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pmt myc bira  (Addgene inc)


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    Addgene inc pmt myc bira
    Pmt Myc Bira, supplied by Addgene inc, used in various techniques. Bioz Stars score: 93/100, based on 10 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pmt myc bira/product/Addgene inc
    Average 93 stars, based on 10 article reviews
    pmt myc bira - by Bioz Stars, 2026-06
    93/100 stars

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    A. Structure of human CBX8, CBX7, CBX1 PCD and BAHCC1 BAH domains (RCSB PDB 3I91, 4X3K, 6D07 and 6VIL) with hydrophobic binding pocket residues highlighted in light blue. Residue substitutions in engineered variants (sea green) are as follows: dCBX7 - F11A; CBX7.VD - Q9D, K33E; CBX1eR - K43A, D59F. B. ELISA binding results for CBX8 fusion proteins. C. ELISA binding results for wild-type and engineered H3K27me3-binding fusion proteins. Dots = mean A450 from 3 technical replicate wells, bars = mean of 2 replicate TX-TL products, error bars = standard deviation.

    Journal: bioRxiv

    Article Title: An engineered chromatin protein with enhanced preferential binding of H3K27me3 over H3K9me3

    doi: 10.1101/2024.10.02.616304

    Figure Lengend Snippet: A. Structure of human CBX8, CBX7, CBX1 PCD and BAHCC1 BAH domains (RCSB PDB 3I91, 4X3K, 6D07 and 6VIL) with hydrophobic binding pocket residues highlighted in light blue. Residue substitutions in engineered variants (sea green) are as follows: dCBX7 - F11A; CBX7.VD - Q9D, K33E; CBX1eR - K43A, D59F. B. ELISA binding results for CBX8 fusion proteins. C. ELISA binding results for wild-type and engineered H3K27me3-binding fusion proteins. Dots = mean A450 from 3 technical replicate wells, bars = mean of 2 replicate TX-TL products, error bars = standard deviation.

    Article Snippet: Plasmid templates from Addgene included CBX1 (ID 180212) and CBX1eR (ID 135089).

    Techniques: Binding Assay, Residue, Enzyme-linked Immunosorbent Assay, Standard Deviation

    A. ELISA binding data for top-performing homotypic CBX8 variants after the introduction of K33E. Dots = mean A450 from 3 technical replicate wells, bars = mean of 2 replicate TX-TL products, error bars = standard deviation. **** p ≤ 0.0001 B. Specificity profiling of homotypic CBX fusion proteins against a panel of unmethylated and methylated histone peptides. Absorbance signal for each histone PTM is normalized to the average signal from the H3 unmodified (negative control) ELISA wells. C. Fold increase of binding to H3K27me3 and H3K9me3 for top-performing CBX8 variants compared to wild-type CBX8. Values for H3K27me3-reader CBX7.VD and H3K9me3-readers CBX1 and CBX1eR are included for comparison.

    Journal: bioRxiv

    Article Title: An engineered chromatin protein with enhanced preferential binding of H3K27me3 over H3K9me3

    doi: 10.1101/2024.10.02.616304

    Figure Lengend Snippet: A. ELISA binding data for top-performing homotypic CBX8 variants after the introduction of K33E. Dots = mean A450 from 3 technical replicate wells, bars = mean of 2 replicate TX-TL products, error bars = standard deviation. **** p ≤ 0.0001 B. Specificity profiling of homotypic CBX fusion proteins against a panel of unmethylated and methylated histone peptides. Absorbance signal for each histone PTM is normalized to the average signal from the H3 unmodified (negative control) ELISA wells. C. Fold increase of binding to H3K27me3 and H3K9me3 for top-performing CBX8 variants compared to wild-type CBX8. Values for H3K27me3-reader CBX7.VD and H3K9me3-readers CBX1 and CBX1eR are included for comparison.

    Article Snippet: Plasmid templates from Addgene included CBX1 (ID 180212) and CBX1eR (ID 135089).

    Techniques: Enzyme-linked Immunosorbent Assay, Binding Assay, Standard Deviation, Methylation, Negative Control, Comparison