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third generation lentiviral packaging vectors  (Addgene inc)


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    Addgene inc third generation lentiviral packaging vectors
    Figure 2. Zinc and cadmium metal toxicity in MT2A knockdown. (A) Amino acid alignment of the 11 expressed human metallothioneins. Note that cysteine residues, which chelate metals, are highly conserved among the proteins and represent a third of all the amino acids in metallothioneins. (B) Nuclear magnetic resonance structure of metallothionein MT2A alpha (PDB ID: 2MRB) and beta (PDB ID:1MRB) domains, with bound Cd2+ ions shown. Zn2+ ions are predicted to be similarly located within the protein in the absence of Cd2+. (C) CAOV3 cells, which only express MT2A (higher) and MT1X (lower), were knocked down by <t>lentiviral</t> shMT2A and validated by RT-qPCR as reduced in expression relative to scrambled shRNA control (shScr). (D) ZnCl2 toxicity was assessed by Hoechst-33342-stained nuclei counts relative to control treated cells, with 2-day (2 d) or 3 d exposure. (E) CdCl2 toxicity was assessed as in (D). Error bars are standard error of the mean. * p < 0.05, ** p < 0.01, *** p < 0.001 by t-test of technical replicates relative to shScr control from a representative experiment.
    Third Generation Lentiviral Packaging Vectors, supplied by Addgene inc, used in various techniques. Bioz Stars score: 98/100, based on 13190 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/third generation lentiviral packaging vectors/product/Addgene inc
    Average 98 stars, based on 13190 article reviews
    third generation lentiviral packaging vectors - by Bioz Stars, 2026-03
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    Images

    1) Product Images from "Screening Methods to Discover the FDA-Approved Cancer Drug Encorafenib as Optimally Selective for Metallothionein Gene Loss Ovarian Cancer."

    Article Title: Screening Methods to Discover the FDA-Approved Cancer Drug Encorafenib as Optimally Selective for Metallothionein Gene Loss Ovarian Cancer.

    Journal: Genes

    doi: 10.3390/genes16010042

    Figure 2. Zinc and cadmium metal toxicity in MT2A knockdown. (A) Amino acid alignment of the 11 expressed human metallothioneins. Note that cysteine residues, which chelate metals, are highly conserved among the proteins and represent a third of all the amino acids in metallothioneins. (B) Nuclear magnetic resonance structure of metallothionein MT2A alpha (PDB ID: 2MRB) and beta (PDB ID:1MRB) domains, with bound Cd2+ ions shown. Zn2+ ions are predicted to be similarly located within the protein in the absence of Cd2+. (C) CAOV3 cells, which only express MT2A (higher) and MT1X (lower), were knocked down by lentiviral shMT2A and validated by RT-qPCR as reduced in expression relative to scrambled shRNA control (shScr). (D) ZnCl2 toxicity was assessed by Hoechst-33342-stained nuclei counts relative to control treated cells, with 2-day (2 d) or 3 d exposure. (E) CdCl2 toxicity was assessed as in (D). Error bars are standard error of the mean. * p < 0.05, ** p < 0.01, *** p < 0.001 by t-test of technical replicates relative to shScr control from a representative experiment.
    Figure Legend Snippet: Figure 2. Zinc and cadmium metal toxicity in MT2A knockdown. (A) Amino acid alignment of the 11 expressed human metallothioneins. Note that cysteine residues, which chelate metals, are highly conserved among the proteins and represent a third of all the amino acids in metallothioneins. (B) Nuclear magnetic resonance structure of metallothionein MT2A alpha (PDB ID: 2MRB) and beta (PDB ID:1MRB) domains, with bound Cd2+ ions shown. Zn2+ ions are predicted to be similarly located within the protein in the absence of Cd2+. (C) CAOV3 cells, which only express MT2A (higher) and MT1X (lower), were knocked down by lentiviral shMT2A and validated by RT-qPCR as reduced in expression relative to scrambled shRNA control (shScr). (D) ZnCl2 toxicity was assessed by Hoechst-33342-stained nuclei counts relative to control treated cells, with 2-day (2 d) or 3 d exposure. (E) CdCl2 toxicity was assessed as in (D). Error bars are standard error of the mean. * p < 0.05, ** p < 0.01, *** p < 0.001 by t-test of technical replicates relative to shScr control from a representative experiment.

    Techniques Used: Knockdown, Nuclear Magnetic Resonance, Quantitative RT-PCR, Expressing, shRNA, Control, Staining



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    third generation lentiviral packaging vectors  (Addgene inc)
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    Addgene inc third generation lentiviral packaging vectors
    Figure 2. Zinc and cadmium metal toxicity in MT2A knockdown. (A) Amino acid alignment of the 11 expressed human metallothioneins. Note that cysteine residues, which chelate metals, are highly conserved among the proteins and represent a third of all the amino acids in metallothioneins. (B) Nuclear magnetic resonance structure of metallothionein MT2A alpha (PDB ID: 2MRB) and beta (PDB ID:1MRB) domains, with bound Cd2+ ions shown. Zn2+ ions are predicted to be similarly located within the protein in the absence of Cd2+. (C) CAOV3 cells, which only express MT2A (higher) and MT1X (lower), were knocked down by <t>lentiviral</t> shMT2A and validated by RT-qPCR as reduced in expression relative to scrambled shRNA control (shScr). (D) ZnCl2 toxicity was assessed by Hoechst-33342-stained nuclei counts relative to control treated cells, with 2-day (2 d) or 3 d exposure. (E) CdCl2 toxicity was assessed as in (D). Error bars are standard error of the mean. * p < 0.05, ** p < 0.01, *** p < 0.001 by t-test of technical replicates relative to shScr control from a representative experiment.
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    Figure 2. Zinc and cadmium metal toxicity in MT2A knockdown. (A) Amino acid alignment of the 11 expressed human metallothioneins. Note that cysteine residues, which chelate metals, are highly conserved among the proteins and represent a third of all the amino acids in metallothioneins. (B) Nuclear magnetic resonance structure of metallothionein MT2A alpha (PDB ID: 2MRB) and beta (PDB ID:1MRB) domains, with bound Cd2+ ions shown. Zn2+ ions are predicted to be similarly located within the protein in the absence of Cd2+. (C) CAOV3 cells, which only express MT2A (higher) and MT1X (lower), were knocked down by <t>lentiviral</t> shMT2A and validated by RT-qPCR as reduced in expression relative to scrambled shRNA control (shScr). (D) ZnCl2 toxicity was assessed by Hoechst-33342-stained nuclei counts relative to control treated cells, with 2-day (2 d) or 3 d exposure. (E) CdCl2 toxicity was assessed as in (D). Error bars are standard error of the mean. * p < 0.05, ** p < 0.01, *** p < 0.001 by t-test of technical replicates relative to shScr control from a representative experiment.
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    Figure 2. Zinc and cadmium metal toxicity in MT2A knockdown. (A) Amino acid alignment of the 11 expressed human metallothioneins. Note that cysteine residues, which chelate metals, are highly conserved among the proteins and represent a third of all the amino acids in metallothioneins. (B) Nuclear magnetic resonance structure of metallothionein MT2A alpha (PDB ID: 2MRB) and beta (PDB ID:1MRB) domains, with bound Cd2+ ions shown. Zn2+ ions are predicted to be similarly located within the protein in the absence of Cd2+. (C) CAOV3 cells, which only express MT2A (higher) and MT1X (lower), were knocked down by <t>lentiviral</t> shMT2A and validated by RT-qPCR as reduced in expression relative to scrambled shRNA control (shScr). (D) ZnCl2 toxicity was assessed by Hoechst-33342-stained nuclei counts relative to control treated cells, with 2-day (2 d) or 3 d exposure. (E) CdCl2 toxicity was assessed as in (D). Error bars are standard error of the mean. * p < 0.05, ** p < 0.01, *** p < 0.001 by t-test of technical replicates relative to shScr control from a representative experiment.
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    Image Search Results


    Figure 2. Zinc and cadmium metal toxicity in MT2A knockdown. (A) Amino acid alignment of the 11 expressed human metallothioneins. Note that cysteine residues, which chelate metals, are highly conserved among the proteins and represent a third of all the amino acids in metallothioneins. (B) Nuclear magnetic resonance structure of metallothionein MT2A alpha (PDB ID: 2MRB) and beta (PDB ID:1MRB) domains, with bound Cd2+ ions shown. Zn2+ ions are predicted to be similarly located within the protein in the absence of Cd2+. (C) CAOV3 cells, which only express MT2A (higher) and MT1X (lower), were knocked down by lentiviral shMT2A and validated by RT-qPCR as reduced in expression relative to scrambled shRNA control (shScr). (D) ZnCl2 toxicity was assessed by Hoechst-33342-stained nuclei counts relative to control treated cells, with 2-day (2 d) or 3 d exposure. (E) CdCl2 toxicity was assessed as in (D). Error bars are standard error of the mean. * p < 0.05, ** p < 0.01, *** p < 0.001 by t-test of technical replicates relative to shScr control from a representative experiment.

    Journal: Genes

    Article Title: Screening Methods to Discover the FDA-Approved Cancer Drug Encorafenib as Optimally Selective for Metallothionein Gene Loss Ovarian Cancer.

    doi: 10.3390/genes16010042

    Figure Lengend Snippet: Figure 2. Zinc and cadmium metal toxicity in MT2A knockdown. (A) Amino acid alignment of the 11 expressed human metallothioneins. Note that cysteine residues, which chelate metals, are highly conserved among the proteins and represent a third of all the amino acids in metallothioneins. (B) Nuclear magnetic resonance structure of metallothionein MT2A alpha (PDB ID: 2MRB) and beta (PDB ID:1MRB) domains, with bound Cd2+ ions shown. Zn2+ ions are predicted to be similarly located within the protein in the absence of Cd2+. (C) CAOV3 cells, which only express MT2A (higher) and MT1X (lower), were knocked down by lentiviral shMT2A and validated by RT-qPCR as reduced in expression relative to scrambled shRNA control (shScr). (D) ZnCl2 toxicity was assessed by Hoechst-33342-stained nuclei counts relative to control treated cells, with 2-day (2 d) or 3 d exposure. (E) CdCl2 toxicity was assessed as in (D). Error bars are standard error of the mean. * p < 0.05, ** p < 0.01, *** p < 0.001 by t-test of technical replicates relative to shScr control from a representative experiment.

    Article Snippet: Fluorescent protein nls-GFP (Addgene, #126688) or nls-BFP (Addgene, #36085) was stably added via lentivirus using third generation lentiviral packaging vectors (Addgene, #12251, 12253, 12259) packaged in HEK293T cells (ATCC, #CRL-3216).

    Techniques: Knockdown, Nuclear Magnetic Resonance, Quantitative RT-PCR, Expressing, shRNA, Control, Staining