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DSMZ pa tu 8988s
Pa Tu 8988s, supplied by DSMZ, 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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    DSMZ patu 8902
    dTAG V -1 is an exclusively selective, in vivo -compatible degrader of FKBP12 F36V -tagged proteins. ( a ) Schematic depiction of the dTAG system using VHL-recruiting dTAG molecules. VHL-recruiting dTAG molecules promote ternary complex formation between the FKBP12 F36V -tagged target protein and E3 ubiquitin ligase complex, inducing target protein ubiquitination and degradation. ( b ) Chemical structures of dTAG V -1 and dTAG V -1-NEG. ( c ) DMSO-normalized ratio of Nluc/Fluc signal of 293FT FKBP12 WT -Nluc or FKBP12 F36V -Nluc cells treated with dTAG V -1 or dTAG V -1-NEG molecules for 24 h. Data are presented as mean ± s.d. of n = 4 biologically independent samples and are representative of n = 3 independent experiments. ( d ) Protein abundance after treatment of <t>PATU-8902</t> LACZ-FKBP12 F36V clone with 500 nM dTAG V -1 for 4 h compared to DMSO treatment. Volcano plots depict fold change abundance relative to DMSO versus P value. Significance designations derived from a permutation-based FDR estimation (q
    Patu 8902, supplied by DSMZ, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/patu 8902/product/DSMZ
    Average 95 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    patu 8902 - by Bioz Stars, 2022-09
    95/100 stars
      Buy from Supplier

    90
    DSMZ cell culture pa tu 8988s
    dTAG V -1 is an exclusively selective, in vivo -compatible degrader of FKBP12 F36V -tagged proteins. ( a ) Schematic depiction of the dTAG system using VHL-recruiting dTAG molecules. VHL-recruiting dTAG molecules promote ternary complex formation between the FKBP12 F36V -tagged target protein and E3 ubiquitin ligase complex, inducing target protein ubiquitination and degradation. ( b ) Chemical structures of dTAG V -1 and dTAG V -1-NEG. ( c ) DMSO-normalized ratio of Nluc/Fluc signal of 293FT FKBP12 WT -Nluc or FKBP12 F36V -Nluc cells treated with dTAG V -1 or dTAG V -1-NEG molecules for 24 h. Data are presented as mean ± s.d. of n = 4 biologically independent samples and are representative of n = 3 independent experiments. ( d ) Protein abundance after treatment of <t>PATU-8902</t> LACZ-FKBP12 F36V clone with 500 nM dTAG V -1 for 4 h compared to DMSO treatment. Volcano plots depict fold change abundance relative to DMSO versus P value. Significance designations derived from a permutation-based FDR estimation (q
    Cell Culture Pa Tu 8988s, supplied by DSMZ, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/cell culture pa tu 8988s/product/DSMZ
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    cell culture pa tu 8988s - by Bioz Stars, 2022-09
    90/100 stars
      Buy from Supplier

    90
    DSMZ pa tu 8988s
    dTAG V -1 is an exclusively selective, in vivo -compatible degrader of FKBP12 F36V -tagged proteins. ( a ) Schematic depiction of the dTAG system using VHL-recruiting dTAG molecules. VHL-recruiting dTAG molecules promote ternary complex formation between the FKBP12 F36V -tagged target protein and E3 ubiquitin ligase complex, inducing target protein ubiquitination and degradation. ( b ) Chemical structures of dTAG V -1 and dTAG V -1-NEG. ( c ) DMSO-normalized ratio of Nluc/Fluc signal of 293FT FKBP12 WT -Nluc or FKBP12 F36V -Nluc cells treated with dTAG V -1 or dTAG V -1-NEG molecules for 24 h. Data are presented as mean ± s.d. of n = 4 biologically independent samples and are representative of n = 3 independent experiments. ( d ) Protein abundance after treatment of <t>PATU-8902</t> LACZ-FKBP12 F36V clone with 500 nM dTAG V -1 for 4 h compared to DMSO treatment. Volcano plots depict fold change abundance relative to DMSO versus P value. Significance designations derived from a permutation-based FDR estimation (q
    Pa Tu 8988s, supplied by DSMZ, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/pa tu 8988s/product/DSMZ
    Average 90 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    pa tu 8988s - by Bioz Stars, 2022-09
    90/100 stars
      Buy from Supplier

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    dTAG V -1 is an exclusively selective, in vivo -compatible degrader of FKBP12 F36V -tagged proteins. ( a ) Schematic depiction of the dTAG system using VHL-recruiting dTAG molecules. VHL-recruiting dTAG molecules promote ternary complex formation between the FKBP12 F36V -tagged target protein and E3 ubiquitin ligase complex, inducing target protein ubiquitination and degradation. ( b ) Chemical structures of dTAG V -1 and dTAG V -1-NEG. ( c ) DMSO-normalized ratio of Nluc/Fluc signal of 293FT FKBP12 WT -Nluc or FKBP12 F36V -Nluc cells treated with dTAG V -1 or dTAG V -1-NEG molecules for 24 h. Data are presented as mean ± s.d. of n = 4 biologically independent samples and are representative of n = 3 independent experiments. ( d ) Protein abundance after treatment of PATU-8902 LACZ-FKBP12 F36V clone with 500 nM dTAG V -1 for 4 h compared to DMSO treatment. Volcano plots depict fold change abundance relative to DMSO versus P value. Significance designations derived from a permutation-based FDR estimation (q

    Journal: bioRxiv

    Article Title: Rapid and direct control of target protein levels with VHL-recruiting dTAG molecules

    doi: 10.1101/2020.03.13.980946

    Figure Lengend Snippet: dTAG V -1 is an exclusively selective, in vivo -compatible degrader of FKBP12 F36V -tagged proteins. ( a ) Schematic depiction of the dTAG system using VHL-recruiting dTAG molecules. VHL-recruiting dTAG molecules promote ternary complex formation between the FKBP12 F36V -tagged target protein and E3 ubiquitin ligase complex, inducing target protein ubiquitination and degradation. ( b ) Chemical structures of dTAG V -1 and dTAG V -1-NEG. ( c ) DMSO-normalized ratio of Nluc/Fluc signal of 293FT FKBP12 WT -Nluc or FKBP12 F36V -Nluc cells treated with dTAG V -1 or dTAG V -1-NEG molecules for 24 h. Data are presented as mean ± s.d. of n = 4 biologically independent samples and are representative of n = 3 independent experiments. ( d ) Protein abundance after treatment of PATU-8902 LACZ-FKBP12 F36V clone with 500 nM dTAG V -1 for 4 h compared to DMSO treatment. Volcano plots depict fold change abundance relative to DMSO versus P value. Significance designations derived from a permutation-based FDR estimation (q

    Article Snippet: Cell lines The following cell lines were employed in this study: 293T (source: Thermo Fisher Scientific, media: DMEM with 10% FBS and 1% Penicillin-Streptomycin), 293FT (source: Thermo Fisher Scientific, media: DMEM with 10% FBS and 1% Penicillin-Streptomycin), PATU-8902 (source: DSMZ, media: DMEM with 10% FBS and 1% Penicillin-Streptomycin), MV4;11 (source: ATCC, media: RPMI with 10% FBS and 1% Penicillin-Streptomycin) and EWS502 (source: Dr. Stephen Lessnick, media: RPMI with 15% FBS and 1% Penicillin-Streptomycin-L-Glutamine).

    Techniques: In Vivo, Derivative Assay

    dTAG V -1 is an in vivo-compatible degrader of FKBP12 F36V -tagged proteins. a Immunoblot analysis of PATU-8902 FKBP12 F36V -KRAS G12V ; KRAS −/− clone treated with DMSO, dTAG V -1, or dTAG V -1-NEG for the indicated time-course. b Immunoblot analysis of 293T WT FKBP12 F36V -KRAS G12V or 293T VHL-/- FKBP12 F36V -KRAS G12V cells treated with DMSO or the indicated dTAG molecules for 24 h. Data in a , b are representative of n = 3 independent experiments. c DMSO-normalized antiproliferation of PATU-8902 LACZ-FKBP12 F36V or FKBP12 F36V -KRAS G12V ; KRAS -/- clones treated with dTAG V -1 or dTAG V -1-NEG for 120 h. Cells were cultured as ultra-low adherent 3D-spheroid suspensions. Data are presented as mean ± s.d. of n = 4 biologically independent samples and are representative of n = 3 independent experiments. d Bioluminescent imaging to evaluate degradation of luciferase-FKBP12 F36V in mice was performed daily as follows: day 0 to establish baseline signal, day 1–3 to monitor luciferase-FKBP12 F36V signal 4 h after vehicle or dTAG molecule treatment (T), day 4 to monitor duration of luciferase-FKBP12 F36V signal 28 h after third and final vehicle or dTAG molecule treatment. Total flux for each mouse is depicted. Data are presented from vehicle ( n = 5 biologically independent mice at day 0–4), dTAG-13 ( n = 5 biologically independent mice at day 0–3; n = 4 biologically independent mice at day 4) or dTAG V -1 ( n = 5 biologically independent mice at day 0–4) treated mice. P values are derived from a two-tailed Welch’s t -test (* P

    Journal: Nature Communications

    Article Title: Rapid and direct control of target protein levels with VHL-recruiting dTAG molecules

    doi: 10.1038/s41467-020-18377-w

    Figure Lengend Snippet: dTAG V -1 is an in vivo-compatible degrader of FKBP12 F36V -tagged proteins. a Immunoblot analysis of PATU-8902 FKBP12 F36V -KRAS G12V ; KRAS −/− clone treated with DMSO, dTAG V -1, or dTAG V -1-NEG for the indicated time-course. b Immunoblot analysis of 293T WT FKBP12 F36V -KRAS G12V or 293T VHL-/- FKBP12 F36V -KRAS G12V cells treated with DMSO or the indicated dTAG molecules for 24 h. Data in a , b are representative of n = 3 independent experiments. c DMSO-normalized antiproliferation of PATU-8902 LACZ-FKBP12 F36V or FKBP12 F36V -KRAS G12V ; KRAS -/- clones treated with dTAG V -1 or dTAG V -1-NEG for 120 h. Cells were cultured as ultra-low adherent 3D-spheroid suspensions. Data are presented as mean ± s.d. of n = 4 biologically independent samples and are representative of n = 3 independent experiments. d Bioluminescent imaging to evaluate degradation of luciferase-FKBP12 F36V in mice was performed daily as follows: day 0 to establish baseline signal, day 1–3 to monitor luciferase-FKBP12 F36V signal 4 h after vehicle or dTAG molecule treatment (T), day 4 to monitor duration of luciferase-FKBP12 F36V signal 28 h after third and final vehicle or dTAG molecule treatment. Total flux for each mouse is depicted. Data are presented from vehicle ( n = 5 biologically independent mice at day 0–4), dTAG-13 ( n = 5 biologically independent mice at day 0–3; n = 4 biologically independent mice at day 4) or dTAG V -1 ( n = 5 biologically independent mice at day 0–4) treated mice. P values are derived from a two-tailed Welch’s t -test (* P

    Article Snippet: Cell lines The following cell lines were employed in this study: 293T (source: ATCC #CRL-3216, media: DMEM with 10% FBS and 1% Penicillin–Streptomycin), 293FT (source: Thermo Fisher Scientific #R70007, media: DMEM with 10% FBS and 1% Penicillin–Streptomycin), PATU-8902 (source: DSMZ #ACC-179, media: DMEM with 10% FBS and 1% Penicillin–Streptomycin), MV4;11 (source: ATCC #CRL-9591, media: RPMI with 10% FBS and 1% Penicillin–Streptomycin) and EWS502 (source: kindly provided by Dr. Stephen L. Lessnick of Nationwide Children’s Hospital and established by Dr. Jonathan A. Fletcher of Harvard Medical School, media: RPMI with 15% FBS and 1% Penicillin–Streptomycin-l -Glutamine).

    Techniques: In Vivo, Clone Assay, Cell Culture, Imaging, Luciferase, Mouse Assay, Derivative Assay, Two Tailed Test

    dTAG V -1 is an exclusively selective degrader of FKBP12 F36V -tagged proteins. a Schematic depiction of the dTAG system using VHL-recruiting dTAG molecules. VHL-recruiting dTAG molecules promote ternary complex formation between the FKBP12 F36V -tagged target protein and E3 ubiquitin ligase complex, inducing target protein ubiquitination and degradation. b Chemical structures of dTAG V -1 and dTAG V -1-NEG. c DMSO-normalized ratio of Nluc/Fluc signal of 293FT FKBP12 WT -Nluc or FKBP12 F36V -Nluc cells treated with dTAG V -1 or dTAG V -1-NEG for 24 h. Data are presented as mean ± s.d. of n = 4 biologically independent samples and are representative of n = 3 independent experiments. d Protein abundance after treatment of PATU-8902 LACZ-FKBP12 F36V clone with 500 nM dTAG V -1 for 4 h compared to DMSO treatment. Volcano plots depict fold change abundance relative to DMSO versus P value derived from a two-tailed Student’s t -test. Fold change values and significance designations derived from a two-tailed Student’s t -test and a permutation-based FDR estimation are provided in Supplementary Data 2 . Data are from n = 3 biologically independent samples. e Immunoblot analysis of PATU-8902 LACZ-FKBP12 F36V clone co-treated with DMSO, THAL-SNS-032, and/or dTAG V -1 as indicated for 24 h. Data is representative of n = 3 independent experiments. Source data for c and e are provided as a Source Data file.

    Journal: Nature Communications

    Article Title: Rapid and direct control of target protein levels with VHL-recruiting dTAG molecules

    doi: 10.1038/s41467-020-18377-w

    Figure Lengend Snippet: dTAG V -1 is an exclusively selective degrader of FKBP12 F36V -tagged proteins. a Schematic depiction of the dTAG system using VHL-recruiting dTAG molecules. VHL-recruiting dTAG molecules promote ternary complex formation between the FKBP12 F36V -tagged target protein and E3 ubiquitin ligase complex, inducing target protein ubiquitination and degradation. b Chemical structures of dTAG V -1 and dTAG V -1-NEG. c DMSO-normalized ratio of Nluc/Fluc signal of 293FT FKBP12 WT -Nluc or FKBP12 F36V -Nluc cells treated with dTAG V -1 or dTAG V -1-NEG for 24 h. Data are presented as mean ± s.d. of n = 4 biologically independent samples and are representative of n = 3 independent experiments. d Protein abundance after treatment of PATU-8902 LACZ-FKBP12 F36V clone with 500 nM dTAG V -1 for 4 h compared to DMSO treatment. Volcano plots depict fold change abundance relative to DMSO versus P value derived from a two-tailed Student’s t -test. Fold change values and significance designations derived from a two-tailed Student’s t -test and a permutation-based FDR estimation are provided in Supplementary Data 2 . Data are from n = 3 biologically independent samples. e Immunoblot analysis of PATU-8902 LACZ-FKBP12 F36V clone co-treated with DMSO, THAL-SNS-032, and/or dTAG V -1 as indicated for 24 h. Data is representative of n = 3 independent experiments. Source data for c and e are provided as a Source Data file.

    Article Snippet: Cell lines The following cell lines were employed in this study: 293T (source: ATCC #CRL-3216, media: DMEM with 10% FBS and 1% Penicillin–Streptomycin), 293FT (source: Thermo Fisher Scientific #R70007, media: DMEM with 10% FBS and 1% Penicillin–Streptomycin), PATU-8902 (source: DSMZ #ACC-179, media: DMEM with 10% FBS and 1% Penicillin–Streptomycin), MV4;11 (source: ATCC #CRL-9591, media: RPMI with 10% FBS and 1% Penicillin–Streptomycin) and EWS502 (source: kindly provided by Dr. Stephen L. Lessnick of Nationwide Children’s Hospital and established by Dr. Jonathan A. Fletcher of Harvard Medical School, media: RPMI with 15% FBS and 1% Penicillin–Streptomycin-l -Glutamine).

    Techniques: Derivative Assay, Two Tailed Test