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small airway epithelial cell growth medium  (PromoCell)


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    Structured Review

    PromoCell small airway epithelial cell growth medium
    BCL XL ‐PROTAC induces potent proteasomal degradation of BCL XL protein in human SAECs and shows high selectivity over BCL 2 degradation. Healthy small airway <t>epithelial</t> cells were treated with 10 −12 to 10 −4 M of BCL XL ‐PROTAC for 24 h. (a) BCL XL degradation by BCL XL ‐PROTAC via CRBN binder and MG132. (b) Protein levels of BCL XL and BCL 2 were measured in the cell lysates and the percentage of degradation, and the half maximal degradation concentration (DC 50 ) were calculated. (c) Cells were treated with BCL XL ‐PROTAC and 3 μM of the proteasome inhibitor MG132 or with a CRBN binder to compete with the E3 ligase binding. BCL XL degradation was measured in cell lysates and expressed as percentage of degradation and DC 50 . Plotted data are represented as mean +/− standard deviation of 3 independent experiments, each with 2 technical duplicates. 0% degradation indicate levels detected in vehicle/DMSO‐treated cells, and 100% degradation indicate no detectable BCL XL protein (= medium control).
    Small Airway Epithelial Cell Growth Medium, supplied by PromoCell, used in various techniques. Bioz Stars score: 95/100, based on 98 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/small airway epithelial cell growth medium/product/PromoCell
    Average 95 stars, based on 98 article reviews
    small airway epithelial cell growth medium - by Bioz Stars, 2026-05
    95/100 stars

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    1) Product Images from "Clearance of Senescent Cells by BCL XL ‐ PROTAC : A Novel Approach to Treat COPD ?"

    Article Title: Clearance of Senescent Cells by BCL XL ‐ PROTAC : A Novel Approach to Treat COPD ?

    Journal: Aging Cell

    doi: 10.1111/acel.70487

    BCL XL ‐PROTAC induces potent proteasomal degradation of BCL XL protein in human SAECs and shows high selectivity over BCL 2 degradation. Healthy small airway epithelial cells were treated with 10 −12 to 10 −4 M of BCL XL ‐PROTAC for 24 h. (a) BCL XL degradation by BCL XL ‐PROTAC via CRBN binder and MG132. (b) Protein levels of BCL XL and BCL 2 were measured in the cell lysates and the percentage of degradation, and the half maximal degradation concentration (DC 50 ) were calculated. (c) Cells were treated with BCL XL ‐PROTAC and 3 μM of the proteasome inhibitor MG132 or with a CRBN binder to compete with the E3 ligase binding. BCL XL degradation was measured in cell lysates and expressed as percentage of degradation and DC 50 . Plotted data are represented as mean +/− standard deviation of 3 independent experiments, each with 2 technical duplicates. 0% degradation indicate levels detected in vehicle/DMSO‐treated cells, and 100% degradation indicate no detectable BCL XL protein (= medium control).
    Figure Legend Snippet: BCL XL ‐PROTAC induces potent proteasomal degradation of BCL XL protein in human SAECs and shows high selectivity over BCL 2 degradation. Healthy small airway epithelial cells were treated with 10 −12 to 10 −4 M of BCL XL ‐PROTAC for 24 h. (a) BCL XL degradation by BCL XL ‐PROTAC via CRBN binder and MG132. (b) Protein levels of BCL XL and BCL 2 were measured in the cell lysates and the percentage of degradation, and the half maximal degradation concentration (DC 50 ) were calculated. (c) Cells were treated with BCL XL ‐PROTAC and 3 μM of the proteasome inhibitor MG132 or with a CRBN binder to compete with the E3 ligase binding. BCL XL degradation was measured in cell lysates and expressed as percentage of degradation and DC 50 . Plotted data are represented as mean +/− standard deviation of 3 independent experiments, each with 2 technical duplicates. 0% degradation indicate levels detected in vehicle/DMSO‐treated cells, and 100% degradation indicate no detectable BCL XL protein (= medium control).

    Techniques Used: Concentration Assay, Binding Assay, Standard Deviation, Control



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    BCL XL ‐PROTAC induces potent proteasomal degradation of BCL XL protein in human SAECs and shows high selectivity over BCL 2 degradation. Healthy small airway <t>epithelial</t> cells were treated with 10 −12 to 10 −4 M of BCL XL ‐PROTAC for 24 h. (a) BCL XL degradation by BCL XL ‐PROTAC via CRBN binder and MG132. (b) Protein levels of BCL XL and BCL 2 were measured in the cell lysates and the percentage of degradation, and the half maximal degradation concentration (DC 50 ) were calculated. (c) Cells were treated with BCL XL ‐PROTAC and 3 μM of the proteasome inhibitor MG132 or with a CRBN binder to compete with the E3 ligase binding. BCL XL degradation was measured in cell lysates and expressed as percentage of degradation and DC 50 . Plotted data are represented as mean +/− standard deviation of 3 independent experiments, each with 2 technical duplicates. 0% degradation indicate levels detected in vehicle/DMSO‐treated cells, and 100% degradation indicate no detectable BCL XL protein (= medium control).
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    BCL XL ‐PROTAC induces potent proteasomal degradation of BCL XL protein in human SAECs and shows high selectivity over BCL 2 degradation. Healthy small airway <t>epithelial</t> cells were treated with 10 −12 to 10 −4 M of BCL XL ‐PROTAC for 24 h. (a) BCL XL degradation by BCL XL ‐PROTAC via CRBN binder and MG132. (b) Protein levels of BCL XL and BCL 2 were measured in the cell lysates and the percentage of degradation, and the half maximal degradation concentration (DC 50 ) were calculated. (c) Cells were treated with BCL XL ‐PROTAC and 3 μM of the proteasome inhibitor MG132 or with a CRBN binder to compete with the E3 ligase binding. BCL XL degradation was measured in cell lysates and expressed as percentage of degradation and DC 50 . Plotted data are represented as mean +/− standard deviation of 3 independent experiments, each with 2 technical duplicates. 0% degradation indicate levels detected in vehicle/DMSO‐treated cells, and 100% degradation indicate no detectable BCL XL protein (= medium control).
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    BCL XL ‐PROTAC induces potent proteasomal degradation of BCL XL protein in human SAECs and shows high selectivity over BCL 2 degradation. Healthy small airway <t>epithelial</t> cells were treated with 10 −12 to 10 −4 M of BCL XL ‐PROTAC for 24 h. (a) BCL XL degradation by BCL XL ‐PROTAC via CRBN binder and MG132. (b) Protein levels of BCL XL and BCL 2 were measured in the cell lysates and the percentage of degradation, and the half maximal degradation concentration (DC 50 ) were calculated. (c) Cells were treated with BCL XL ‐PROTAC and 3 μM of the proteasome inhibitor MG132 or with a CRBN binder to compete with the E3 ligase binding. BCL XL degradation was measured in cell lysates and expressed as percentage of degradation and DC 50 . Plotted data are represented as mean +/− standard deviation of 3 independent experiments, each with 2 technical duplicates. 0% degradation indicate levels detected in vehicle/DMSO‐treated cells, and 100% degradation indicate no detectable BCL XL protein (= medium control).
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    Image Search Results


    BCL XL ‐PROTAC induces potent proteasomal degradation of BCL XL protein in human SAECs and shows high selectivity over BCL 2 degradation. Healthy small airway epithelial cells were treated with 10 −12 to 10 −4 M of BCL XL ‐PROTAC for 24 h. (a) BCL XL degradation by BCL XL ‐PROTAC via CRBN binder and MG132. (b) Protein levels of BCL XL and BCL 2 were measured in the cell lysates and the percentage of degradation, and the half maximal degradation concentration (DC 50 ) were calculated. (c) Cells were treated with BCL XL ‐PROTAC and 3 μM of the proteasome inhibitor MG132 or with a CRBN binder to compete with the E3 ligase binding. BCL XL degradation was measured in cell lysates and expressed as percentage of degradation and DC 50 . Plotted data are represented as mean +/− standard deviation of 3 independent experiments, each with 2 technical duplicates. 0% degradation indicate levels detected in vehicle/DMSO‐treated cells, and 100% degradation indicate no detectable BCL XL protein (= medium control).

    Journal: Aging Cell

    Article Title: Clearance of Senescent Cells by BCL XL ‐ PROTAC : A Novel Approach to Treat COPD ?

    doi: 10.1111/acel.70487

    Figure Lengend Snippet: BCL XL ‐PROTAC induces potent proteasomal degradation of BCL XL protein in human SAECs and shows high selectivity over BCL 2 degradation. Healthy small airway epithelial cells were treated with 10 −12 to 10 −4 M of BCL XL ‐PROTAC for 24 h. (a) BCL XL degradation by BCL XL ‐PROTAC via CRBN binder and MG132. (b) Protein levels of BCL XL and BCL 2 were measured in the cell lysates and the percentage of degradation, and the half maximal degradation concentration (DC 50 ) were calculated. (c) Cells were treated with BCL XL ‐PROTAC and 3 μM of the proteasome inhibitor MG132 or with a CRBN binder to compete with the E3 ligase binding. BCL XL degradation was measured in cell lysates and expressed as percentage of degradation and DC 50 . Plotted data are represented as mean +/− standard deviation of 3 independent experiments, each with 2 technical duplicates. 0% degradation indicate levels detected in vehicle/DMSO‐treated cells, and 100% degradation indicate no detectable BCL XL protein (= medium control).

    Article Snippet: Primary small airway epithelial cells (SAEC) were cultured as monolayers in Small Airway Epithelial Cell Growth Medium (Promocell, Germany) on collagen (1% w/v) coated plates (Devulder et al. ).

    Techniques: Concentration Assay, Binding Assay, Standard Deviation, Control