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ssf-mor plasmid glosensor 22f  (Promega)

 
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    Structured Review

    Promega ssf-mor plasmid glosensor 22f
    (A) Reaction scheme depicting the one-step alkylation procedure used to synthesize DEAC-OXM from commercially available oxymorphone ( 2 ) and DEAC-Br, as well as its photochemical conversion to the proposed primary reaction product “rearranged DEAC-OXM” (RE-DEAC-OXM), which likely occurs via a 1,4-Photo-Claisen rearrangement. (B) High pressure liquid chromatography (HPLC) chromatograms measured at 220 nm indicating predominant photoconversion of DEAC-OXM to RE-DEAC-OXM, which has a similar retention time, along with a much smaller amount of OXM in PBS (pH 7.2). (C) (Top) LC-MS (mass spectrometry) chromatogram of the reaction mixture shown in B. (Bottom) MS traces revealing that RE-DEAC-OXM has the same molecular weight as DEAC-OXM (531 Da). (D) Agonist dose-response curves at the MOR for DEAC-OXM, RE-DEAC-OXM, and OXM using the <t>GloSensor™</t> assay of cAMP signaling in HEK293T cells. The solid line depicts the best-fit sigmoidal function used to derive the indicated EC 50 value. OXM EC 50 = 1.3 nM, DEAC-OXM EC 50 = 380 nM, RE-DEAC-OXM EC 50 = 1.3 µM. Data were normalized to the response produced by DAMGO (1 µM) and are expressed as mean ± SEM (n=5-10 wells per concentration).
    Ssf Mor Plasmid Glosensor 22f, supplied by Promega, 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/ssf-mor plasmid glosensor 22f/product/Promega
    Average 90 stars, based on 1 article reviews
    ssf-mor plasmid glosensor 22f - by Bioz Stars, 2026-05
    90/100 stars

    Images

    1) Product Images from "In vivo photopharmacology with light-activated opioid drugs"

    Article Title: In vivo photopharmacology with light-activated opioid drugs

    Journal: bioRxiv

    doi: 10.1101/2023.02.02.526901

    (A) Reaction scheme depicting the one-step alkylation procedure used to synthesize DEAC-OXM from commercially available oxymorphone ( 2 ) and DEAC-Br, as well as its photochemical conversion to the proposed primary reaction product “rearranged DEAC-OXM” (RE-DEAC-OXM), which likely occurs via a 1,4-Photo-Claisen rearrangement. (B) High pressure liquid chromatography (HPLC) chromatograms measured at 220 nm indicating predominant photoconversion of DEAC-OXM to RE-DEAC-OXM, which has a similar retention time, along with a much smaller amount of OXM in PBS (pH 7.2). (C) (Top) LC-MS (mass spectrometry) chromatogram of the reaction mixture shown in B. (Bottom) MS traces revealing that RE-DEAC-OXM has the same molecular weight as DEAC-OXM (531 Da). (D) Agonist dose-response curves at the MOR for DEAC-OXM, RE-DEAC-OXM, and OXM using the GloSensor™ assay of cAMP signaling in HEK293T cells. The solid line depicts the best-fit sigmoidal function used to derive the indicated EC 50 value. OXM EC 50 = 1.3 nM, DEAC-OXM EC 50 = 380 nM, RE-DEAC-OXM EC 50 = 1.3 µM. Data were normalized to the response produced by DAMGO (1 µM) and are expressed as mean ± SEM (n=5-10 wells per concentration).
    Figure Legend Snippet: (A) Reaction scheme depicting the one-step alkylation procedure used to synthesize DEAC-OXM from commercially available oxymorphone ( 2 ) and DEAC-Br, as well as its photochemical conversion to the proposed primary reaction product “rearranged DEAC-OXM” (RE-DEAC-OXM), which likely occurs via a 1,4-Photo-Claisen rearrangement. (B) High pressure liquid chromatography (HPLC) chromatograms measured at 220 nm indicating predominant photoconversion of DEAC-OXM to RE-DEAC-OXM, which has a similar retention time, along with a much smaller amount of OXM in PBS (pH 7.2). (C) (Top) LC-MS (mass spectrometry) chromatogram of the reaction mixture shown in B. (Bottom) MS traces revealing that RE-DEAC-OXM has the same molecular weight as DEAC-OXM (531 Da). (D) Agonist dose-response curves at the MOR for DEAC-OXM, RE-DEAC-OXM, and OXM using the GloSensor™ assay of cAMP signaling in HEK293T cells. The solid line depicts the best-fit sigmoidal function used to derive the indicated EC 50 value. OXM EC 50 = 1.3 nM, DEAC-OXM EC 50 = 380 nM, RE-DEAC-OXM EC 50 = 1.3 µM. Data were normalized to the response produced by DAMGO (1 µM) and are expressed as mean ± SEM (n=5-10 wells per concentration).

    Techniques Used: High Performance Liquid Chromatography, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Molecular Weight, Produced, Concentration Assay

    (A) Agonist dose-response curves at the mu opioid receptor (MOR) for PhOX and OXM using the GloSensor™ assay of cAMP signaling in HEK293T cells. The solid line depicts the best-fit sigmoidal function used to derive the indicated EC 50 value. OXM EC 50 = 1.4 nM. Data were normalized to the response produced by DAMGO (1 µM) and are expressed as mean ± SEM (n=5 wells per concentration). (B) Antagonist dose-response curves at the MOR for NLX and PhNX in the presence of DAMGO (100 nM) using the GloSensor™ assay. Data are presented as in A. NLX IC 50 = 86 nM. (C) Agonist dose-response curves at the MOR for DAMGO in the absence and presence of NLX (100 nM) or PhOX (300 nM) using the GloSensor™ assay. Data are presented as in A. DAMGO EC 50 = 0.7 nM, DAMGO + PhOX EC 50 = 0.9 nM, DAMGO + NLX EC 50 = 32 nM. (D) Agonist dose-response curves at the MOR for DAMGO and PhOX using a NanoBiT-based luminescence complementation assay of β-arrestin signaling in HEK293T cells (n=4 wells per concentration). DAMGO EC 50 = 11 nM. Data were normalized to the maximal response to DAMGO (10 µM) and are expressed as the mean ± SEM.
    Figure Legend Snippet: (A) Agonist dose-response curves at the mu opioid receptor (MOR) for PhOX and OXM using the GloSensor™ assay of cAMP signaling in HEK293T cells. The solid line depicts the best-fit sigmoidal function used to derive the indicated EC 50 value. OXM EC 50 = 1.4 nM. Data were normalized to the response produced by DAMGO (1 µM) and are expressed as mean ± SEM (n=5 wells per concentration). (B) Antagonist dose-response curves at the MOR for NLX and PhNX in the presence of DAMGO (100 nM) using the GloSensor™ assay. Data are presented as in A. NLX IC 50 = 86 nM. (C) Agonist dose-response curves at the MOR for DAMGO in the absence and presence of NLX (100 nM) or PhOX (300 nM) using the GloSensor™ assay. Data are presented as in A. DAMGO EC 50 = 0.7 nM, DAMGO + PhOX EC 50 = 0.9 nM, DAMGO + NLX EC 50 = 32 nM. (D) Agonist dose-response curves at the MOR for DAMGO and PhOX using a NanoBiT-based luminescence complementation assay of β-arrestin signaling in HEK293T cells (n=4 wells per concentration). DAMGO EC 50 = 11 nM. Data were normalized to the maximal response to DAMGO (10 µM) and are expressed as the mean ± SEM.

    Techniques Used: Produced, Concentration Assay



    Similar Products

    ssf-mor plasmid glosensor 22f  (Promega)
    90
    Promega ssf-mor plasmid glosensor 22f
    (A) Reaction scheme depicting the one-step alkylation procedure used to synthesize DEAC-OXM from commercially available oxymorphone ( 2 ) and DEAC-Br, as well as its photochemical conversion to the proposed primary reaction product “rearranged DEAC-OXM” (RE-DEAC-OXM), which likely occurs via a 1,4-Photo-Claisen rearrangement. (B) High pressure liquid chromatography (HPLC) chromatograms measured at 220 nm indicating predominant photoconversion of DEAC-OXM to RE-DEAC-OXM, which has a similar retention time, along with a much smaller amount of OXM in PBS (pH 7.2). (C) (Top) LC-MS (mass spectrometry) chromatogram of the reaction mixture shown in B. (Bottom) MS traces revealing that RE-DEAC-OXM has the same molecular weight as DEAC-OXM (531 Da). (D) Agonist dose-response curves at the MOR for DEAC-OXM, RE-DEAC-OXM, and OXM using the <t>GloSensor™</t> assay of cAMP signaling in HEK293T cells. The solid line depicts the best-fit sigmoidal function used to derive the indicated EC 50 value. OXM EC 50 = 1.3 nM, DEAC-OXM EC 50 = 380 nM, RE-DEAC-OXM EC 50 = 1.3 µM. Data were normalized to the response produced by DAMGO (1 µM) and are expressed as mean ± SEM (n=5-10 wells per concentration).
    Ssf Mor Plasmid Glosensor 22f, supplied by Promega, 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/ssf-mor plasmid glosensor 22f/product/Promega
    Average 90 stars, based on 1 article reviews
    ssf-mor plasmid glosensor 22f - by Bioz Stars, 2026-05
    90/100 stars
    		  Buy from Supplier

    Image Search Results


    (A) Reaction scheme depicting the one-step alkylation procedure used to synthesize DEAC-OXM from commercially available oxymorphone ( 2 ) and DEAC-Br, as well as its photochemical conversion to the proposed primary reaction product “rearranged DEAC-OXM” (RE-DEAC-OXM), which likely occurs via a 1,4-Photo-Claisen rearrangement. (B) High pressure liquid chromatography (HPLC) chromatograms measured at 220 nm indicating predominant photoconversion of DEAC-OXM to RE-DEAC-OXM, which has a similar retention time, along with a much smaller amount of OXM in PBS (pH 7.2). (C) (Top) LC-MS (mass spectrometry) chromatogram of the reaction mixture shown in B. (Bottom) MS traces revealing that RE-DEAC-OXM has the same molecular weight as DEAC-OXM (531 Da). (D) Agonist dose-response curves at the MOR for DEAC-OXM, RE-DEAC-OXM, and OXM using the GloSensor™ assay of cAMP signaling in HEK293T cells. The solid line depicts the best-fit sigmoidal function used to derive the indicated EC 50 value. OXM EC 50 = 1.3 nM, DEAC-OXM EC 50 = 380 nM, RE-DEAC-OXM EC 50 = 1.3 µM. Data were normalized to the response produced by DAMGO (1 µM) and are expressed as mean ± SEM (n=5-10 wells per concentration).

    Journal: bioRxiv

    Article Title: In vivo photopharmacology with light-activated opioid drugs

    doi: 10.1101/2023.02.02.526901

    Figure Lengend Snippet: (A) Reaction scheme depicting the one-step alkylation procedure used to synthesize DEAC-OXM from commercially available oxymorphone ( 2 ) and DEAC-Br, as well as its photochemical conversion to the proposed primary reaction product “rearranged DEAC-OXM” (RE-DEAC-OXM), which likely occurs via a 1,4-Photo-Claisen rearrangement. (B) High pressure liquid chromatography (HPLC) chromatograms measured at 220 nm indicating predominant photoconversion of DEAC-OXM to RE-DEAC-OXM, which has a similar retention time, along with a much smaller amount of OXM in PBS (pH 7.2). (C) (Top) LC-MS (mass spectrometry) chromatogram of the reaction mixture shown in B. (Bottom) MS traces revealing that RE-DEAC-OXM has the same molecular weight as DEAC-OXM (531 Da). (D) Agonist dose-response curves at the MOR for DEAC-OXM, RE-DEAC-OXM, and OXM using the GloSensor™ assay of cAMP signaling in HEK293T cells. The solid line depicts the best-fit sigmoidal function used to derive the indicated EC 50 value. OXM EC 50 = 1.3 nM, DEAC-OXM EC 50 = 380 nM, RE-DEAC-OXM EC 50 = 1.3 µM. Data were normalized to the response produced by DAMGO (1 µM) and are expressed as mean ± SEM (n=5-10 wells per concentration).

    Article Snippet: Then the SSF-MOR plasmid, GloSensor (Promega) 22F cAMP dependent reporter plasmid (Promega), and Lipofectamine 2000 (Invitrogen) in Opti-MEM were added.

    Techniques: High Performance Liquid Chromatography, Liquid Chromatography with Mass Spectroscopy, Mass Spectrometry, Molecular Weight, Produced, Concentration Assay

    (A) Agonist dose-response curves at the mu opioid receptor (MOR) for PhOX and OXM using the GloSensor™ assay of cAMP signaling in HEK293T cells. The solid line depicts the best-fit sigmoidal function used to derive the indicated EC 50 value. OXM EC 50 = 1.4 nM. Data were normalized to the response produced by DAMGO (1 µM) and are expressed as mean ± SEM (n=5 wells per concentration). (B) Antagonist dose-response curves at the MOR for NLX and PhNX in the presence of DAMGO (100 nM) using the GloSensor™ assay. Data are presented as in A. NLX IC 50 = 86 nM. (C) Agonist dose-response curves at the MOR for DAMGO in the absence and presence of NLX (100 nM) or PhOX (300 nM) using the GloSensor™ assay. Data are presented as in A. DAMGO EC 50 = 0.7 nM, DAMGO + PhOX EC 50 = 0.9 nM, DAMGO + NLX EC 50 = 32 nM. (D) Agonist dose-response curves at the MOR for DAMGO and PhOX using a NanoBiT-based luminescence complementation assay of β-arrestin signaling in HEK293T cells (n=4 wells per concentration). DAMGO EC 50 = 11 nM. Data were normalized to the maximal response to DAMGO (10 µM) and are expressed as the mean ± SEM.

    Journal: bioRxiv

    Article Title: In vivo photopharmacology with light-activated opioid drugs

    doi: 10.1101/2023.02.02.526901

    Figure Lengend Snippet: (A) Agonist dose-response curves at the mu opioid receptor (MOR) for PhOX and OXM using the GloSensor™ assay of cAMP signaling in HEK293T cells. The solid line depicts the best-fit sigmoidal function used to derive the indicated EC 50 value. OXM EC 50 = 1.4 nM. Data were normalized to the response produced by DAMGO (1 µM) and are expressed as mean ± SEM (n=5 wells per concentration). (B) Antagonist dose-response curves at the MOR for NLX and PhNX in the presence of DAMGO (100 nM) using the GloSensor™ assay. Data are presented as in A. NLX IC 50 = 86 nM. (C) Agonist dose-response curves at the MOR for DAMGO in the absence and presence of NLX (100 nM) or PhOX (300 nM) using the GloSensor™ assay. Data are presented as in A. DAMGO EC 50 = 0.7 nM, DAMGO + PhOX EC 50 = 0.9 nM, DAMGO + NLX EC 50 = 32 nM. (D) Agonist dose-response curves at the MOR for DAMGO and PhOX using a NanoBiT-based luminescence complementation assay of β-arrestin signaling in HEK293T cells (n=4 wells per concentration). DAMGO EC 50 = 11 nM. Data were normalized to the maximal response to DAMGO (10 µM) and are expressed as the mean ± SEM.

    Article Snippet: Then the SSF-MOR plasmid, GloSensor (Promega) 22F cAMP dependent reporter plasmid (Promega), and Lipofectamine 2000 (Invitrogen) in Opti-MEM were added.

    Techniques: Produced, Concentration Assay