ab antigenic peptide drg brain region Search Results


93
Bioss il 17 igg
Il 17 Igg, supplied by Bioss, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ab+antigenic+peptide+drg+brain+region/IL-17+Polyclonal+Antibody/pm31432577-57-18-20
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Novus Biologicals mrgx2 antibody
LAD2 mast cells were stably transduced with scrambled shRNA control lentivirus or shRNA lentivirus targeted against <t>MrgX2.</t> (A) Western blotting was performed to determine MrgX2 expression in control and MrgX2 knockdown (KD) cells. (B) shRNA control and MrgX2 KD cells were stimulated with hBD2, hBD3, cortistatin (CST) or C3a and percent degranulation (β-hexosaminidase release) was determined. Data are mean ± SEM of three experiments. Statistical significance was determined by one-way ANOVA with Bonferroni's post test. * indicates p<0.01 and ** indicates p<0.001.
Mrgx2 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/ab+antigenic+peptide+drg+brain+region/MRGX2+Antibody/pmc03691353-38-0-5
Average 90 stars, based on 1 article reviews
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R&D Systems probdnf antibody
LAD2 mast cells were stably transduced with scrambled shRNA control lentivirus or shRNA lentivirus targeted against <t>MrgX2.</t> (A) Western blotting was performed to determine MrgX2 expression in control and MrgX2 knockdown (KD) cells. (B) shRNA control and MrgX2 KD cells were stimulated with hBD2, hBD3, cortistatin (CST) or C3a and percent degranulation (β-hexosaminidase release) was determined. Data are mean ± SEM of three experiments. Statistical significance was determined by one-way ANOVA with Bonferroni's post test. * indicates p<0.01 and ** indicates p<0.001.
Probdnf Antibody, supplied by R&D Systems, 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/ab+antigenic+peptide+drg+brain+region/proBDNF+Antibody/pmc07723927__DataSheet_1-19-14-16
Average 90 stars, based on 1 article reviews
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Novus Biologicals antibody against α smooth muscle actin
LAD2 mast cells were stably transduced with scrambled shRNA control lentivirus or shRNA lentivirus targeted against <t>MrgX2.</t> (A) Western blotting was performed to determine MrgX2 expression in control and MrgX2 knockdown (KD) cells. (B) shRNA control and MrgX2 KD cells were stimulated with hBD2, hBD3, cortistatin (CST) or C3a and percent degranulation (β-hexosaminidase release) was determined. Data are mean ± SEM of three experiments. Statistical significance was determined by one-way ANOVA with Bonferroni's post test. * indicates p<0.01 and ** indicates p<0.001.
Antibody Against α Smooth Muscle Actin, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 93 stars, based on 1 article reviews
antibody against α smooth muscle actin - by Bioz Stars, 2026-10
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90
ProSci Incorporated anti tnfr1
RARγ has a role in the formation of death complexes. a Western blot analysis of HT-29 cont-shRNA, and RARγ-shRNA-A treated with DMSO, TS or TSZ for 24 h and cell lysates were immunoblotted with the indicated antibodies. b , c Immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated with TSZ for the indicated time. Cell lysates were collected and immunoprecipitated with anti-Caspase-8 antibody b or <t>anti-TNFR1</t> antibody c . The immunoprecipitated complexes were immunoblotted with the indicated antibodies. d Sequential immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated TSZ for 2 h. First IP : <t>TNFR1</t> complex I was immunoprecipitated using anti-TNFR1 antibody. Second IP : the remaining lysates were immunoprecipitated again with anti-TNFR1 antibody. Third IP : the remaining lysates were then immunoprecipitated with anti-TRADD antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. (M: marker). All blots above are representative of one of three experiments
Anti Tnfr1, supplied by ProSci Incorporated, 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/ab+antigenic+peptide+drg+brain+region/Tnfrsf1b+Peptide/pmc05583178-283-60-52
Average 90 stars, based on 1 article reviews
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90
ATCC h 2d q antibody 30 5 7s
RARγ has a role in the formation of death complexes. a Western blot analysis of HT-29 cont-shRNA, and RARγ-shRNA-A treated with DMSO, TS or TSZ for 24 h and cell lysates were immunoblotted with the indicated antibodies. b , c Immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated with TSZ for the indicated time. Cell lysates were collected and immunoprecipitated with anti-Caspase-8 antibody b or <t>anti-TNFR1</t> antibody c . The immunoprecipitated complexes were immunoblotted with the indicated antibodies. d Sequential immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated TSZ for 2 h. First IP : <t>TNFR1</t> complex I was immunoprecipitated using anti-TNFR1 antibody. Second IP : the remaining lysates were immunoprecipitated again with anti-TNFR1 antibody. Third IP : the remaining lysates were then immunoprecipitated with anti-TRADD antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. (M: marker). All blots above are representative of one of three experiments
H 2d Q Antibody 30 5 7s, supplied by ATCC, 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/ab+antigenic+peptide+drg+brain+region/30-5-7S/pmc02212915-205-26-30
Average 90 stars, based on 1 article reviews
h 2d q antibody 30 5 7s - by Bioz Stars, 2026-10
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98
Cell Signaling Technology Inc anti alpha smooth muscle actin α sma
Effect of MPs and Cd on fibrosis in mouse kidneys. ( A – C ): Representative images of Sirius Red staining and Masson staining of the kidney after MP and/or Cd exposure. a: Glomerulus, b: Renal tubule. ( B , C ): Quantitative analysis. ( D – G ): The levels of collagen type IV <t>alpha</t> 1 chain (COL4A1), transforming growth factor beta 1 (TGF-β1), and alpha smooth muscle actin <t>(α-SMA)</t> were detected using western blotting. ( D ): Representative western blot image; ( E – G ): Quantitative analysis. Data are presented as means ± SD from three independent experiments. ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared to the control group; # p < 0.05, ## p < 0.01, #### p < 0.0001 compared to the Cd group.
Anti Alpha Smooth Muscle Actin α Sma, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 98/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ab+antigenic+peptide+drg+brain+region/alpha-Smooth+Muscle+Actin+XP+Rabbit+mAb/pmc09694236-134-10-38
Average 98 stars, based on 1 article reviews
anti alpha smooth muscle actin α sma - by Bioz Stars, 2026-10
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93
Cell Signaling Technology Inc notch1 polyclonal antibody
Effect of MPs and Cd on fibrosis in mouse kidneys. ( A – C ): Representative images of Sirius Red staining and Masson staining of the kidney after MP and/or Cd exposure. a: Glomerulus, b: Renal tubule. ( B , C ): Quantitative analysis. ( D – G ): The levels of collagen type IV <t>alpha</t> 1 chain (COL4A1), transforming growth factor beta 1 (TGF-β1), and alpha smooth muscle actin <t>(α-SMA)</t> were detected using western blotting. ( D ): Representative western blot image; ( E – G ): Quantitative analysis. Data are presented as means ± SD from three independent experiments. ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared to the control group; # p < 0.05, ## p < 0.01, #### p < 0.0001 compared to the Cd group.
Notch1 Polyclonal Antibody, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ab+antigenic+peptide+drg+brain+region/Prostate+Specific+Membrane+Antigen+XP+Rabbit+mAb/pmc11382803-165-100-111
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notch1 polyclonal antibody - by Bioz Stars, 2026-10
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97
Cell Signaling Technology Inc pcna d3h8p xp rabbit mab
Effect of MPs and Cd on fibrosis in mouse kidneys. ( A – C ): Representative images of Sirius Red staining and Masson staining of the kidney after MP and/or Cd exposure. a: Glomerulus, b: Renal tubule. ( B , C ): Quantitative analysis. ( D – G ): The levels of collagen type IV <t>alpha</t> 1 chain (COL4A1), transforming growth factor beta 1 (TGF-β1), and alpha smooth muscle actin <t>(α-SMA)</t> were detected using western blotting. ( D ): Representative western blot image; ( E – G ): Quantitative analysis. Data are presented as means ± SD from three independent experiments. ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared to the control group; # p < 0.05, ## p < 0.01, #### p < 0.0001 compared to the Cd group.
Pcna D3h8p Xp Rabbit Mab, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ab+antigenic+peptide+drg+brain+region/PCNA+XP+Rabbit+mAb/pmc06737211-459-6-13
Average 97 stars, based on 1 article reviews
pcna d3h8p xp rabbit mab - by Bioz Stars, 2026-10
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97
Bio X Cell anti cd8a depleting antibody
Effect of MPs and Cd on fibrosis in mouse kidneys. ( A – C ): Representative images of Sirius Red staining and Masson staining of the kidney after MP and/or Cd exposure. a: Glomerulus, b: Renal tubule. ( B , C ): Quantitative analysis. ( D – G ): The levels of collagen type IV <t>alpha</t> 1 chain (COL4A1), transforming growth factor beta 1 (TGF-β1), and alpha smooth muscle actin <t>(α-SMA)</t> were detected using western blotting. ( D ): Representative western blot image; ( E – G ): Quantitative analysis. Data are presented as means ± SD from three independent experiments. ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared to the control group; # p < 0.05, ## p < 0.01, #### p < 0.0001 compared to the Cd group.
Anti Cd8a Depleting Antibody, supplied by Bio X Cell, used in various techniques. Bioz Stars score: 97/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ab+antigenic+peptide+drg+brain+region/Anti-CD8+Cd8A+Antibody/pm38678024-270-6-12
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94
Proteintech antibodies tap1
The expression of transporter associated with antigen processing 1 <t>(TAP1)</t> in pan-cancer. (A) TAP1 expression of 31 kinds of normal tissues downloaded from genotype-tissue expression (GTEx) database. (B) TAP1 expression in 21 kinds of cancer cell lines derived from the cancer cell line encyclopedia (CCLE). (C) TAP1 expression in tumor samples and the adjacent normal samples of 20 cancers derived from the TCGA. (D) TAP1 expression in tumor samples and normal samples of 27 cancers derived from the cancer genome atlas (TCGA) and GTEx database. * p < 0.05. ** p < 0.01. *** p < 0.001.
Antibodies Tap1, supplied by Proteintech, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ab+antigenic+peptide+drg+brain+region/TAP1+Antibody/pmc08702961-80-8-14
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Bioss α smooth muscle actin α sma monoclonal antibody
The expression of transporter associated with antigen processing 1 <t>(TAP1)</t> in pan-cancer. (A) TAP1 expression of 31 kinds of normal tissues downloaded from genotype-tissue expression (GTEx) database. (B) TAP1 expression in 21 kinds of cancer cell lines derived from the cancer cell line encyclopedia (CCLE). (C) TAP1 expression in tumor samples and the adjacent normal samples of 20 cancers derived from the TCGA. (D) TAP1 expression in tumor samples and normal samples of 27 cancers derived from the cancer genome atlas (TCGA) and GTEx database. * p < 0.05. ** p < 0.01. *** p < 0.001.
α Smooth Muscle Actin α Sma Monoclonal Antibody, supplied by Bioss, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/ab+antigenic+peptide+drg+brain+region/alpha+smooth+muscle+Actin+(8B2)+Monoclonal+Antibody/pm35573239-49-18-24
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α smooth muscle actin α sma monoclonal antibody - by Bioz Stars, 2026-10
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Image Search Results


LAD2 mast cells were stably transduced with scrambled shRNA control lentivirus or shRNA lentivirus targeted against MrgX2. (A) Western blotting was performed to determine MrgX2 expression in control and MrgX2 knockdown (KD) cells. (B) shRNA control and MrgX2 KD cells were stimulated with hBD2, hBD3, cortistatin (CST) or C3a and percent degranulation (β-hexosaminidase release) was determined. Data are mean ± SEM of three experiments. Statistical significance was determined by one-way ANOVA with Bonferroni's post test. * indicates p<0.01 and ** indicates p<0.001.

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: ?-defensins activate human mast cells via Mas-related Gene-X2 (MrgX2)

doi: 10.4049/jimmunol.1300023

Figure Lengend Snippet: LAD2 mast cells were stably transduced with scrambled shRNA control lentivirus or shRNA lentivirus targeted against MrgX2. (A) Western blotting was performed to determine MrgX2 expression in control and MrgX2 knockdown (KD) cells. (B) shRNA control and MrgX2 KD cells were stimulated with hBD2, hBD3, cortistatin (CST) or C3a and percent degranulation (β-hexosaminidase release) was determined. Data are mean ± SEM of three experiments. Statistical significance was determined by one-way ANOVA with Bonferroni's post test. * indicates p<0.01 and ** indicates p<0.001.

Article Snippet: MrgX2 antibody was purchased from Novus Biologicals (Littleton, CO).

Techniques: Stable Transfection, Transduction, shRNA, Control, Western Blot, Expressing, Knockdown

(A) RBL-2H3 cells stably expressing MrgX2 were stimulated with buffer, hBD2, hBD3 or cortistatin (CST) for 30 min and β-hexosaminidase release was measured. Data shown are representative of 3 similar experiments. Statistical significance was determined by one-way ANOVA with Bonferroni's post test. * indicates p<0.01 and ** indicates p<0.001. RBL-2H3 cells stably expressing MrgX2 were loaded with Indo-1AM and Ca2+ mobilization in response to (B) hBD2, (C) hBD3 or (D) CST was determined. HEK293 cells stably expressing MrgX2 were loaded with Indo-1AM and Ca2+ mobilization in response to (E) hBD3 or (F) CST was determined. Traces shown are representative of 3 individual experiments.

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: ?-defensins activate human mast cells via Mas-related Gene-X2 (MrgX2)

doi: 10.4049/jimmunol.1300023

Figure Lengend Snippet: (A) RBL-2H3 cells stably expressing MrgX2 were stimulated with buffer, hBD2, hBD3 or cortistatin (CST) for 30 min and β-hexosaminidase release was measured. Data shown are representative of 3 similar experiments. Statistical significance was determined by one-way ANOVA with Bonferroni's post test. * indicates p<0.01 and ** indicates p<0.001. RBL-2H3 cells stably expressing MrgX2 were loaded with Indo-1AM and Ca2+ mobilization in response to (B) hBD2, (C) hBD3 or (D) CST was determined. HEK293 cells stably expressing MrgX2 were loaded with Indo-1AM and Ca2+ mobilization in response to (E) hBD3 or (F) CST was determined. Traces shown are representative of 3 individual experiments.

Article Snippet: MrgX2 antibody was purchased from Novus Biologicals (Littleton, CO).

Techniques: Stable Transfection, Expressing

(A) BMMCs were transiently transfected with HA tagged MrgX2 (solid line) or control plasmid vector (broken line) and MrgX2 receptor expression level was analyzed using flow cytometry. A representative histogram is shown. (B) Control and MrgX2 expressing BMMCs were incubated with DNP specific mouse IgE (1 μg/mL, 16 h). Cells were exposed to buffer (control), CST, hBD3, mCRAMP or DNP-BSA (10 ng/mL) for 30 minutes and β-hexosaminidase release was measured. LAD2 cells were stimulated with mCRAMP and (C) intracellular Ca2+ mobilization or (D) degranulation was determined. Traces are representative of 3 independent experiments. Bar graphs represent mean ± SEM of three experiments. Statistical significance was determined by one-way ANOVA with Bonferroni's post test. * indicates p<0.01.

Journal: Journal of immunology (Baltimore, Md. : 1950)

Article Title: ?-defensins activate human mast cells via Mas-related Gene-X2 (MrgX2)

doi: 10.4049/jimmunol.1300023

Figure Lengend Snippet: (A) BMMCs were transiently transfected with HA tagged MrgX2 (solid line) or control plasmid vector (broken line) and MrgX2 receptor expression level was analyzed using flow cytometry. A representative histogram is shown. (B) Control and MrgX2 expressing BMMCs were incubated with DNP specific mouse IgE (1 μg/mL, 16 h). Cells were exposed to buffer (control), CST, hBD3, mCRAMP or DNP-BSA (10 ng/mL) for 30 minutes and β-hexosaminidase release was measured. LAD2 cells were stimulated with mCRAMP and (C) intracellular Ca2+ mobilization or (D) degranulation was determined. Traces are representative of 3 independent experiments. Bar graphs represent mean ± SEM of three experiments. Statistical significance was determined by one-way ANOVA with Bonferroni's post test. * indicates p<0.01.

Article Snippet: MrgX2 antibody was purchased from Novus Biologicals (Littleton, CO).

Techniques: Transfection, Control, Plasmid Preparation, Expressing, Flow Cytometry, Incubation

RARγ has a role in the formation of death complexes. a Western blot analysis of HT-29 cont-shRNA, and RARγ-shRNA-A treated with DMSO, TS or TSZ for 24 h and cell lysates were immunoblotted with the indicated antibodies. b , c Immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated with TSZ for the indicated time. Cell lysates were collected and immunoprecipitated with anti-Caspase-8 antibody b or anti-TNFR1 antibody c . The immunoprecipitated complexes were immunoblotted with the indicated antibodies. d Sequential immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated TSZ for 2 h. First IP : TNFR1 complex I was immunoprecipitated using anti-TNFR1 antibody. Second IP : the remaining lysates were immunoprecipitated again with anti-TNFR1 antibody. Third IP : the remaining lysates were then immunoprecipitated with anti-TRADD antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. (M: marker). All blots above are representative of one of three experiments

Journal: Nature Communications

Article Title: The cytoplasmic nuclear receptor RARγ controls RIP1 initiated cell death when cIAP activity is inhibited

doi: 10.1038/s41467-017-00496-6

Figure Lengend Snippet: RARγ has a role in the formation of death complexes. a Western blot analysis of HT-29 cont-shRNA, and RARγ-shRNA-A treated with DMSO, TS or TSZ for 24 h and cell lysates were immunoblotted with the indicated antibodies. b , c Immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated with TSZ for the indicated time. Cell lysates were collected and immunoprecipitated with anti-Caspase-8 antibody b or anti-TNFR1 antibody c . The immunoprecipitated complexes were immunoblotted with the indicated antibodies. d Sequential immunoprecipitation of HT-29 cont-shRNA or RARγ-shRNA-A cells treated TSZ for 2 h. First IP : TNFR1 complex I was immunoprecipitated using anti-TNFR1 antibody. Second IP : the remaining lysates were immunoprecipitated again with anti-TNFR1 antibody. Third IP : the remaining lysates were then immunoprecipitated with anti-TRADD antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. (M: marker). All blots above are representative of one of three experiments

Article Snippet: Anti-RARγ (C-15) (sc-550) for human, anti-RARα (C-20) (sc-551), anti-caspase-8 (C-20) (sc-6136), anti-cIAP2 (sc7944) and anti-Fas (C-20) (sc-715) from Santa Cruz; anti-RIP1 (610459) and anti-FADD (610400) from BD Biosciences; anti-RARγ1 (ab5905) for mouse, anti-RIP3 (ab72106), anti-MLKL (ab184718) for human, anti-MLKL (ab172868) for mouse and anti-cIAP1 (ab2399) from Abcam; anti-RIP3 (2283) for mouse from ProSci, anti-TRADD (05-473) from Upstate; anti-TRAF2 (MAB3277) and anti-TNFR1 (AF-425-PB) from R&D; anti-Actin (A3853) (dilution 1:10,000), anti-FLAG (F9291) (dilution 1:5,000) and anti-GFP (G6539) (dilution 1:5 000) from Sigma; anti-V5 (R960-25) (dilution 1:5,000) from Invitrogen; anti-PARP1 (BML-SA250-0050) from Enzo Life Science; anti-GAPDH (NB300-22) (dilution 1:5,000) from Novus Biologicals; anti-cleaved caspase-8 (9496), anti-CYLD (4495), anti-RIP1 (137451) and anti-p-RIP1(65746) from Cell Signaling Technology; anti-DsRed (632392) (dilution 1:5,000) from Clontech.

Techniques: Western Blot, shRNA, Immunoprecipitation, Marker

RARγ initiates the formation of death complexes by dissociating RIP1 from TNFR1. a Immunoprecipitation of HT-29 cont-shRNA, TRADD-shRNA or RIP1-shRNA treated with TSZ for the indicated times. Cell lysates were immunoprecipitated using anti-TNFR1 antibody and immunoblotted with the indicated antibodies. b Sequential immunoprecipitation of HEK293T cells co-transfected with FLAG-TNFR1, DsRed-RIP1 and increasing amounts of V5-RARγ-NLSmut plasmids as indicated. First IP : cell lysates were immunoprecipitated with anti-FLAG (TNFR1) antibody. Second IP : the remaining lysates were then immunoprecipitated with anti-V5 (RARγ) antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. c Sequential immunoprecipitation of HEK293T cells co-transfected with V5-RARγ-NLSmut, RIP1-Myc, and increasing amounts of DsRed-RIP3 plasmids as indicated. First IP : cell lysates were immunoprecipitated with anti-V5 (RARγ) antibody. Second IP : the remaining lysates were then immunoprecipitated with anti-DsRed (RIP3) antibody. The immunoprecipitated complexes were analyzed with the indicated antibodies. d WT and RIP3−/− MEFs treated with TSZ for the indicated times. Cell lysates were immunoprecipitated using anti-Caspase-8 antibody and immunoblotted with the indicated antibodies. All blots above are representative of one of three experiments

Journal: Nature Communications

Article Title: The cytoplasmic nuclear receptor RARγ controls RIP1 initiated cell death when cIAP activity is inhibited

doi: 10.1038/s41467-017-00496-6

Figure Lengend Snippet: RARγ initiates the formation of death complexes by dissociating RIP1 from TNFR1. a Immunoprecipitation of HT-29 cont-shRNA, TRADD-shRNA or RIP1-shRNA treated with TSZ for the indicated times. Cell lysates were immunoprecipitated using anti-TNFR1 antibody and immunoblotted with the indicated antibodies. b Sequential immunoprecipitation of HEK293T cells co-transfected with FLAG-TNFR1, DsRed-RIP1 and increasing amounts of V5-RARγ-NLSmut plasmids as indicated. First IP : cell lysates were immunoprecipitated with anti-FLAG (TNFR1) antibody. Second IP : the remaining lysates were then immunoprecipitated with anti-V5 (RARγ) antibody. The immunoprecipitated complexes were analyzed by with the indicated antibodies. c Sequential immunoprecipitation of HEK293T cells co-transfected with V5-RARγ-NLSmut, RIP1-Myc, and increasing amounts of DsRed-RIP3 plasmids as indicated. First IP : cell lysates were immunoprecipitated with anti-V5 (RARγ) antibody. Second IP : the remaining lysates were then immunoprecipitated with anti-DsRed (RIP3) antibody. The immunoprecipitated complexes were analyzed with the indicated antibodies. d WT and RIP3−/− MEFs treated with TSZ for the indicated times. Cell lysates were immunoprecipitated using anti-Caspase-8 antibody and immunoblotted with the indicated antibodies. All blots above are representative of one of three experiments

Article Snippet: Anti-RARγ (C-15) (sc-550) for human, anti-RARα (C-20) (sc-551), anti-caspase-8 (C-20) (sc-6136), anti-cIAP2 (sc7944) and anti-Fas (C-20) (sc-715) from Santa Cruz; anti-RIP1 (610459) and anti-FADD (610400) from BD Biosciences; anti-RARγ1 (ab5905) for mouse, anti-RIP3 (ab72106), anti-MLKL (ab184718) for human, anti-MLKL (ab172868) for mouse and anti-cIAP1 (ab2399) from Abcam; anti-RIP3 (2283) for mouse from ProSci, anti-TRADD (05-473) from Upstate; anti-TRAF2 (MAB3277) and anti-TNFR1 (AF-425-PB) from R&D; anti-Actin (A3853) (dilution 1:10,000), anti-FLAG (F9291) (dilution 1:5,000) and anti-GFP (G6539) (dilution 1:5 000) from Sigma; anti-V5 (R960-25) (dilution 1:5,000) from Invitrogen; anti-PARP1 (BML-SA250-0050) from Enzo Life Science; anti-GAPDH (NB300-22) (dilution 1:5,000) from Novus Biologicals; anti-cleaved caspase-8 (9496), anti-CYLD (4495), anti-RIP1 (137451) and anti-p-RIP1(65746) from Cell Signaling Technology; anti-DsRed (632392) (dilution 1:5,000) from Clontech.

Techniques: Immunoprecipitation, shRNA, Transfection

RARγ modulates TNF-induced RIP-initiated cell death. a TRADD is responsible for initiated TC or TCZ-induced cell death. b RARγ is essential for the transition from inflammatory signaling to death pathways in TNF-induced RIP1-initiated cell death. When RARγ is released from the nucleus in response to TNF under the conditions of cIAP inhibition, it initiates the formation of death complex IIa by dissociating RIP1 from TNFR1. When RIP1 recruits RIP3 to necrosome/complex IIb, RARγ is replaced from the complex

Journal: Nature Communications

Article Title: The cytoplasmic nuclear receptor RARγ controls RIP1 initiated cell death when cIAP activity is inhibited

doi: 10.1038/s41467-017-00496-6

Figure Lengend Snippet: RARγ modulates TNF-induced RIP-initiated cell death. a TRADD is responsible for initiated TC or TCZ-induced cell death. b RARγ is essential for the transition from inflammatory signaling to death pathways in TNF-induced RIP1-initiated cell death. When RARγ is released from the nucleus in response to TNF under the conditions of cIAP inhibition, it initiates the formation of death complex IIa by dissociating RIP1 from TNFR1. When RIP1 recruits RIP3 to necrosome/complex IIb, RARγ is replaced from the complex

Article Snippet: Anti-RARγ (C-15) (sc-550) for human, anti-RARα (C-20) (sc-551), anti-caspase-8 (C-20) (sc-6136), anti-cIAP2 (sc7944) and anti-Fas (C-20) (sc-715) from Santa Cruz; anti-RIP1 (610459) and anti-FADD (610400) from BD Biosciences; anti-RARγ1 (ab5905) for mouse, anti-RIP3 (ab72106), anti-MLKL (ab184718) for human, anti-MLKL (ab172868) for mouse and anti-cIAP1 (ab2399) from Abcam; anti-RIP3 (2283) for mouse from ProSci, anti-TRADD (05-473) from Upstate; anti-TRAF2 (MAB3277) and anti-TNFR1 (AF-425-PB) from R&D; anti-Actin (A3853) (dilution 1:10,000), anti-FLAG (F9291) (dilution 1:5,000) and anti-GFP (G6539) (dilution 1:5 000) from Sigma; anti-V5 (R960-25) (dilution 1:5,000) from Invitrogen; anti-PARP1 (BML-SA250-0050) from Enzo Life Science; anti-GAPDH (NB300-22) (dilution 1:5,000) from Novus Biologicals; anti-cleaved caspase-8 (9496), anti-CYLD (4495), anti-RIP1 (137451) and anti-p-RIP1(65746) from Cell Signaling Technology; anti-DsRed (632392) (dilution 1:5,000) from Clontech.

Techniques: Inhibition

Effect of MPs and Cd on fibrosis in mouse kidneys. ( A – C ): Representative images of Sirius Red staining and Masson staining of the kidney after MP and/or Cd exposure. a: Glomerulus, b: Renal tubule. ( B , C ): Quantitative analysis. ( D – G ): The levels of collagen type IV alpha 1 chain (COL4A1), transforming growth factor beta 1 (TGF-β1), and alpha smooth muscle actin (α-SMA) were detected using western blotting. ( D ): Representative western blot image; ( E – G ): Quantitative analysis. Data are presented as means ± SD from three independent experiments. ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared to the control group; # p < 0.05, ## p < 0.01, #### p < 0.0001 compared to the Cd group.

Journal: International Journal of Molecular Sciences

Article Title: Microplastics Exacerbate Cadmium-Induced Kidney Injury by Enhancing Oxidative Stress, Autophagy, Apoptosis, and Fibrosis

doi: 10.3390/ijms232214411

Figure Lengend Snippet: Effect of MPs and Cd on fibrosis in mouse kidneys. ( A – C ): Representative images of Sirius Red staining and Masson staining of the kidney after MP and/or Cd exposure. a: Glomerulus, b: Renal tubule. ( B , C ): Quantitative analysis. ( D – G ): The levels of collagen type IV alpha 1 chain (COL4A1), transforming growth factor beta 1 (TGF-β1), and alpha smooth muscle actin (α-SMA) were detected using western blotting. ( D ): Representative western blot image; ( E – G ): Quantitative analysis. Data are presented as means ± SD from three independent experiments. ** p < 0.01, *** p < 0.001, **** p < 0.0001 compared to the control group; # p < 0.05, ## p < 0.01, #### p < 0.0001 compared to the Cd group.

Article Snippet: Anti-microtubule associated protein 1 light chain 3 beta (LC3B) (#83506), anti-alpha smooth muscle actin (α-SMA) (#19245), anti-transforming growth factor beta 1 (TGF-β1) (#3711), anti-collagen type IV alpha 1 chain (COL4A1) (#50273), and anti-β-actin (#4970) antibodies were obtained from Cell Signaling Technology (Danvers, MA, USA).

Techniques: Staining, Western Blot

The expression of transporter associated with antigen processing 1 (TAP1) in pan-cancer. (A) TAP1 expression of 31 kinds of normal tissues downloaded from genotype-tissue expression (GTEx) database. (B) TAP1 expression in 21 kinds of cancer cell lines derived from the cancer cell line encyclopedia (CCLE). (C) TAP1 expression in tumor samples and the adjacent normal samples of 20 cancers derived from the TCGA. (D) TAP1 expression in tumor samples and normal samples of 27 cancers derived from the cancer genome atlas (TCGA) and GTEx database. * p < 0.05. ** p < 0.01. *** p < 0.001.

Journal: Frontiers in Molecular Biosciences

Article Title: Comprehensive Analysis of the Potential Immune-Related Biomarker Transporter Associated With Antigen Processing 1 That Inhibits Metastasis and Invasion of Ovarian Cancer Cells

doi: 10.3389/fmolb.2021.763958

Figure Lengend Snippet: The expression of transporter associated with antigen processing 1 (TAP1) in pan-cancer. (A) TAP1 expression of 31 kinds of normal tissues downloaded from genotype-tissue expression (GTEx) database. (B) TAP1 expression in 21 kinds of cancer cell lines derived from the cancer cell line encyclopedia (CCLE). (C) TAP1 expression in tumor samples and the adjacent normal samples of 20 cancers derived from the TCGA. (D) TAP1 expression in tumor samples and normal samples of 27 cancers derived from the cancer genome atlas (TCGA) and GTEx database. * p < 0.05. ** p < 0.01. *** p < 0.001.

Article Snippet: The membrane was incubated with the following primary antibodies TAP1 (1:3,000), MEF2A (1:2000, #12382-1-AP, Proteintech, United States), LEF1 (1:1000, #14972-1-AP, Proteintech), E-cadherin (1:10000, #20874-1-AP, Proteintech), vimentin (1:2000, #10366-1-AP, Proteintech), and beta actin (1:1000, # 20536-1-AP, Proteintech).

Techniques: Expressing, Derivative Assay

The prediction ability of transporter associated with antigen processing 1 (TAP1) in pan-cancer prognosis. (A–C) The top three cancers correlated with TAP1 in disease-free survival (DFS). (D–F) The top three cancers correlated with TAP1 in disease-specific survival (DSS). (G–I) The top three cancers correlated with TAP1 in progression-free survival (PFS). (J–L) The top three cancers correlated with TAP1 in Overall survival (OS).

Journal: Frontiers in Molecular Biosciences

Article Title: Comprehensive Analysis of the Potential Immune-Related Biomarker Transporter Associated With Antigen Processing 1 That Inhibits Metastasis and Invasion of Ovarian Cancer Cells

doi: 10.3389/fmolb.2021.763958

Figure Lengend Snippet: The prediction ability of transporter associated with antigen processing 1 (TAP1) in pan-cancer prognosis. (A–C) The top three cancers correlated with TAP1 in disease-free survival (DFS). (D–F) The top three cancers correlated with TAP1 in disease-specific survival (DSS). (G–I) The top three cancers correlated with TAP1 in progression-free survival (PFS). (J–L) The top three cancers correlated with TAP1 in Overall survival (OS).

Article Snippet: The membrane was incubated with the following primary antibodies TAP1 (1:3,000), MEF2A (1:2000, #12382-1-AP, Proteintech, United States), LEF1 (1:1000, #14972-1-AP, Proteintech), E-cadherin (1:10000, #20874-1-AP, Proteintech), vimentin (1:2000, #10366-1-AP, Proteintech), and beta actin (1:1000, # 20536-1-AP, Proteintech).

Techniques:

The correlation of transporter associated with antigen processing 1 (TAP1) with immune infiltration in multiple cancers. The top three cancers with the strongest correlation with 6 immune infiltration cells which included B cells, CD4+T cells, CD8+T cells, neutrophils, macrophages, and dendritic cells. The cancers were colon adenocarcinoma (COAD), kidney renal clear cell carcinoma (KIRC), and breast invasive carcinoma (BRCA), respectively.

Journal: Frontiers in Molecular Biosciences

Article Title: Comprehensive Analysis of the Potential Immune-Related Biomarker Transporter Associated With Antigen Processing 1 That Inhibits Metastasis and Invasion of Ovarian Cancer Cells

doi: 10.3389/fmolb.2021.763958

Figure Lengend Snippet: The correlation of transporter associated with antigen processing 1 (TAP1) with immune infiltration in multiple cancers. The top three cancers with the strongest correlation with 6 immune infiltration cells which included B cells, CD4+T cells, CD8+T cells, neutrophils, macrophages, and dendritic cells. The cancers were colon adenocarcinoma (COAD), kidney renal clear cell carcinoma (KIRC), and breast invasive carcinoma (BRCA), respectively.

Article Snippet: The membrane was incubated with the following primary antibodies TAP1 (1:3,000), MEF2A (1:2000, #12382-1-AP, Proteintech, United States), LEF1 (1:1000, #14972-1-AP, Proteintech), E-cadherin (1:10000, #20874-1-AP, Proteintech), vimentin (1:2000, #10366-1-AP, Proteintech), and beta actin (1:1000, # 20536-1-AP, Proteintech).

Techniques:

The relationship between TAP1 and ESTIMATE score in multiple cancers. The ESTIMATE score was used to determine the correlation of TAP1 with immune cells and stromal cells in 33 tumors. TAP1 was positively correlated with ESTIMATE scores in cervical squamous cell carcinoma (CESC), ovarian cancer (OC), uveal melanoma (UVM), testicular germ cell tumors (TGCT), and thyroid carcinoma (THCA) ( p < 0.05).

Journal: Frontiers in Molecular Biosciences

Article Title: Comprehensive Analysis of the Potential Immune-Related Biomarker Transporter Associated With Antigen Processing 1 That Inhibits Metastasis and Invasion of Ovarian Cancer Cells

doi: 10.3389/fmolb.2021.763958

Figure Lengend Snippet: The relationship between TAP1 and ESTIMATE score in multiple cancers. The ESTIMATE score was used to determine the correlation of TAP1 with immune cells and stromal cells in 33 tumors. TAP1 was positively correlated with ESTIMATE scores in cervical squamous cell carcinoma (CESC), ovarian cancer (OC), uveal melanoma (UVM), testicular germ cell tumors (TGCT), and thyroid carcinoma (THCA) ( p < 0.05).

Article Snippet: The membrane was incubated with the following primary antibodies TAP1 (1:3,000), MEF2A (1:2000, #12382-1-AP, Proteintech, United States), LEF1 (1:1000, #14972-1-AP, Proteintech), E-cadherin (1:10000, #20874-1-AP, Proteintech), vimentin (1:2000, #10366-1-AP, Proteintech), and beta actin (1:1000, # 20536-1-AP, Proteintech).

Techniques:

The relationship between transporter associated with antigen processing 1 (TAP1) and immune checkpoint therapy in multiple cancers. (A) The relationship between TAP1 and 47 immune checkpoint genes. Color green represented negative correlation with TAP1 and color red represented positive correlation with TAP1. (B) The correlation of TAP1 with tumor mutation burden (TMB). (C) The correlation of TAP1 with microsatellite instability (MSI). * p < 0.05. ** p < 0.01. *** p < 0.001.

Journal: Frontiers in Molecular Biosciences

Article Title: Comprehensive Analysis of the Potential Immune-Related Biomarker Transporter Associated With Antigen Processing 1 That Inhibits Metastasis and Invasion of Ovarian Cancer Cells

doi: 10.3389/fmolb.2021.763958

Figure Lengend Snippet: The relationship between transporter associated with antigen processing 1 (TAP1) and immune checkpoint therapy in multiple cancers. (A) The relationship between TAP1 and 47 immune checkpoint genes. Color green represented negative correlation with TAP1 and color red represented positive correlation with TAP1. (B) The correlation of TAP1 with tumor mutation burden (TMB). (C) The correlation of TAP1 with microsatellite instability (MSI). * p < 0.05. ** p < 0.01. *** p < 0.001.

Article Snippet: The membrane was incubated with the following primary antibodies TAP1 (1:3,000), MEF2A (1:2000, #12382-1-AP, Proteintech, United States), LEF1 (1:1000, #14972-1-AP, Proteintech), E-cadherin (1:10000, #20874-1-AP, Proteintech), vimentin (1:2000, #10366-1-AP, Proteintech), and beta actin (1:1000, # 20536-1-AP, Proteintech).

Techniques: Mutagenesis

The relationship between transporter associated with antigen processing 1 (TAP1) and neoantigen in various cancers. TAP1 was positively related to neoantigens in ovarian cancer (OC), cervical squamous cell carcinoma (CESC), lung adenocarcinoma (LUAD), breast invasive carcinoma (BRCA), skin cutaneous melanoma (SKCM), and brain lower grade glioma (LGG) ( p < 0.05), whereas it was negatively correlated in colon adenocarcinoma (COAD) and rectum adenocarcinoma (READ).

Journal: Frontiers in Molecular Biosciences

Article Title: Comprehensive Analysis of the Potential Immune-Related Biomarker Transporter Associated With Antigen Processing 1 That Inhibits Metastasis and Invasion of Ovarian Cancer Cells

doi: 10.3389/fmolb.2021.763958

Figure Lengend Snippet: The relationship between transporter associated with antigen processing 1 (TAP1) and neoantigen in various cancers. TAP1 was positively related to neoantigens in ovarian cancer (OC), cervical squamous cell carcinoma (CESC), lung adenocarcinoma (LUAD), breast invasive carcinoma (BRCA), skin cutaneous melanoma (SKCM), and brain lower grade glioma (LGG) ( p < 0.05), whereas it was negatively correlated in colon adenocarcinoma (COAD) and rectum adenocarcinoma (READ).

Article Snippet: The membrane was incubated with the following primary antibodies TAP1 (1:3,000), MEF2A (1:2000, #12382-1-AP, Proteintech, United States), LEF1 (1:1000, #14972-1-AP, Proteintech), E-cadherin (1:10000, #20874-1-AP, Proteintech), vimentin (1:2000, #10366-1-AP, Proteintech), and beta actin (1:1000, # 20536-1-AP, Proteintech).

Techniques: Immunopeptidomics

Correlation of transporter associated with antigen processing 1 (TAP1) expression with the prognosis of ovarian cancer (OC) and cervical cancer (CC). (A) Immunohistochemical (IHC) analysis of transporter associated with antigen processing 1 (TAP1) protein expression in OC tissues. Original magnifications:×200 and ×400. i represents strong positive staining, ii represents moderately positive staining, and iii represents weakly positive staining. (B) IHC analysis of TAP1 protein expression in CC tissues. Original magnifications:×200 and ×400. i represents strong positive staining, ii represents moderately positive staining, and iii represents weakly positive staining. Scale bars 200 μm. (C) 5-Year Kaplan–Meier analysis of overall survival in OC patients on the basis of TAP1 protein expression. (D) 5-Year Kaplan–Meier analysis of overall survival in CC patients on the basis of the TAP1 protein expression. (E) The protein-protein interaction (PPI) network of TAP1 and top 26 correlated transcription factors (TFs) were identified using STRING ( https://string-db.org/cgi/input.pl ). Color blue represented TFs negatively correlated with TAP1, color red represented TFs positively correlated with TAP1, and color white represented TFs significantly correlated with the top 26 TFs in enrichment analysis. (F) Gene set enrichment analysis of transporter associated with antigen processing 1 (TAP1) and pivotal TFs in OC. (G) TAP1, MEF2A, LEF1, and β-actin protein expression in normal cell lines and cancer cell lines. Error bars represent the SD of triplicate measurements. * p < 0.05; ** p < 0.01; *** p < 0.001.

Journal: Frontiers in Molecular Biosciences

Article Title: Comprehensive Analysis of the Potential Immune-Related Biomarker Transporter Associated With Antigen Processing 1 That Inhibits Metastasis and Invasion of Ovarian Cancer Cells

doi: 10.3389/fmolb.2021.763958

Figure Lengend Snippet: Correlation of transporter associated with antigen processing 1 (TAP1) expression with the prognosis of ovarian cancer (OC) and cervical cancer (CC). (A) Immunohistochemical (IHC) analysis of transporter associated with antigen processing 1 (TAP1) protein expression in OC tissues. Original magnifications:×200 and ×400. i represents strong positive staining, ii represents moderately positive staining, and iii represents weakly positive staining. (B) IHC analysis of TAP1 protein expression in CC tissues. Original magnifications:×200 and ×400. i represents strong positive staining, ii represents moderately positive staining, and iii represents weakly positive staining. Scale bars 200 μm. (C) 5-Year Kaplan–Meier analysis of overall survival in OC patients on the basis of TAP1 protein expression. (D) 5-Year Kaplan–Meier analysis of overall survival in CC patients on the basis of the TAP1 protein expression. (E) The protein-protein interaction (PPI) network of TAP1 and top 26 correlated transcription factors (TFs) were identified using STRING ( https://string-db.org/cgi/input.pl ). Color blue represented TFs negatively correlated with TAP1, color red represented TFs positively correlated with TAP1, and color white represented TFs significantly correlated with the top 26 TFs in enrichment analysis. (F) Gene set enrichment analysis of transporter associated with antigen processing 1 (TAP1) and pivotal TFs in OC. (G) TAP1, MEF2A, LEF1, and β-actin protein expression in normal cell lines and cancer cell lines. Error bars represent the SD of triplicate measurements. * p < 0.05; ** p < 0.01; *** p < 0.001.

Article Snippet: The membrane was incubated with the following primary antibodies TAP1 (1:3,000), MEF2A (1:2000, #12382-1-AP, Proteintech, United States), LEF1 (1:1000, #14972-1-AP, Proteintech), E-cadherin (1:10000, #20874-1-AP, Proteintech), vimentin (1:2000, #10366-1-AP, Proteintech), and beta actin (1:1000, # 20536-1-AP, Proteintech).

Techniques: Expressing, Immunohistochemical staining, Staining

Downregulation of transporter associated with antigen processing 1 (TAP1) reduces the invasion and migration in ovarian cancer cells. (A) The volcano map of TAP1-related pathways by gene set variation analysis. (B) Enriching pathway analysis in ovarian cancer of TAP1. (C) The migration abilities of OVCAR3 and SKOV3 were photographed (i, ii) and measured (iii) by examining the wound closure after TAP1 knockdown using wound healing assays. Original magnifications, ×100. Scale bars 150 μm. (D) Transwell assays were photographed (i) and measured (ii) to detect the migration abilities after TAP1 knockdown in SKOV3 and OVCAR3 cells. Original magnifications, ×200. Scale bars 100 μm. (E) Colony formation assays were photographed (i) and measured (ii) to detect the proliferation abilities after TAP1 knockdown in SKOV3 and OVCAR3 cells. (F) Effects of TAP1 knockdown on migration-associated protein (E-cadherin and vimentin) and transcription factor (MEF2A and LEF1) were analyzed by western blotting in SKOV3 and OVCAR3 cells (i). Error bars of histogram (ii) represented the SD of triplicate measurements. * p < 0.05; ** p < 0.01; *** p < 0.001.

Journal: Frontiers in Molecular Biosciences

Article Title: Comprehensive Analysis of the Potential Immune-Related Biomarker Transporter Associated With Antigen Processing 1 That Inhibits Metastasis and Invasion of Ovarian Cancer Cells

doi: 10.3389/fmolb.2021.763958

Figure Lengend Snippet: Downregulation of transporter associated with antigen processing 1 (TAP1) reduces the invasion and migration in ovarian cancer cells. (A) The volcano map of TAP1-related pathways by gene set variation analysis. (B) Enriching pathway analysis in ovarian cancer of TAP1. (C) The migration abilities of OVCAR3 and SKOV3 were photographed (i, ii) and measured (iii) by examining the wound closure after TAP1 knockdown using wound healing assays. Original magnifications, ×100. Scale bars 150 μm. (D) Transwell assays were photographed (i) and measured (ii) to detect the migration abilities after TAP1 knockdown in SKOV3 and OVCAR3 cells. Original magnifications, ×200. Scale bars 100 μm. (E) Colony formation assays were photographed (i) and measured (ii) to detect the proliferation abilities after TAP1 knockdown in SKOV3 and OVCAR3 cells. (F) Effects of TAP1 knockdown on migration-associated protein (E-cadherin and vimentin) and transcription factor (MEF2A and LEF1) were analyzed by western blotting in SKOV3 and OVCAR3 cells (i). Error bars of histogram (ii) represented the SD of triplicate measurements. * p < 0.05; ** p < 0.01; *** p < 0.001.

Article Snippet: The membrane was incubated with the following primary antibodies TAP1 (1:3,000), MEF2A (1:2000, #12382-1-AP, Proteintech, United States), LEF1 (1:1000, #14972-1-AP, Proteintech), E-cadherin (1:10000, #20874-1-AP, Proteintech), vimentin (1:2000, #10366-1-AP, Proteintech), and beta actin (1:1000, # 20536-1-AP, Proteintech).

Techniques: Migration, Knockdown, Western Blot

To establish the model of tumor metastasis, SKOV3 cells were injected into nude mice by the i.p. route and randomly treated with si-TAP1_01 or si-NC ( n = 4/group). (A) Representative images of metastatic tumors in the peritoneal cavity. Yellow arrows and rectangles highlighted visible tumor nodes and liver metastasis. (B,C) Number of metastasis and total weight of all metastases were shown (mean ± SEM). (D) Body weight growth of all mice were shown (mean ± SEM). (E) The protein expression of migration-associated protein (E-cadherin and vimentin) and transcription factor (MEF2A and LEF1) in the tumor of si-TAP1_01 group and si-NC group (i). Error bars of histogram (ii) represented the SD of quadruplicate measurements. * p < 0.05; ** p < 0.01; *** p < 0.001.

Journal: Frontiers in Molecular Biosciences

Article Title: Comprehensive Analysis of the Potential Immune-Related Biomarker Transporter Associated With Antigen Processing 1 That Inhibits Metastasis and Invasion of Ovarian Cancer Cells

doi: 10.3389/fmolb.2021.763958

Figure Lengend Snippet: To establish the model of tumor metastasis, SKOV3 cells were injected into nude mice by the i.p. route and randomly treated with si-TAP1_01 or si-NC ( n = 4/group). (A) Representative images of metastatic tumors in the peritoneal cavity. Yellow arrows and rectangles highlighted visible tumor nodes and liver metastasis. (B,C) Number of metastasis and total weight of all metastases were shown (mean ± SEM). (D) Body weight growth of all mice were shown (mean ± SEM). (E) The protein expression of migration-associated protein (E-cadherin and vimentin) and transcription factor (MEF2A and LEF1) in the tumor of si-TAP1_01 group and si-NC group (i). Error bars of histogram (ii) represented the SD of quadruplicate measurements. * p < 0.05; ** p < 0.01; *** p < 0.001.

Article Snippet: The membrane was incubated with the following primary antibodies TAP1 (1:3,000), MEF2A (1:2000, #12382-1-AP, Proteintech, United States), LEF1 (1:1000, #14972-1-AP, Proteintech), E-cadherin (1:10000, #20874-1-AP, Proteintech), vimentin (1:2000, #10366-1-AP, Proteintech), and beta actin (1:1000, # 20536-1-AP, Proteintech).

Techniques: Injection, Expressing, Migration