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Novus Biologicals rabbit polyclonal anti usp1 antibody

Figure 1. Expression level of <t>USP1,</t> USP4, USP10, USP14, USP22, USP25, and GSA7 mRNA in glioma cell line U87 (Vector) and its subline with a deficiency of both protein kinase and endoribonuclease of the signaling enzyme IRE-1α (dnIRE-1α) measured by qPCR. mRNA expressions values were normalized to beta-actin mRNA expression and presented as percent of control (vector, 100%); mean ± SEM; n = 4; * - P < 0,05 versus control; ** - P < 0,01 versus control.

Rabbit Polyclonal Anti Usp1 Antibody, supplied by Novus Biologicals, 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/product/rabbit+polyclonal+anti+usp1+antibody/USP1+Antibody/10__1515_slash_ersc___2016___0003-46-0-34
Average 90 stars, based on 1 article reviews

rabbit polyclonal anti usp1 antibody - by Bioz Stars, 2026-10

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1) Product Images from "IRE-1α regulates expression of ubiquitin specific peptidases during hypoxic response in U87 glioma cells"

Article Title: IRE-1α regulates expression of ubiquitin specific peptidases during hypoxic response in U87 glioma cells

Journal: Endoplasmic Reticulum Stress in Diseases

doi: 10.1515/ersc-2016-0003

Figure 1. Expression level of USP1, USP4, USP10, USP14, USP22, USP25, and GSA7 mRNA in glioma cell line U87 (Vector) and its subline with a deficiency of both protein kinase and endoribonuclease of the signaling enzyme IRE-1α (dnIRE-1α) measured by qPCR. mRNA expressions values were normalized to beta-actin mRNA expression and presented as percent of control (vector, 100%); mean ± SEM; n = 4; * - P < 0,05 versus control; ** - P < 0,01 versus control.

Figure Legend Snippet: Figure 1. Expression level of USP1, USP4, USP10, USP14, USP22, USP25, and GSA7 mRNA in glioma cell line U87 (Vector) and its subline with a deficiency of both protein kinase and endoribonuclease of the signaling enzyme IRE-1α (dnIRE-1α) measured by qPCR. mRNA expressions values were normalized to beta-actin mRNA expression and presented as percent of control (vector, 100%); mean ± SEM; n = 4; * - P < 0,05 versus control; ** - P < 0,01 versus control.

Techniques Used: Expressing, Plasmid Preparation, Control

Figure 2. Effect of hypoxia (3% oxygen – 16h) on the expression level of USP1 (A), USP4 (B), USP10 (C), USP14 (D), USP22 (E), USP25 (F), and GSA7/ATG7 (G) mRNA (by qPCR) in glioma cells with a deficiency of IRE-1α (dnIRE-1α). mRNA expressions values were normalized to beta- actin mRNA expression and presented as percent of control 1 (control glioma cells transfected by vector, 100%); mean ± SEM; n = 4.

Figure Legend Snippet: Figure 2. Effect of hypoxia (3% oxygen – 16h) on the expression level of USP1 (A), USP4 (B), USP10 (C), USP14 (D), USP22 (E), USP25 (F), and GSA7/ATG7 (G) mRNA (by qPCR) in glioma cells with a deficiency of IRE-1α (dnIRE-1α). mRNA expressions values were normalized to beta- actin mRNA expression and presented as percent of control 1 (control glioma cells transfected by vector, 100%); mean ± SEM; n = 4.

Techniques Used: Expressing, Control, Transfection, Plasmid Preparation

Figure 4. Comparative effect of hypoxia (3% oxygen – 16h) on the expression level of USP1, USP4, USP10, USP14, USP22, USP25, and GSA7 mRNA cells with a deficiency of IRE-1α (dnIRE-1α). mRNA expressions values were normalized to beta-actin mRNA expression and presented as percent of corresponding controls (vector as well as dnIRE-1α), 100%); mean ± SEM; n = 4.

Figure Legend Snippet: Figure 4. Comparative effect of hypoxia (3% oxygen – 16h) on the expression level of USP1, USP4, USP10, USP14, USP22, USP25, and GSA7 mRNA cells with a deficiency of IRE-1α (dnIRE-1α). mRNA expressions values were normalized to beta-actin mRNA expression and presented as percent of corresponding controls (vector as well as dnIRE-1α), 100%); mean ± SEM; n = 4.

Techniques Used: Expressing, Plasmid Preparation

Figure 3. Effect of hypoxia (3% oxygen – 16h) on protein level of USP1, USP14, and GSA7/ATG7 in glioma cells with a deficiency of IRE-1α (dnIRE-1α) measured by Western blot. ACTB protein level was used to ensure equal loading of the samples.

Figure Legend Snippet: Figure 3. Effect of hypoxia (3% oxygen – 16h) on protein level of USP1, USP14, and GSA7/ATG7 in glioma cells with a deficiency of IRE-1α (dnIRE-1α) measured by Western blot. ACTB protein level was used to ensure equal loading of the samples.

Techniques Used: Western Blot

Expressing:

Article Title: IRE-1α regulates expression of ubiquitin specific peptidases during hypoxic response in U87 glioma cells
Article Snippet: The glioma cell line U87 (HTB-14) was obtained from ATCC (USA) and grown in high glucose (4.5 g/l) Dulbecco’s modified Eagle’s minimum essential medium (DMEM; Gibco, Invitrogen, USA) supplemented with glutamine (2 mM), 10% fetal bovine serum (EquitechBio, Inc., USA), penicillin (100 units/ml; Gibco, USA) and streptomycin (0.1 mg/ml; Gibco) at 37oC in a 5% CO2 incubator.and grown in high glucose (4.5 g/l) Dulbecco’s modified Eagle’s minimum essential medium (DMEM; Gibco, Invitrogen, USA) supplemented with glutamine (2 mM), 10% fetal bovine serum (EquitechBio, Inc., USA), penicillin (100 units/ml; Gibco, USA) and streptomycin (0.1 mg/ml; Gibco) at 37oC in a 5% CO2 incubator. ... Rabbit polyclonal anti-USP1 antibody (ab108104), anti-USP14 antibody (ab137432), and anti-Apg7 antibody (ab53255) were from Abcam (UK), anti-ACTB (β-actin) antibodies were from Santa Cruz Biotechnology (Santa Cruz, USA) and rabbit polyclonal anti-HIF-1α antibody was from Novus Biologicals, USA.. Unauthenticated Download Date | 1/11/17 2:17 PM Cell lines.Unauthenticated Download Date | 1/11/17 2:17 PM Cell lines.

Plasmid Preparation:

Control:

Transfection:

Western Blot:

Image Search Results

Fig. 8 USP1 stabilizes RIG-I protein expression by inhibiting RIG-I ubiquitination

Journal: Cellular and molecular life sciences : CMLS

Article Title: USP1 inhibits influenza A and B virus replication in MDCK cells by mediating RIG-I deubiquitination.

doi: 10.1007/s00018-025-05733-6

Figure Lengend Snippet: Fig. 8 USP1 stabilizes RIG-I protein expression by inhibiting RIG-I ubiquitination

Article Snippet: RIPA lysis buffer (PC101), PMSF (GRF101), and a BCA Protein Quantitative Kit (ZJ101) were purchased from Shanghai Yamei Biomedical Technology Co., Ltd.; SDS-PAGE loading buffer, 5 × (P1040), and a WB gel making kit (A1010) were purchased from Beijing Solarbio Science & Technology Co., Ltd.; low molecular weight poly(I:C) is from InvivoGen Co., Ltd; PBS buffer, DMEM, 1640 medium were purchased from Cellmax Technology (Beijing) Co., Ltd; Newborn bovine serum/ fetal bovine serum were purchased from Lanzhou Minhai Bioengineering Co., Ltd; Canine IFN-α from Zhongkebaike Biotechnology Co., Ltd; Anti-flag murine monoclonal antibody (cat: T0003) was purchased from affinity; Anti IBV NP rabbit monoclonal antibody (cat: B017) was purchased from Abcam; Goat anti-mouse IgG (cat: SA00001-1)/ Goat anti-rabbit IgG (cat: SA00001-2)/anti USP1 mouse polyclonal antibody (cat: SA00013-3) were purchased from Proteintech; resist β-actin murine monoclonal antibody (cat:66,009) was purchased from CST.

Techniques: Expressing, Ubiquitin Proteomics

The E3 ligase Cdh1 interacts with and downregulates MAST1 protein. (A) HeLa cells were transfected with a panel of E3 ligases, and the expression of MAST1 protein was analyzed using Western blotting. (B) Interactions between endogenous and (C) exogenous Cdh1 and MAST1 proteins were analyzed in HeLa cells and HEK293 cells, respectively. Cell lysates were immunoprecipitated and immunoblotted with the indicated antibodies. Protein expression was checked using Western blotting. GAPDH was used as a loading control. (D) HeLa cells were subjected to the Duolink PLA assay to analyze the interaction between Cdh1 and MAST1 using specific antibodies. Scale bar: 10 µm. (E) Schematic representation of full length Cdh1 (1-496 aa) encoding WD40 domain (represented as Cdh1-WT), N-terminus Cdh1 (1-155 aa) lacking WD40 domain (represented as Cdh1-CTM1), and C-terminus Cdh1 (156-496 aa) encoding WD40 domain (represented as Cdh1-CTM2). Interactions between full length MAST1 and Cdh1 truncated mutants by co-immunoprecipitation and immunoblotting with the indicated antibodies (lower panel). (F) Schematic representation of full length MAST1 (1-1570 aa) encoding serine/threonine (S/T) kinase domain and PDZ domain (represented as MAST1-WT), N-terminus MAST1 (1-832 aa) encoding S/T kinase domain (represented as MAST1-MTM1), C-terminus MAST1 (833-1570 aa) encoding PDZ domain (represented as MAST1-MTM2), and C-terminus MAST1 (1118-1465 aa) lacking PDZ domain (represented as MAST1-MTM3). Interactions between full length Cdh1 and MAST1 truncated mutants by co-immunoprecipitation and immunoblotting with the indicated antibodies (lower panel). (G) The effect of Cdh1 on endogenous MAST1 protein was analyzed in HeLa cells transfected with increasing concentrations of Flag-Cdh1. (H) HeLa cells were transfected with sgRNA1 and sgRNA2 targeting Cdh1 to assess the endogenous protein levels of Cdh1 and MAST1 by Western blotting. (I) The Cdh1-mediated degradation of endogenous MAST1 protein was rescued in cells transfected with sgRNA targeting Cdh1 . (J) The ubiquitination of endogenous MAST1 was analyzed by transfecting HeLa cells with Flag-Cdh1 or sgRNA targeting Cdh1 followed by immunoprecipitation with an anti-MAST1 antibody and immunoblotting with an anti-ubiquitin antibody. Protein expression was checked by Western blotting with the indicated antibodies. GAPDH was used as a loading control.

Journal: Theranostics

Article Title: CRISPR/Cas9-based genome-wide screening for deubiquitinase subfamily identifies USP1 regulating MAST1-driven cisplatin-resistance in cancer cells

doi: 10.7150/thno.72826

Figure Lengend Snippet: The E3 ligase Cdh1 interacts with and downregulates MAST1 protein. (A) HeLa cells were transfected with a panel of E3 ligases, and the expression of MAST1 protein was analyzed using Western blotting. (B) Interactions between endogenous and (C) exogenous Cdh1 and MAST1 proteins were analyzed in HeLa cells and HEK293 cells, respectively. Cell lysates were immunoprecipitated and immunoblotted with the indicated antibodies. Protein expression was checked using Western blotting. GAPDH was used as a loading control. (D) HeLa cells were subjected to the Duolink PLA assay to analyze the interaction between Cdh1 and MAST1 using specific antibodies. Scale bar: 10 µm. (E) Schematic representation of full length Cdh1 (1-496 aa) encoding WD40 domain (represented as Cdh1-WT), N-terminus Cdh1 (1-155 aa) lacking WD40 domain (represented as Cdh1-CTM1), and C-terminus Cdh1 (156-496 aa) encoding WD40 domain (represented as Cdh1-CTM2). Interactions between full length MAST1 and Cdh1 truncated mutants by co-immunoprecipitation and immunoblotting with the indicated antibodies (lower panel). (F) Schematic representation of full length MAST1 (1-1570 aa) encoding serine/threonine (S/T) kinase domain and PDZ domain (represented as MAST1-WT), N-terminus MAST1 (1-832 aa) encoding S/T kinase domain (represented as MAST1-MTM1), C-terminus MAST1 (833-1570 aa) encoding PDZ domain (represented as MAST1-MTM2), and C-terminus MAST1 (1118-1465 aa) lacking PDZ domain (represented as MAST1-MTM3). Interactions between full length Cdh1 and MAST1 truncated mutants by co-immunoprecipitation and immunoblotting with the indicated antibodies (lower panel). (G) The effect of Cdh1 on endogenous MAST1 protein was analyzed in HeLa cells transfected with increasing concentrations of Flag-Cdh1. (H) HeLa cells were transfected with sgRNA1 and sgRNA2 targeting Cdh1 to assess the endogenous protein levels of Cdh1 and MAST1 by Western blotting. (I) The Cdh1-mediated degradation of endogenous MAST1 protein was rescued in cells transfected with sgRNA targeting Cdh1 . (J) The ubiquitination of endogenous MAST1 was analyzed by transfecting HeLa cells with Flag-Cdh1 or sgRNA targeting Cdh1 followed by immunoprecipitation with an anti-MAST1 antibody and immunoblotting with an anti-ubiquitin antibody. Protein expression was checked by Western blotting with the indicated antibodies. GAPDH was used as a loading control.

Article Snippet: Rabbit polyclonal antibodies against MAST1 (13306-1-AP, 1:500, Proteintech; CSB-PA897529LA01HU, 1:100, Cusabio; CSB-PA013511GA01HU, 1:500, Cusabio), USP1 (14346-1-AP, 1: 2,000; Proteintech), ERK1/2 (CST, 9102, 1: 1,000; Cell Signaling Technology), phospho-ERK1/2 (CST, 9106, 1: 1,000; Cell Signaling Technology), phospho-MEK1 (S221) (Cat no. 9121, 1: 1,000, Cell Signaling Technology), BIM (ab15184, 1:25, Abcam), cleaved PARP (D64E10, 1: 1,000, Cell Signaling Technology), and 488/594-conjugated secondary antibodies (Cat. no. A21207 and Cat. no. A21203, 1:200; Life Technologies) were used.

Techniques: Transfection, Expressing, Western Blot, Immunoprecipitation, Control, Ubiquitin Proteomics

DUB knockout library kit-based screening for USPs regulating MAST1 protein level by Western blot analysis. (A) Schematic representation of secondary screening with a CRISPR/Cas9-based sgRNA library to find DUBs that regulate MAST1 protein level. Steps 1-2: The designed DUB knockout sgRNA library, which consists of an entire set of genes encoding USPs, was co-transfected with Cas9 into HeLa-cis R cells (day 1). Step 3: The cells were placed under puromycin selection (2 µg/mL) and incubated for 3 days (days 2-5). Step 4: The transfected cells were harvested and lysed, and protein was isolated. Steps 5-6: Protein concentration was estimated by Bradford reagent, and equal concentrations of all DUBKO cell lysates were loaded on SDS-PAGE and screened for DUB candidates regulating endogenous expression pattern of MAST1 using Western blot (WB) analysis. (B) Equal protein concentrations from the cell lysates from (A) were subjected to Western blotting to determine the endogenous MAST1 protein level. For each blot, HeLa-cis R cells co-transfected with scrambled sgRNA and Cas9 served as the mock control. GAPDH was used as a loading control. The protein band intensities were estimated using ImageJ software with reference to the GAPDH control for each individual sgRNA (MAST1/GAPDH) and presented below the blot. (C) The effects of the targeting the putative DUB candidates on the MAST1 protein level were estimated by Western blotting. The protein band intensities were estimated using ImageJ software with reference to the GAPDH control band for each individual sgRNA (MAST1/GAPDH) ) and presented below the blot. (D) The interactions between putative DUB candidates and MAST1 by co-immunoprecipitation analysis. Myc-MAST1 and DUBs (Flag-USP1, Flag-USP28, and Flag-USP44) were transfected into HEK293 cells. (E) The interaction between endogenous USP9X and MAST1 by co-immunoprecipitation analysis. Cell lysates were immunoprecipitated and immunoblotted with the indicated antibodies. (F) A Venn diagram showing the overlapping DUB candidate based on cisplatin cytotoxicity, loss-of-function effect on MAST1 protein level, and interaction analysis with MAST1.

Journal: Theranostics

Article Title: CRISPR/Cas9-based genome-wide screening for deubiquitinase subfamily identifies USP1 regulating MAST1-driven cisplatin-resistance in cancer cells

doi: 10.7150/thno.72826

Figure Lengend Snippet: DUB knockout library kit-based screening for USPs regulating MAST1 protein level by Western blot analysis. (A) Schematic representation of secondary screening with a CRISPR/Cas9-based sgRNA library to find DUBs that regulate MAST1 protein level. Steps 1-2: The designed DUB knockout sgRNA library, which consists of an entire set of genes encoding USPs, was co-transfected with Cas9 into HeLa-cis R cells (day 1). Step 3: The cells were placed under puromycin selection (2 µg/mL) and incubated for 3 days (days 2-5). Step 4: The transfected cells were harvested and lysed, and protein was isolated. Steps 5-6: Protein concentration was estimated by Bradford reagent, and equal concentrations of all DUBKO cell lysates were loaded on SDS-PAGE and screened for DUB candidates regulating endogenous expression pattern of MAST1 using Western blot (WB) analysis. (B) Equal protein concentrations from the cell lysates from (A) were subjected to Western blotting to determine the endogenous MAST1 protein level. For each blot, HeLa-cis R cells co-transfected with scrambled sgRNA and Cas9 served as the mock control. GAPDH was used as a loading control. The protein band intensities were estimated using ImageJ software with reference to the GAPDH control for each individual sgRNA (MAST1/GAPDH) and presented below the blot. (C) The effects of the targeting the putative DUB candidates on the MAST1 protein level were estimated by Western blotting. The protein band intensities were estimated using ImageJ software with reference to the GAPDH control band for each individual sgRNA (MAST1/GAPDH) ) and presented below the blot. (D) The interactions between putative DUB candidates and MAST1 by co-immunoprecipitation analysis. Myc-MAST1 and DUBs (Flag-USP1, Flag-USP28, and Flag-USP44) were transfected into HEK293 cells. (E) The interaction between endogenous USP9X and MAST1 by co-immunoprecipitation analysis. Cell lysates were immunoprecipitated and immunoblotted with the indicated antibodies. (F) A Venn diagram showing the overlapping DUB candidate based on cisplatin cytotoxicity, loss-of-function effect on MAST1 protein level, and interaction analysis with MAST1.

Techniques: Knock-Out, Western Blot, CRISPR, Transfection, Selection, Incubation, Isolation, Protein Concentration, SDS Page, Expressing, Control, Software, Immunoprecipitation

USP1 interacts with and regulates the MAST1 protein. (A) Schematic representation of the sgRNAs targeting exon 5 of the USP1 gene. Red arrowheads indicate the positions of sgRNAs that target the top strand. sgRNA sequences are in red; PAM sequences are in bold blue font. (B) Validation of sgRNA efficiency targeting USP1 by transient transfection of sgRNA1 and sgRNA2 into HeLa cells and immunoblotting with USP1 antibody. (C) HeLa cells were transfected with sgRNA1 and shRNA1 targeting USP1 , and the endogenous protein levels of USP1 and MAST1 were checked by Western blotting. (D) HeLa cells were transfected with increasing concentrations of Flag-USP1 to check the endogenous MAST1 protein level. (E) HeLa cells were transfected with increasing concentrations of Flag-USP1CS to assess the endogenous MAST1 protein level. (F) The reconstitution effect of Flag-USP1 on endogenous MAST1 protein in USP1-depleted HeLa cells. The protein band intensities (Fig C-F) were estimated using ImageJ software with reference to the GAPDH control band for each individual sgRNA (MAST1/GAPDH) and presented below the blot. (G) Interactions between endogenous and (H) exogenous USP1 and MAST1 proteins were analyzed in HeLa cells and HEK293 cells, respectively. Cell lysates were immunoprecipitated and immunoblotted with the indicated antibodies. Protein expression was checked using Western blotting. GAPDH was used as a loading control. (I) HeLa cells were subjected to the Duolink PLA assay to analyze the interaction between USP1 and MAST1 using specific antibodies. In situ USP1-MAST1 interaction (PLA dots) was observed when USP1 and MAST1 were immunostained together but not when they were stained with individual antibodies. Scale bar: 10 µm. (J) HeLa cells were treated with either MLN7243 (10 µM) or PR-619 (20 µM) for 1 h before harvesting. Cell lysates were immunoprecipitated and immunoblotted with the indicated antibodies. (K) Schematic representation of full length USP1 (1-785 aa) encoding USP domain with catalytic triad residues (Cys, His, and Asp box) (represented as USP1-WT), N-terminus USP1 (1-400 aa) encoding catalytic Cys box (represented as USP1-UTM1), C-terminus USP1 (401-785 aa) encoding catalytic His and Asp box (represented as USP1-UTM2), and extended C-terminus USP1 (201-785 aa) encoding catalytic His and Asp box (represented as USP1-UTM3). Interactions between full length MAST1 and USP1 truncated mutants by co-immunoprecipitation and immunoblotting with the indicated antibodies (lower panel). (L) Schematic representation of full length MAST1 (1-1570 aa) encoding serine/threonine (S/T) kinase domain and PDZ domain (represented as MAST1-WT), N-terminus MAST1 (1-832 aa) encoding S/T kinase domain (represented as MAST1-MTM1), C-terminus MAST1 (833-1570 aa) encoding PDZ domain (represented as MAST1-MTM2), and C-terminus MAST1 (1118-1465 aa) lacking PDZ domain (represented as MAST1-MTM3). Interactions between full length USP1 and MAST1 truncated mutants were analyzed by co-immunoprecipitation and immunoblotting with the indicated antibodies (lower panel).

Journal: Theranostics

Article Title: CRISPR/Cas9-based genome-wide screening for deubiquitinase subfamily identifies USP1 regulating MAST1-driven cisplatin-resistance in cancer cells

doi: 10.7150/thno.72826

Figure Lengend Snippet: USP1 interacts with and regulates the MAST1 protein. (A) Schematic representation of the sgRNAs targeting exon 5 of the USP1 gene. Red arrowheads indicate the positions of sgRNAs that target the top strand. sgRNA sequences are in red; PAM sequences are in bold blue font. (B) Validation of sgRNA efficiency targeting USP1 by transient transfection of sgRNA1 and sgRNA2 into HeLa cells and immunoblotting with USP1 antibody. (C) HeLa cells were transfected with sgRNA1 and shRNA1 targeting USP1 , and the endogenous protein levels of USP1 and MAST1 were checked by Western blotting. (D) HeLa cells were transfected with increasing concentrations of Flag-USP1 to check the endogenous MAST1 protein level. (E) HeLa cells were transfected with increasing concentrations of Flag-USP1CS to assess the endogenous MAST1 protein level. (F) The reconstitution effect of Flag-USP1 on endogenous MAST1 protein in USP1-depleted HeLa cells. The protein band intensities (Fig C-F) were estimated using ImageJ software with reference to the GAPDH control band for each individual sgRNA (MAST1/GAPDH) and presented below the blot. (G) Interactions between endogenous and (H) exogenous USP1 and MAST1 proteins were analyzed in HeLa cells and HEK293 cells, respectively. Cell lysates were immunoprecipitated and immunoblotted with the indicated antibodies. Protein expression was checked using Western blotting. GAPDH was used as a loading control. (I) HeLa cells were subjected to the Duolink PLA assay to analyze the interaction between USP1 and MAST1 using specific antibodies. In situ USP1-MAST1 interaction (PLA dots) was observed when USP1 and MAST1 were immunostained together but not when they were stained with individual antibodies. Scale bar: 10 µm. (J) HeLa cells were treated with either MLN7243 (10 µM) or PR-619 (20 µM) for 1 h before harvesting. Cell lysates were immunoprecipitated and immunoblotted with the indicated antibodies. (K) Schematic representation of full length USP1 (1-785 aa) encoding USP domain with catalytic triad residues (Cys, His, and Asp box) (represented as USP1-WT), N-terminus USP1 (1-400 aa) encoding catalytic Cys box (represented as USP1-UTM1), C-terminus USP1 (401-785 aa) encoding catalytic His and Asp box (represented as USP1-UTM2), and extended C-terminus USP1 (201-785 aa) encoding catalytic His and Asp box (represented as USP1-UTM3). Interactions between full length MAST1 and USP1 truncated mutants by co-immunoprecipitation and immunoblotting with the indicated antibodies (lower panel). (L) Schematic representation of full length MAST1 (1-1570 aa) encoding serine/threonine (S/T) kinase domain and PDZ domain (represented as MAST1-WT), N-terminus MAST1 (1-832 aa) encoding S/T kinase domain (represented as MAST1-MTM1), C-terminus MAST1 (833-1570 aa) encoding PDZ domain (represented as MAST1-MTM2), and C-terminus MAST1 (1118-1465 aa) lacking PDZ domain (represented as MAST1-MTM3). Interactions between full length USP1 and MAST1 truncated mutants were analyzed by co-immunoprecipitation and immunoblotting with the indicated antibodies (lower panel).

Techniques: Biomarker Discovery, Transfection, Western Blot, Software, Control, Immunoprecipitation, Expressing, In Situ, Staining

USP1 extends MAST1 protein half-life by its deubiquitinating activity. (A) The ubiquitination and deubiquitination of endogenous MAST1 were analyzed by transfecting HeLa cells with Flag-USP1, Flag-USP1CS, or sgRNA targeting USP1 followed by immunoprecipitation with an anti-MAST1 antibody and immunoblotting with an anti-ubiquitin antibody. The cells were treated with MG132 for 6 h prior to harvest. (B) The K48- and K63-linked polyubiquitination of MAST1 was analyzed by transfecting HEK293 cells with Myc-MAST1, HA-ubiquitin, HA-K48-ubiquitin, and HA-K63-ubiquitin, followed by immunoprecipitation with an anti-Myc antibody and immunoblotting with anti-HA and anti-Myc antibodies. (C) The deubiquitination of K48-linked ubiquitination of MAST1 by USP1 was analyzed by transfecting HEK293 cells with Myc-MAST1 and HA-K48-ubiquitin along with Flag-USP1 or Flag-USP1CS, followed by immunoprecipitation with an anti-Myc antibody and immunoblotting with anti-HA and anti-Myc antibodies. The relative protein expression of MAST1-(Ub)n with respect to input MAST1 for (A-C) was quantified using ImageJ software and represented as (MAST1-(Ub)n/MAST1) below the blot. (D) Sanger sequencing data showing the disrupted USP1 gene sequences in A549 cells (USP1-KO1). The sgRNA recognition site is denoted in red. The deleted bases are indicated with dashes, and the inserted bases are denoted with green, with the number of deleted or inserted bases indicated in parentheses. The number of occurrences of the indicated sequence is shown in parentheses (for example, X3 and X7 indicate the number of each clone sequenced). (E) Flow cytometry assay showing the expression of USP1 in mock control vs. USP1-KO1. (F) The effect of USP1-KO1 on the mRNA expression of USP1 and (G) MAST1 was analyzed by qRT-PCR with specific primers. The relative mRNA expression levels are shown after normalization to GAPDH mRNA expression. Data are presented as the mean and standard deviation of three independent experiments (n = 3). A two-tailed t -test was used, and the P values are indicated. (H) Western blot analysis of the endogenous expression of USP1 and MAST1 protein in USP1-KO1. GAPDH was used as the internal loading control. (I) The effect of USP1 gene disruption on the endogenous expression of MAST1 was analyzed by immunofluorescence staining. Scale bar: 10 µm. (J) The TUBEs assay was performed to assess the ubiquitination status of the MAST1 protein in mock control and USP1-KO1 and USP1-KO2 clones. Cell lysates were immunoprecipitated with TUBEs antibodies, followed by immunoblotting with the indicated antibodies. (K) The total polyubiquitinated MAST1 protein was pulled down using TUBE2 resin from USP1-KO1 A549 cells treated with or without rUSP1 protein in the presence or absence of PR-619 (100 µM) and pimozide (20 µM) at 37 °C for 1 h. The eluted samples were analyzed by Western blotting with indicated antibodies. (L) The polyubiquitinated MAST1 protein was pulled down using TUBE2 resin treated with or without rUSP1 protein in the presence or absence of increasing concentrations of pimozide (0, 5, 10, and 20 µM) at 37 °C for 1 h. The eluted samples were analyzed by Western blotting with indicated antibodies. (M) Mock control, USP1-KO1, and USP1-KO1 reconstituted with either Flag-USP1 or (N) Flag-USP1CS were used to analyze the half-life of MAST1. CHX (150 µg/mL) was administered for the indicated time, and the cells were then harvested for Western blotting with the indicated antibodies, GAPDH was used as a loading control. Data are presented as the mean and standard deviation of three independent experiments (n=3). Two-way ANOVA followed by Tukey's post hoc test was used with the indicated P values.

Journal: Theranostics

Article Title: CRISPR/Cas9-based genome-wide screening for deubiquitinase subfamily identifies USP1 regulating MAST1-driven cisplatin-resistance in cancer cells

doi: 10.7150/thno.72826

Figure Lengend Snippet: USP1 extends MAST1 protein half-life by its deubiquitinating activity. (A) The ubiquitination and deubiquitination of endogenous MAST1 were analyzed by transfecting HeLa cells with Flag-USP1, Flag-USP1CS, or sgRNA targeting USP1 followed by immunoprecipitation with an anti-MAST1 antibody and immunoblotting with an anti-ubiquitin antibody. The cells were treated with MG132 for 6 h prior to harvest. (B) The K48- and K63-linked polyubiquitination of MAST1 was analyzed by transfecting HEK293 cells with Myc-MAST1, HA-ubiquitin, HA-K48-ubiquitin, and HA-K63-ubiquitin, followed by immunoprecipitation with an anti-Myc antibody and immunoblotting with anti-HA and anti-Myc antibodies. (C) The deubiquitination of K48-linked ubiquitination of MAST1 by USP1 was analyzed by transfecting HEK293 cells with Myc-MAST1 and HA-K48-ubiquitin along with Flag-USP1 or Flag-USP1CS, followed by immunoprecipitation with an anti-Myc antibody and immunoblotting with anti-HA and anti-Myc antibodies. The relative protein expression of MAST1-(Ub)n with respect to input MAST1 for (A-C) was quantified using ImageJ software and represented as (MAST1-(Ub)n/MAST1) below the blot. (D) Sanger sequencing data showing the disrupted USP1 gene sequences in A549 cells (USP1-KO1). The sgRNA recognition site is denoted in red. The deleted bases are indicated with dashes, and the inserted bases are denoted with green, with the number of deleted or inserted bases indicated in parentheses. The number of occurrences of the indicated sequence is shown in parentheses (for example, X3 and X7 indicate the number of each clone sequenced). (E) Flow cytometry assay showing the expression of USP1 in mock control vs. USP1-KO1. (F) The effect of USP1-KO1 on the mRNA expression of USP1 and (G) MAST1 was analyzed by qRT-PCR with specific primers. The relative mRNA expression levels are shown after normalization to GAPDH mRNA expression. Data are presented as the mean and standard deviation of three independent experiments (n = 3). A two-tailed t -test was used, and the P values are indicated. (H) Western blot analysis of the endogenous expression of USP1 and MAST1 protein in USP1-KO1. GAPDH was used as the internal loading control. (I) The effect of USP1 gene disruption on the endogenous expression of MAST1 was analyzed by immunofluorescence staining. Scale bar: 10 µm. (J) The TUBEs assay was performed to assess the ubiquitination status of the MAST1 protein in mock control and USP1-KO1 and USP1-KO2 clones. Cell lysates were immunoprecipitated with TUBEs antibodies, followed by immunoblotting with the indicated antibodies. (K) The total polyubiquitinated MAST1 protein was pulled down using TUBE2 resin from USP1-KO1 A549 cells treated with or without rUSP1 protein in the presence or absence of PR-619 (100 µM) and pimozide (20 µM) at 37 °C for 1 h. The eluted samples were analyzed by Western blotting with indicated antibodies. (L) The polyubiquitinated MAST1 protein was pulled down using TUBE2 resin treated with or without rUSP1 protein in the presence or absence of increasing concentrations of pimozide (0, 5, 10, and 20 µM) at 37 °C for 1 h. The eluted samples were analyzed by Western blotting with indicated antibodies. (M) Mock control, USP1-KO1, and USP1-KO1 reconstituted with either Flag-USP1 or (N) Flag-USP1CS were used to analyze the half-life of MAST1. CHX (150 µg/mL) was administered for the indicated time, and the cells were then harvested for Western blotting with the indicated antibodies, GAPDH was used as a loading control. Data are presented as the mean and standard deviation of three independent experiments (n=3). Two-way ANOVA followed by Tukey's post hoc test was used with the indicated P values.

Techniques: Activity Assay, Ubiquitin Proteomics, Immunoprecipitation, Western Blot, Expressing, Software, Sequencing, Flow Cytometry, Control, Quantitative RT-PCR, Standard Deviation, Two Tailed Test, Disruption, Immunofluorescence, Staining, Clone Assay

Clinical correlation between USP1 and MAST1 expression in various cancer tissues. (A) Box plot showing the difference between USP1 expression in tumor and normal tissues using Correlation AnalyzeR. Significance was determined via the Wilcoxon rank sum test: **** P < 0.0001. (B) Box plot showing the difference between MAST1 expression in tumor and normal tissues using Correlation AnalyzeR. Significance was determined via the Wilcoxon rank sum test: * P < .05, **** P < 0.0001. VST stands for variance-stabilizing transform. (C) A heat map showing mRNA expression levels of USP1 and MAST1 derived from the CCLE database. Representative samples are arranged from high to low mRNA levels of MAST1, and corresponding USP1 values are sorted. (D) A scatterplot showing the expression correlation between USP1 and MAST1 mRNA levels. Pearson correlations (r) quantifying the relationship between USP1 and MAST1 are given. (E) Endogenous protein expression patterns of USP1 and MAST1 in different cancer and non-cancer cell lines were assessed by Western blotting. GAPDH was used as the loading control. (F-H) Representative immunohistochemical (IHC) staining images of endogenous USP1 and MAST1 in (F) human lung cancer (n = 32), (G) colon cancer (n = 32), and (H) breast cancer (n = 21) tissues. All IHC images were quantified with an H-score. Scale bar = 30 µm.

Journal: Theranostics

Article Title: CRISPR/Cas9-based genome-wide screening for deubiquitinase subfamily identifies USP1 regulating MAST1-driven cisplatin-resistance in cancer cells

doi: 10.7150/thno.72826

Figure Lengend Snippet: Clinical correlation between USP1 and MAST1 expression in various cancer tissues. (A) Box plot showing the difference between USP1 expression in tumor and normal tissues using Correlation AnalyzeR. Significance was determined via the Wilcoxon rank sum test: **** P < 0.0001. (B) Box plot showing the difference between MAST1 expression in tumor and normal tissues using Correlation AnalyzeR. Significance was determined via the Wilcoxon rank sum test: * P < .05, **** P < 0.0001. VST stands for variance-stabilizing transform. (C) A heat map showing mRNA expression levels of USP1 and MAST1 derived from the CCLE database. Representative samples are arranged from high to low mRNA levels of MAST1, and corresponding USP1 values are sorted. (D) A scatterplot showing the expression correlation between USP1 and MAST1 mRNA levels. Pearson correlations (r) quantifying the relationship between USP1 and MAST1 are given. (E) Endogenous protein expression patterns of USP1 and MAST1 in different cancer and non-cancer cell lines were assessed by Western blotting. GAPDH was used as the loading control. (F-H) Representative immunohistochemical (IHC) staining images of endogenous USP1 and MAST1 in (F) human lung cancer (n = 32), (G) colon cancer (n = 32), and (H) breast cancer (n = 21) tissues. All IHC images were quantified with an H-score. Scale bar = 30 µm.

Techniques: Expressing, Derivative Assay, Western Blot, Control, Immunohistochemical staining, Immunohistochemistry

Depletion of USP1 promotes apoptosis, DNA damage, and tumor growth arrest. Mock control, USP1-KO1, and USP1-KO1 cells reconstituted with either USP1 or MAST1 were used to perform the following experiments. (A) Western blot analyses to validate the expression of USP1 and MAST1 using USP1- and MAST1-specific antibodies. GAPDH was used as the loading control. (B) The cells were treated with either vehicle or cisplatin (2 µg/mL) for 24 h and subjected to immunofluorescence analysis to estimate γH2AX foci formation. Green, γH2AX; blue, nucleus stained by DAPI. Scale bar = 100 µm. The right panel depicts the percentage of γH2AX-positive cells. (C) The cells were treated with cisplatin (2 µg/mL) for 24 h, and MEK1 activation and apoptosis-related factors were determined using Western blotting. GAPDH was used as the internal loading control. (D) The cells were treated with either vehicle or cisplatin (2 µg/mL) for 48 h and subjected to flow cytometry to measure the DNA content using PI staining and (E) annexin-V and 7-AAD staining. (F) The cells were treated with a sub-lethal dose of cisplatin (2 µg/mL) for 48 h, and cell viability was assayed using CCK-8 reagent. Data are presented as the mean and standard deviation of three independent experiments (n = 3). (G-I) Vehicle- or cisplatin-treated cells were subjected to a (G) colony formation assay, (H) wound-healing assay, and (I) Transwell cell-invasion assay. Data are presented as the mean and standard deviation of four independent experiments (n = 4). (J) Xenografts were generated by subcutaneously injecting the mentioned cell groups into the right flanks of NSG mice (n = 4/group). Mice were i.p. injected with either saline (vehicle) or cisplatin (2 mg/kg) twice a week beginning 7 days after xenograft implantation, and tumor size was monitored. Tumor volumes were recorded, and tissues were stored for IHC experiments. The right panel shows the tumors excised from the mice after the experiment. (K) Tumor volume was measured every other day and is presented graphically. Data are presented as the mean and standard deviation of four independent experiments (n = 4). Two-way ANOVA followed by Tukey's post hoc test was used with the indicated P values. (L) Xenograft tumors were embedded in paraffin and sectioned. IHC analyses were performed with the indicated antibodies. Scale bar = 30 µm.

Journal: Theranostics

Article Title: CRISPR/Cas9-based genome-wide screening for deubiquitinase subfamily identifies USP1 regulating MAST1-driven cisplatin-resistance in cancer cells

doi: 10.7150/thno.72826

Figure Lengend Snippet: Depletion of USP1 promotes apoptosis, DNA damage, and tumor growth arrest. Mock control, USP1-KO1, and USP1-KO1 cells reconstituted with either USP1 or MAST1 were used to perform the following experiments. (A) Western blot analyses to validate the expression of USP1 and MAST1 using USP1- and MAST1-specific antibodies. GAPDH was used as the loading control. (B) The cells were treated with either vehicle or cisplatin (2 µg/mL) for 24 h and subjected to immunofluorescence analysis to estimate γH2AX foci formation. Green, γH2AX; blue, nucleus stained by DAPI. Scale bar = 100 µm. The right panel depicts the percentage of γH2AX-positive cells. (C) The cells were treated with cisplatin (2 µg/mL) for 24 h, and MEK1 activation and apoptosis-related factors were determined using Western blotting. GAPDH was used as the internal loading control. (D) The cells were treated with either vehicle or cisplatin (2 µg/mL) for 48 h and subjected to flow cytometry to measure the DNA content using PI staining and (E) annexin-V and 7-AAD staining. (F) The cells were treated with a sub-lethal dose of cisplatin (2 µg/mL) for 48 h, and cell viability was assayed using CCK-8 reagent. Data are presented as the mean and standard deviation of three independent experiments (n = 3). (G-I) Vehicle- or cisplatin-treated cells were subjected to a (G) colony formation assay, (H) wound-healing assay, and (I) Transwell cell-invasion assay. Data are presented as the mean and standard deviation of four independent experiments (n = 4). (J) Xenografts were generated by subcutaneously injecting the mentioned cell groups into the right flanks of NSG mice (n = 4/group). Mice were i.p. injected with either saline (vehicle) or cisplatin (2 mg/kg) twice a week beginning 7 days after xenograft implantation, and tumor size was monitored. Tumor volumes were recorded, and tissues were stored for IHC experiments. The right panel shows the tumors excised from the mice after the experiment. (K) Tumor volume was measured every other day and is presented graphically. Data are presented as the mean and standard deviation of four independent experiments (n = 4). Two-way ANOVA followed by Tukey's post hoc test was used with the indicated P values. (L) Xenograft tumors were embedded in paraffin and sectioned. IHC analyses were performed with the indicated antibodies. Scale bar = 30 µm.

Techniques: Control, Western Blot, Expressing, Immunofluorescence, Staining, Activation Assay, Flow Cytometry, CCK-8 Assay, Standard Deviation, Colony Assay, Wound Healing Assay, Invasion Assay, Generated, Injection, Saline

Combination of pimozide and lestaurtinib inhibits MAST1 protein and cisplatin-resistant tumor growth more than either single treatment. (A) The effect of USP1 inhibition on MAST1 protein level was determined by treating HeLa-cis R cells with increasing concentrations of pimozide for 24 h. The protein expression of MAST1 was determined by Western blotting. GAPDH was used as an internal loading control. (B) The effect of combination treatment of pimozide and lestaurtinib on MAST1-mediated MEK phosphorylation. HeLa-cis R cells were treated with pimozide (50 µM) and lestaurtinib (200 nM) in the presence of sub-lethal doses of cisplatin (5 µg/mL) for 24 h. The activity of MAST1 was assessed by a Western blot analysis of the phospho-MEK1 and phospho-ERK levels. GAPDH was used as an internal loading control. (C, D) The effect of combined treatment with pimozide and lestaurtinib on (C) cisplatin sensitivity (n = 3) (D) and cell viability in A549-cis R and HeLa-cis R cells (n = 4). Data are presented as the mean and standard deviation of at least three independent experiments. Two-way ANOVA followed by Tukey's post hoc test was used with the indicated P values. (E) Combination index (CI) plots for the synergistic effect of pimozide and lestaurtinib in A549-cis R and HeLa-cis R cells. (F-H) The effect of combination treatment with pimozide and lestaurtinib was validated using (F) colony formation assay, (G) wound-healing assay, and (H) Transwell cell-invasion assay. Data are presented as the mean and standard deviation of three independent experiments (n = 3). Two-way ANOVA followed by Tukey's post hoc test was used with the indicated P values. (I) Xenografts were generated by subcutaneously injecting A549-cis R cells into the right flanks of NSG mice (n = 4). Mice were treated with pimozide (10 mg/kg), lestaurtinib (20 mg/kg), and cisplatin (5 mg/kg) beginning 26 days after xenograft implantation, and tumor size was monitored. The right panel shows the tumors excised from the mice after the experiment. (J) Tumor volume and tumor weight were measured and are presented graphically. Data are presented as the mean and standard deviation of four independent experiments (n = 4). Two-way ANOVA followed by Tukey's post hoc test was used with the indicated P values. For brevity, statistical significance is shown only for comparisons between the groups of interest, except for the negative control group.

Journal: Theranostics

Article Title: CRISPR/Cas9-based genome-wide screening for deubiquitinase subfamily identifies USP1 regulating MAST1-driven cisplatin-resistance in cancer cells

doi: 10.7150/thno.72826

Figure Lengend Snippet: Combination of pimozide and lestaurtinib inhibits MAST1 protein and cisplatin-resistant tumor growth more than either single treatment. (A) The effect of USP1 inhibition on MAST1 protein level was determined by treating HeLa-cis R cells with increasing concentrations of pimozide for 24 h. The protein expression of MAST1 was determined by Western blotting. GAPDH was used as an internal loading control. (B) The effect of combination treatment of pimozide and lestaurtinib on MAST1-mediated MEK phosphorylation. HeLa-cis R cells were treated with pimozide (50 µM) and lestaurtinib (200 nM) in the presence of sub-lethal doses of cisplatin (5 µg/mL) for 24 h. The activity of MAST1 was assessed by a Western blot analysis of the phospho-MEK1 and phospho-ERK levels. GAPDH was used as an internal loading control. (C, D) The effect of combined treatment with pimozide and lestaurtinib on (C) cisplatin sensitivity (n = 3) (D) and cell viability in A549-cis R and HeLa-cis R cells (n = 4). Data are presented as the mean and standard deviation of at least three independent experiments. Two-way ANOVA followed by Tukey's post hoc test was used with the indicated P values. (E) Combination index (CI) plots for the synergistic effect of pimozide and lestaurtinib in A549-cis R and HeLa-cis R cells. (F-H) The effect of combination treatment with pimozide and lestaurtinib was validated using (F) colony formation assay, (G) wound-healing assay, and (H) Transwell cell-invasion assay. Data are presented as the mean and standard deviation of three independent experiments (n = 3). Two-way ANOVA followed by Tukey's post hoc test was used with the indicated P values. (I) Xenografts were generated by subcutaneously injecting A549-cis R cells into the right flanks of NSG mice (n = 4). Mice were treated with pimozide (10 mg/kg), lestaurtinib (20 mg/kg), and cisplatin (5 mg/kg) beginning 26 days after xenograft implantation, and tumor size was monitored. The right panel shows the tumors excised from the mice after the experiment. (J) Tumor volume and tumor weight were measured and are presented graphically. Data are presented as the mean and standard deviation of four independent experiments (n = 4). Two-way ANOVA followed by Tukey's post hoc test was used with the indicated P values. For brevity, statistical significance is shown only for comparisons between the groups of interest, except for the negative control group.

Techniques: Inhibition, Expressing, Western Blot, Control, Phospho-proteomics, Activity Assay, Standard Deviation, Colony Assay, Wound Healing Assay, Invasion Assay, Generated, Negative Control

Journal: Endoplasmic Reticulum Stress in Diseases

Article Title: IRE-1α regulates expression of ubiquitin specific peptidases during hypoxic response in U87 glioma cells

doi: 10.1515/ersc-2016-0003

Figure Lengend Snippet: Figure 1. Expression level of USP1, USP4, USP10, USP14, USP22, USP25, and GSA7 mRNA in glioma cell line U87 (Vector) and its subline with a deficiency of both protein kinase and endoribonuclease of the signaling enzyme IRE-1α (dnIRE-1α) measured by qPCR. mRNA expressions values were normalized to beta-actin mRNA expression and presented as percent of control (vector, 100%); mean ± SEM; n = 4; * - P < 0,05 versus control; ** - P < 0,01 versus control.

Article Snippet: Rabbit polyclonal anti-USP1 antibody (ab108104), anti-USP14 antibody (ab137432), and anti-Apg7 antibody (ab53255) were from Abcam (UK), anti-ACTB (β-actin) antibodies were from Santa Cruz Biotechnology (Santa Cruz, USA) and rabbit polyclonal anti-HIF-1α antibody was from Novus Biologicals, USA.

Techniques: Expressing, Plasmid Preparation, Control

Journal: Endoplasmic Reticulum Stress in Diseases

Article Title: IRE-1α regulates expression of ubiquitin specific peptidases during hypoxic response in U87 glioma cells

doi: 10.1515/ersc-2016-0003

Figure Lengend Snippet: Figure 2. Effect of hypoxia (3% oxygen – 16h) on the expression level of USP1 (A), USP4 (B), USP10 (C), USP14 (D), USP22 (E), USP25 (F), and GSA7/ATG7 (G) mRNA (by qPCR) in glioma cells with a deficiency of IRE-1α (dnIRE-1α). mRNA expressions values were normalized to beta- actin mRNA expression and presented as percent of control 1 (control glioma cells transfected by vector, 100%); mean ± SEM; n = 4.

Techniques: Expressing, Control, Transfection, Plasmid Preparation

Journal: Endoplasmic Reticulum Stress in Diseases

Article Title: IRE-1α regulates expression of ubiquitin specific peptidases during hypoxic response in U87 glioma cells

doi: 10.1515/ersc-2016-0003

Figure Lengend Snippet: Figure 4. Comparative effect of hypoxia (3% oxygen – 16h) on the expression level of USP1, USP4, USP10, USP14, USP22, USP25, and GSA7 mRNA cells with a deficiency of IRE-1α (dnIRE-1α). mRNA expressions values were normalized to beta-actin mRNA expression and presented as percent of corresponding controls (vector as well as dnIRE-1α), 100%); mean ± SEM; n = 4.

Techniques: Expressing, Plasmid Preparation

Journal: Endoplasmic Reticulum Stress in Diseases

Article Title: IRE-1α regulates expression of ubiquitin specific peptidases during hypoxic response in U87 glioma cells

doi: 10.1515/ersc-2016-0003

Figure Lengend Snippet: Figure 3. Effect of hypoxia (3% oxygen – 16h) on protein level of USP1, USP14, and GSA7/ATG7 in glioma cells with a deficiency of IRE-1α (dnIRE-1α) measured by Western blot. ACTB protein level was used to ensure equal loading of the samples.

Techniques: Western Blot

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rabbit polyclonal anti usp1 antibody (Novus Biologicals)

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