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rabbit anti usp22  (Santa Cruz Biotechnology)


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    Structured Review

    Santa Cruz Biotechnology rabbit anti usp22
    Rabbit Anti Usp22, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 93/100, based on 32 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/rabbit+anti+usp22/USP22+Antibody/pm33994359-61-43-53
    Average 93 stars, based on 32 article reviews
    rabbit anti usp22 - by Bioz Stars, 2026-09
    93/100 stars

    Images

    Related Articles

    Immunofluorescence:

    Article Title: Usp22 is expressed in mouse uterus during early pregnancy and involved in endometrial stromal cell decidualization.
    Article Snippet: .. Immunofluorescence was conducted using cells that had been fixed on coverslips for 20 min with 4% PFA, and that had then been washed with PBS, permeabilized for 10 min with Triton X-100-PBS, blocked with 0.5% bovine serum albumin, incubated overnight with primary antibodies: Rabbit anti-USP22 (1:100 for IHC or 1:200 for IF; sc-390585, Santa Cruz Biotechnology, USA), anti-Vimentin (1:200; sc-6260, Santa Cruz Biotechnology, USA), and cytokeratin (1:200; DAKO) at 4 ◦C, then probed with appropriate secondary antibodies (1:200; Jackson Immuno Research, USA) for 2 h, and stained using 4′,6-diamidino-2-phenylindole (DAPI) dye (0.1 μg/ml, Sigma) for 10 min. ..

    Incubation:

    Article Title: Usp22 is expressed in mouse uterus during early pregnancy and involved in endometrial stromal cell decidualization.
    Article Snippet: .. Immunofluorescence was conducted using cells that had been fixed on coverslips for 20 min with 4% PFA, and that had then been washed with PBS, permeabilized for 10 min with Triton X-100-PBS, blocked with 0.5% bovine serum albumin, incubated overnight with primary antibodies: Rabbit anti-USP22 (1:100 for IHC or 1:200 for IF; sc-390585, Santa Cruz Biotechnology, USA), anti-Vimentin (1:200; sc-6260, Santa Cruz Biotechnology, USA), and cytokeratin (1:200; DAKO) at 4 ◦C, then probed with appropriate secondary antibodies (1:200; Jackson Immuno Research, USA) for 2 h, and stained using 4′,6-diamidino-2-phenylindole (DAPI) dye (0.1 μg/ml, Sigma) for 10 min. ..

    Immunohistochemistry:

    Article Title: Usp22 is expressed in mouse uterus during early pregnancy and involved in endometrial stromal cell decidualization.
    Article Snippet: .. Immunofluorescence was conducted using cells that had been fixed on coverslips for 20 min with 4% PFA, and that had then been washed with PBS, permeabilized for 10 min with Triton X-100-PBS, blocked with 0.5% bovine serum albumin, incubated overnight with primary antibodies: Rabbit anti-USP22 (1:100 for IHC or 1:200 for IF; sc-390585, Santa Cruz Biotechnology, USA), anti-Vimentin (1:200; sc-6260, Santa Cruz Biotechnology, USA), and cytokeratin (1:200; DAKO) at 4 ◦C, then probed with appropriate secondary antibodies (1:200; Jackson Immuno Research, USA) for 2 h, and stained using 4′,6-diamidino-2-phenylindole (DAPI) dye (0.1 μg/ml, Sigma) for 10 min. ..

    Staining:

    Article Title: Usp22 is expressed in mouse uterus during early pregnancy and involved in endometrial stromal cell decidualization.
    Article Snippet: .. Immunofluorescence was conducted using cells that had been fixed on coverslips for 20 min with 4% PFA, and that had then been washed with PBS, permeabilized for 10 min with Triton X-100-PBS, blocked with 0.5% bovine serum albumin, incubated overnight with primary antibodies: Rabbit anti-USP22 (1:100 for IHC or 1:200 for IF; sc-390585, Santa Cruz Biotechnology, USA), anti-Vimentin (1:200; sc-6260, Santa Cruz Biotechnology, USA), and cytokeratin (1:200; DAKO) at 4 ◦C, then probed with appropriate secondary antibodies (1:200; Jackson Immuno Research, USA) for 2 h, and stained using 4′,6-diamidino-2-phenylindole (DAPI) dye (0.1 μg/ml, Sigma) for 10 min. ..



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    A Western blot analysis of basal PML and <t>USP22</t> expression in control (non-human target; n.h.t) and USP22 knockout (KO) HT-29 cells. The major (120 kDa) PML isoform is indicated with a red arrow. Vinculin served as loading control. Representative blots of at least two different independent experiments are shown. B Densitometric quantification of gray level intensities of the major (120 kDa) PML isoform (indicated with red arrow) detected by Western blot analysis of PML in n.h.t and USP22 KO HT-29 cells from ( A ), normalized against loading control intensities. Mean and SEM of three independent experiments are shown. C Basal mRNA expression levels of all PML isoforms in n.h.t and USP22 KO HT-29 cells using qRT-PCR. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to n.h.t. Mean and SEM of three independent experiments are shown. D Western blot analysis of n.h.t and USP22 KO HEK293T cells transiently transfected with plasmids expressing PML-HA isoform IV and mCherry, prior to treatment with 20 μg/ml cycloheximide (CHX) for the indicated timepoints. β-Actin served as loading control. Representative blots of at least three different independent experiments are shown. E Densitometric quantification of gray level intensities of PML-HA isoform IV detected by Western blot analysis of HA in n.h.t and USP22 KO HEK293T cells in the presence of CHX for the indicated timepoints, normalized against loading control intensities. Mean and SEM of three independent biological replicates are shown.
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    A Western blot analysis of basal PML and <t>USP22</t> expression in control (non-human target; n.h.t) and USP22 knockout (KO) HT-29 cells. The major (120 kDa) PML isoform is indicated with a red arrow. Vinculin served as loading control. Representative blots of at least two different independent experiments are shown. B Densitometric quantification of gray level intensities of the major (120 kDa) PML isoform (indicated with red arrow) detected by Western blot analysis of PML in n.h.t and USP22 KO HT-29 cells from ( A ), normalized against loading control intensities. Mean and SEM of three independent experiments are shown. C Basal mRNA expression levels of all PML isoforms in n.h.t and USP22 KO HT-29 cells using qRT-PCR. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to n.h.t. Mean and SEM of three independent experiments are shown. D Western blot analysis of n.h.t and USP22 KO HEK293T cells transiently transfected with plasmids expressing PML-HA isoform IV and mCherry, prior to treatment with 20 μg/ml cycloheximide (CHX) for the indicated timepoints. β-Actin served as loading control. Representative blots of at least three different independent experiments are shown. E Densitometric quantification of gray level intensities of PML-HA isoform IV detected by Western blot analysis of HA in n.h.t and USP22 KO HEK293T cells in the presence of CHX for the indicated timepoints, normalized against loading control intensities. Mean and SEM of three independent biological replicates are shown.
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    A Western blot analysis of basal PML and <t>USP22</t> expression in control (non-human target; n.h.t) and USP22 knockout (KO) HT-29 cells. The major (120 kDa) PML isoform is indicated with a red arrow. Vinculin served as loading control. Representative blots of at least two different independent experiments are shown. B Densitometric quantification of gray level intensities of the major (120 kDa) PML isoform (indicated with red arrow) detected by Western blot analysis of PML in n.h.t and USP22 KO HT-29 cells from ( A ), normalized against loading control intensities. Mean and SEM of three independent experiments are shown. C Basal mRNA expression levels of all PML isoforms in n.h.t and USP22 KO HT-29 cells using qRT-PCR. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to n.h.t. Mean and SEM of three independent experiments are shown. D Western blot analysis of n.h.t and USP22 KO HEK293T cells transiently transfected with plasmids expressing PML-HA isoform IV and mCherry, prior to treatment with 20 μg/ml cycloheximide (CHX) for the indicated timepoints. β-Actin served as loading control. Representative blots of at least three different independent experiments are shown. E Densitometric quantification of gray level intensities of PML-HA isoform IV detected by Western blot analysis of HA in n.h.t and USP22 KO HEK293T cells in the presence of CHX for the indicated timepoints, normalized against loading control intensities. Mean and SEM of three independent biological replicates are shown.
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    A Western blot analysis of basal PML and <t>USP22</t> expression in control (non-human target; n.h.t) and USP22 knockout (KO) HT-29 cells. The major (120 kDa) PML isoform is indicated with a red arrow. Vinculin served as loading control. Representative blots of at least two different independent experiments are shown. B Densitometric quantification of gray level intensities of the major (120 kDa) PML isoform (indicated with red arrow) detected by Western blot analysis of PML in n.h.t and USP22 KO HT-29 cells from ( A ), normalized against loading control intensities. Mean and SEM of three independent experiments are shown. C Basal mRNA expression levels of all PML isoforms in n.h.t and USP22 KO HT-29 cells using qRT-PCR. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to n.h.t. Mean and SEM of three independent experiments are shown. D Western blot analysis of n.h.t and USP22 KO HEK293T cells transiently transfected with plasmids expressing PML-HA isoform IV and mCherry, prior to treatment with 20 μg/ml cycloheximide (CHX) for the indicated timepoints. β-Actin served as loading control. Representative blots of at least three different independent experiments are shown. E Densitometric quantification of gray level intensities of PML-HA isoform IV detected by Western blot analysis of HA in n.h.t and USP22 KO HEK293T cells in the presence of CHX for the indicated timepoints, normalized against loading control intensities. Mean and SEM of three independent biological replicates are shown.
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    Image Search Results


    A Western blot analysis of basal PML and USP22 expression in control (non-human target; n.h.t) and USP22 knockout (KO) HT-29 cells. The major (120 kDa) PML isoform is indicated with a red arrow. Vinculin served as loading control. Representative blots of at least two different independent experiments are shown. B Densitometric quantification of gray level intensities of the major (120 kDa) PML isoform (indicated with red arrow) detected by Western blot analysis of PML in n.h.t and USP22 KO HT-29 cells from ( A ), normalized against loading control intensities. Mean and SEM of three independent experiments are shown. C Basal mRNA expression levels of all PML isoforms in n.h.t and USP22 KO HT-29 cells using qRT-PCR. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to n.h.t. Mean and SEM of three independent experiments are shown. D Western blot analysis of n.h.t and USP22 KO HEK293T cells transiently transfected with plasmids expressing PML-HA isoform IV and mCherry, prior to treatment with 20 μg/ml cycloheximide (CHX) for the indicated timepoints. β-Actin served as loading control. Representative blots of at least three different independent experiments are shown. E Densitometric quantification of gray level intensities of PML-HA isoform IV detected by Western blot analysis of HA in n.h.t and USP22 KO HEK293T cells in the presence of CHX for the indicated timepoints, normalized against loading control intensities. Mean and SEM of three independent biological replicates are shown.

    Journal: Cell Death Discovery

    Article Title: USP22 regulates APL differentiation via PML-RARα stabilization and IFN repression

    doi: 10.1038/s41420-024-01894-8

    Figure Lengend Snippet: A Western blot analysis of basal PML and USP22 expression in control (non-human target; n.h.t) and USP22 knockout (KO) HT-29 cells. The major (120 kDa) PML isoform is indicated with a red arrow. Vinculin served as loading control. Representative blots of at least two different independent experiments are shown. B Densitometric quantification of gray level intensities of the major (120 kDa) PML isoform (indicated with red arrow) detected by Western blot analysis of PML in n.h.t and USP22 KO HT-29 cells from ( A ), normalized against loading control intensities. Mean and SEM of three independent experiments are shown. C Basal mRNA expression levels of all PML isoforms in n.h.t and USP22 KO HT-29 cells using qRT-PCR. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to n.h.t. Mean and SEM of three independent experiments are shown. D Western blot analysis of n.h.t and USP22 KO HEK293T cells transiently transfected with plasmids expressing PML-HA isoform IV and mCherry, prior to treatment with 20 μg/ml cycloheximide (CHX) for the indicated timepoints. β-Actin served as loading control. Representative blots of at least three different independent experiments are shown. E Densitometric quantification of gray level intensities of PML-HA isoform IV detected by Western blot analysis of HA in n.h.t and USP22 KO HEK293T cells in the presence of CHX for the indicated timepoints, normalized against loading control intensities. Mean and SEM of three independent biological replicates are shown.

    Article Snippet: The following primary antibodies were used in this study: rabbit-anti-PML (ab179466, Abcam), rabbit-anti-USP22 (ab195298, Abcam), mouse-anti-β-ACTIN (A5441, Sigma-Aldrich), mouse-anti-GAPDH (5G4-6C5, HyTest, Ltd., Turku, Finland), mouse-anti-HA (F-7) (sc-7392x, Santa Cruz Biotechnology), mouse-anti-Vinculin (V9131, SIGMA-Aldrich), rabbit-anti-GFP (632592, Clontech), rabbit-anti-RFP (ab62341, Abcam), rabbit-anti-RARα (62294 S, Cell Signaling), rabbit-anti-His-tag (sc-53073, Santa Cruz Biotechnology), mouse-anti-ubiquitin (P4D1) (sc-8017, Santa Cruz Biotechnology).

    Techniques: Western Blot, Expressing, Knock-Out, Quantitative RT-PCR, Transfection

    A Western blot analysis of basal PML-RARα and USP22 expression in wild-type (wt), control (non-human target; n.h.t) and USP22 knockout (KO) NB4 acute promyelocytic leukemia (APL) cells. β-Actin served as loading control. Representative blots of at least two different independent experiments are shown. B Densitometric quantification of gray level intensities of the major (130 kDa) PML-RARα isoform detected by Western blot analysis in wt, n.h.t and USP22 KO NB4 APL cells, normalized against loading control intensities. Mean and SEM of three independent experiments are shown. C Basal mRNA expression levels of the PML-RARα long isoform in wt, n.h.t. and USP22 KO NB4 APL cells using qRT-PCR. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to n.h.t. Mean and SEM of three independent experiments are shown. D Western blot analysis of wt, n.h.t and USP22 KO NB4 APL cells treated with 20 μg/ml CHX for the indicated timepoints. GAPDH served as loading control. Representative blots of at least two different independent experiments are shown. Red dashed line indicates protein stability at 50% compared to untreated controls. E Densitometric quantification of gray level intensities of the major (130 kDa) PML-RARα isoform detected by Western blot analysis in wt, n.h.t and USP22 KO NB4 APL cells treated with 20 μg/ml CHX for the indicated timepoints, normalized against loading control intensities. Mean and SEM of three independent experiments are shown. F Western blot analysis of n.h.t and USP22 KO HEK293T cells, transiently transfected with plasmids encoding the long isoform of PML-RARα and treated with 20 μg/ml CHX for the indicated timepoints. Co-transfection with GFP plasmid served as transfection control. GAPDH served as loading control. Representative blots of at least two different independent experiments are shown. Red dashed line indicates protein stability at 50% compared to untreated controls. G Densitometric quantification of gray level intensities of the long isoform of PML-RARα transiently transfected in n.h.t and USP22 KO HEK293T cells treated with 20 μg/ml CHX for the indicated timepoints, normalized against loading control intensities. Mean and SEM of three independent experiments are shown. H Western blot analysis of HEK293T cells, transiently transfected with plasmids encoding the long isoform of wt (PML-RARα) and K394R (KR) PML-RARα (PML-K394R-RARα) and treated with 20 μg/ml CHX for the indicated timepoints. Co-transfection with GFP plasmid served as transfection control. GAPDH served as loading control. Representative blots of at least two different independent experiments are shown. Red dashed line indicates protein stability at 50% compared to untreated controls. I Densitometric quantification of gray level intensities of the long isoform of wt (PML-RARα) and K394R (KR) PML-RARα (PML-K394R-RARα) transiently transfected in HEK293T cells treated with 20 μg/ml CHX for the indicated timepoints, normalized against loading control intensities. Mean and SEM of three independent experiments are shown.

    Journal: Cell Death Discovery

    Article Title: USP22 regulates APL differentiation via PML-RARα stabilization and IFN repression

    doi: 10.1038/s41420-024-01894-8

    Figure Lengend Snippet: A Western blot analysis of basal PML-RARα and USP22 expression in wild-type (wt), control (non-human target; n.h.t) and USP22 knockout (KO) NB4 acute promyelocytic leukemia (APL) cells. β-Actin served as loading control. Representative blots of at least two different independent experiments are shown. B Densitometric quantification of gray level intensities of the major (130 kDa) PML-RARα isoform detected by Western blot analysis in wt, n.h.t and USP22 KO NB4 APL cells, normalized against loading control intensities. Mean and SEM of three independent experiments are shown. C Basal mRNA expression levels of the PML-RARα long isoform in wt, n.h.t. and USP22 KO NB4 APL cells using qRT-PCR. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to n.h.t. Mean and SEM of three independent experiments are shown. D Western blot analysis of wt, n.h.t and USP22 KO NB4 APL cells treated with 20 μg/ml CHX for the indicated timepoints. GAPDH served as loading control. Representative blots of at least two different independent experiments are shown. Red dashed line indicates protein stability at 50% compared to untreated controls. E Densitometric quantification of gray level intensities of the major (130 kDa) PML-RARα isoform detected by Western blot analysis in wt, n.h.t and USP22 KO NB4 APL cells treated with 20 μg/ml CHX for the indicated timepoints, normalized against loading control intensities. Mean and SEM of three independent experiments are shown. F Western blot analysis of n.h.t and USP22 KO HEK293T cells, transiently transfected with plasmids encoding the long isoform of PML-RARα and treated with 20 μg/ml CHX for the indicated timepoints. Co-transfection with GFP plasmid served as transfection control. GAPDH served as loading control. Representative blots of at least two different independent experiments are shown. Red dashed line indicates protein stability at 50% compared to untreated controls. G Densitometric quantification of gray level intensities of the long isoform of PML-RARα transiently transfected in n.h.t and USP22 KO HEK293T cells treated with 20 μg/ml CHX for the indicated timepoints, normalized against loading control intensities. Mean and SEM of three independent experiments are shown. H Western blot analysis of HEK293T cells, transiently transfected with plasmids encoding the long isoform of wt (PML-RARα) and K394R (KR) PML-RARα (PML-K394R-RARα) and treated with 20 μg/ml CHX for the indicated timepoints. Co-transfection with GFP plasmid served as transfection control. GAPDH served as loading control. Representative blots of at least two different independent experiments are shown. Red dashed line indicates protein stability at 50% compared to untreated controls. I Densitometric quantification of gray level intensities of the long isoform of wt (PML-RARα) and K394R (KR) PML-RARα (PML-K394R-RARα) transiently transfected in HEK293T cells treated with 20 μg/ml CHX for the indicated timepoints, normalized against loading control intensities. Mean and SEM of three independent experiments are shown.

    Article Snippet: The following primary antibodies were used in this study: rabbit-anti-PML (ab179466, Abcam), rabbit-anti-USP22 (ab195298, Abcam), mouse-anti-β-ACTIN (A5441, Sigma-Aldrich), mouse-anti-GAPDH (5G4-6C5, HyTest, Ltd., Turku, Finland), mouse-anti-HA (F-7) (sc-7392x, Santa Cruz Biotechnology), mouse-anti-Vinculin (V9131, SIGMA-Aldrich), rabbit-anti-GFP (632592, Clontech), rabbit-anti-RFP (ab62341, Abcam), rabbit-anti-RARα (62294 S, Cell Signaling), rabbit-anti-His-tag (sc-53073, Santa Cruz Biotechnology), mouse-anti-ubiquitin (P4D1) (sc-8017, Santa Cruz Biotechnology).

    Techniques: Western Blot, Expressing, Knock-Out, Quantitative RT-PCR, Transfection, Cotransfection, Plasmid Preparation

    A Western blot analysis of RARα and USP22 in wild-type (wt), control (non-human target; n.h.t) and USP22 knockout (KO) NB4 APL cells treated with the indicated concentrations of all- trans retinoic acid (ATRA) for 120 h. β-actin served as loading control. Representative blots of at least two different independent experiments are shown. B Basal and ATRA-induced mRNA expression levels of PML-RARα in wt, n.h.t and USP22 KO NB4 APL cells incubated with the indicated ATRA concentrations for 120 h using qRT-PCR. UT, untreated. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to UT of wt NB4 cells Mean and SEM of three independent biological replicates are shown. C FACS analysis of wt, n.h.t., and USP22 KO NB4 APL cells incubated with the indicated ATRA concentrations for 120 h. Shown is the cell count per fluorescence intensity of PE-labeled CD11b. D Mean fluorescence intensities (MFIs) of CD11b-PE signals on wt, n.h.t., and USP22 KO NB4 APL cells incubated with the indicated ATRA concentrations for 120 h. UT, untreated. Mean and SEM of four independent biological replicates are shown. E Basal and ATRA-induced mRNA expression levels of CD11b in wt, n.h.t and USP22 KO NB4 APL cells incubated with the indicated ATRA concentrations for for 120 h using qRT-PCR. UT, untreated. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to UT of wt NB4 cells Mean and SEM of three independent biological replicates are shown.

    Journal: Cell Death Discovery

    Article Title: USP22 regulates APL differentiation via PML-RARα stabilization and IFN repression

    doi: 10.1038/s41420-024-01894-8

    Figure Lengend Snippet: A Western blot analysis of RARα and USP22 in wild-type (wt), control (non-human target; n.h.t) and USP22 knockout (KO) NB4 APL cells treated with the indicated concentrations of all- trans retinoic acid (ATRA) for 120 h. β-actin served as loading control. Representative blots of at least two different independent experiments are shown. B Basal and ATRA-induced mRNA expression levels of PML-RARα in wt, n.h.t and USP22 KO NB4 APL cells incubated with the indicated ATRA concentrations for 120 h using qRT-PCR. UT, untreated. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to UT of wt NB4 cells Mean and SEM of three independent biological replicates are shown. C FACS analysis of wt, n.h.t., and USP22 KO NB4 APL cells incubated with the indicated ATRA concentrations for 120 h. Shown is the cell count per fluorescence intensity of PE-labeled CD11b. D Mean fluorescence intensities (MFIs) of CD11b-PE signals on wt, n.h.t., and USP22 KO NB4 APL cells incubated with the indicated ATRA concentrations for 120 h. UT, untreated. Mean and SEM of four independent biological replicates are shown. E Basal and ATRA-induced mRNA expression levels of CD11b in wt, n.h.t and USP22 KO NB4 APL cells incubated with the indicated ATRA concentrations for for 120 h using qRT-PCR. UT, untreated. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to UT of wt NB4 cells Mean and SEM of three independent biological replicates are shown.

    Article Snippet: The following primary antibodies were used in this study: rabbit-anti-PML (ab179466, Abcam), rabbit-anti-USP22 (ab195298, Abcam), mouse-anti-β-ACTIN (A5441, Sigma-Aldrich), mouse-anti-GAPDH (5G4-6C5, HyTest, Ltd., Turku, Finland), mouse-anti-HA (F-7) (sc-7392x, Santa Cruz Biotechnology), mouse-anti-Vinculin (V9131, SIGMA-Aldrich), rabbit-anti-GFP (632592, Clontech), rabbit-anti-RFP (ab62341, Abcam), rabbit-anti-RARα (62294 S, Cell Signaling), rabbit-anti-His-tag (sc-53073, Santa Cruz Biotechnology), mouse-anti-ubiquitin (P4D1) (sc-8017, Santa Cruz Biotechnology).

    Techniques: Western Blot, Knock-Out, Expressing, Incubation, Quantitative RT-PCR, Cell Counting, Fluorescence, Labeling

    A Basal and ATRA-induced mRNA expression levels of IRF1 in wild-type (wt), control (non-human target; n.h.t) and USP22 knockout (KO) NB4 APL cells incubated with the indicated ATRA concentrations for 120 h using qRT-PCR. UT, untreated. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to UT of wt NB4 cells. Mean and SEM of three independent biological replicates are shown. B Basal mRNA expression levels of USP22 and the indicated ISGs in n.h.t and USP22 KO NB4 APL cells using qRT-PCR. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to n.h.t. Mean and SEM of three independent biological replicates are shown. C Model of USP22-mediated effects on PML-RARα and IFN signaling in APL.

    Journal: Cell Death Discovery

    Article Title: USP22 regulates APL differentiation via PML-RARα stabilization and IFN repression

    doi: 10.1038/s41420-024-01894-8

    Figure Lengend Snippet: A Basal and ATRA-induced mRNA expression levels of IRF1 in wild-type (wt), control (non-human target; n.h.t) and USP22 knockout (KO) NB4 APL cells incubated with the indicated ATRA concentrations for 120 h using qRT-PCR. UT, untreated. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to UT of wt NB4 cells. Mean and SEM of three independent biological replicates are shown. B Basal mRNA expression levels of USP22 and the indicated ISGs in n.h.t and USP22 KO NB4 APL cells using qRT-PCR. Gene expression was normalized against 28S mRNA and is presented as x-fold mRNA expression compared to n.h.t. Mean and SEM of three independent biological replicates are shown. C Model of USP22-mediated effects on PML-RARα and IFN signaling in APL.

    Article Snippet: The following primary antibodies were used in this study: rabbit-anti-PML (ab179466, Abcam), rabbit-anti-USP22 (ab195298, Abcam), mouse-anti-β-ACTIN (A5441, Sigma-Aldrich), mouse-anti-GAPDH (5G4-6C5, HyTest, Ltd., Turku, Finland), mouse-anti-HA (F-7) (sc-7392x, Santa Cruz Biotechnology), mouse-anti-Vinculin (V9131, SIGMA-Aldrich), rabbit-anti-GFP (632592, Clontech), rabbit-anti-RFP (ab62341, Abcam), rabbit-anti-RARα (62294 S, Cell Signaling), rabbit-anti-His-tag (sc-53073, Santa Cruz Biotechnology), mouse-anti-ubiquitin (P4D1) (sc-8017, Santa Cruz Biotechnology).

    Techniques: Expressing, Knock-Out, Incubation, Quantitative RT-PCR