the wild-type E658 or mutant K658 residue. Data shown represent the average of three independent repeats. Statistical analysis was performed using an unpaired t test. *p < 0.05. (E) Comparison of antigenic property between CNE40 SOSIP.664 gp140 Env bearing the wild- type E658 or mutant K658 residue. Antibody binding is measured by ELISA and summarized as the area under the curve (AUC). Shown are repre- sentative data from two independent experiments.

    Journal: Cell reports

    Article Title: A Single Substitution in gp41 Modulates the Neutralization Profile of SHIV during In Vivo Adaptation.

    doi: 10.1016/j.celrep.2019.04.108

    Figure Lengend Snippet: Figure 7. Comparison in Biophysical and Antigenic Properties between CNE40 SOSIP.664 gp140 Trimers Bearing the Wild- Type E658 and Mutant K658 Residue (A) Linear representation of CNE40 SOSIP.664 gp140 Env with D7324 tag, bearing the wild-type E658 or mutant K658 residue. (B) Size exclusion chromatography (SEC) pro- files of 293F-expressed, GNL-purified CNE40 SOSIP.664 gp140 trimers with wild-type E658 or mutant K658 residue. The y axis shows the absorbance at UV280. Peaks of protein aggrega- tion, trimer, and dimer and monomer complex are indicated with dotted line for trimer. Data shown are representative of three independent experiments. (C) Thermal stability of CNE40 SOSIP.664 gp140 Env with wild-type E658 or mutant K658 residue measured by DSC. Tm, thermal denaturation midpoint temperature. Data shown are represen- tative of two independent experiments. (D) Comparison of trimer content between CNE40 SOSIP.664 gp140 Env bearing the wild-type E658 or mutant K658 residue. Data shown represent the average of three independent repeats. Statistical analysis was performed using an unpaired t test. *p < 0.05. (E) Comparison of antigenic property between CNE40 SOSIP.664 gp140 Env bearing the wild- type E658 or mutant K658 residue. Antibody binding is measured by ELISA and summarized as the area under the curve (AUC). Shown are repre- sentative data from two independent experiments.

    Article Snippet: 96-well plates were coated with C5 tag-specific antibody D7324 (Aalto Bioreagents, Dublin, Ireland) at 10 mg/ml Cell Reports 27, 2593–2607.e1–e5, May 28, 2019 e4 (100 ml/well).

    Techniques: Comparison, Mutagenesis, Residue, Size-exclusion Chromatography, Binding Assay, Enzyme-linked Immunosorbent Assay