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USP25 interacts with RIPK1 through the USP domain. (A) Schematic diagram of the proteomic screening for USP25-interacting proteins. (B) Two-dimensional plot of USP25-binding proteins, with the Y axis showing protein intensity and the X axis showing protein molecular weight. (C) List of potential substrates with unique peptides ≥2 identified by the mass spectrometry analysis. (D–E) Whole cell lysates of BMDMs were immunoprecipitated with anti-USP25 (D) or anti-RIPK1 (E) antibodies, followed by Western blot analysis. Rabbit IgG served as negative control. (F–G) HEK293 cells were co-transfected with <t>FLAG-USP25</t> and MYC-RIPK1 plasmids for 24 h. Whole-cell lysates were immunoprecipitated with <t>anti-FLAG</t> (F) or anti-MYC (G) antibodies, followed by Western blot analysis. (H) BMDMs were left untreated or treated with ox-LDL (50 μg/mL) for 30 min before lysis. Whole-cell lysates were immunoprecipitated with anti-USP25 antibody, followed by Western blot analysis. (I) Subcellular distribution of USP25 (red) and RIPK1 (green) in BMDMs treated with or without ox-LDL (50 μg/mL) for 30 min was detected by immunofluorescence. Scale bar: 5 μm. (J) Schematic diagram of structural domains and truncation mutants of USP25. (K) HEK293 cells were co-transfected with indicated plasmids for 24 h. Cell lysates were immunoprecipitated with anti-FLAG antibody and further analysed by Western blot with indicated antibodies.
Antibodies Against Flag, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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USP25 interacts with RIPK1 through the USP domain. (A) Schematic diagram of the proteomic screening for USP25-interacting proteins. (B) Two-dimensional plot of USP25-binding proteins, with the Y axis showing protein intensity and the X axis showing protein molecular weight. (C) List of potential substrates with unique peptides ≥2 identified by the mass spectrometry analysis. (D–E) Whole cell lysates of BMDMs were immunoprecipitated with anti-USP25 (D) or anti-RIPK1 (E) antibodies, followed by Western blot analysis. Rabbit IgG served as negative control. (F–G) HEK293 cells were co-transfected with <t>FLAG-USP25</t> and MYC-RIPK1 plasmids for 24 h. Whole-cell lysates were immunoprecipitated with <t>anti-FLAG</t> (F) or anti-MYC (G) antibodies, followed by Western blot analysis. (H) BMDMs were left untreated or treated with ox-LDL (50 μg/mL) for 30 min before lysis. Whole-cell lysates were immunoprecipitated with anti-USP25 antibody, followed by Western blot analysis. (I) Subcellular distribution of USP25 (red) and RIPK1 (green) in BMDMs treated with or without ox-LDL (50 μg/mL) for 30 min was detected by immunofluorescence. Scale bar: 5 μm. (J) Schematic diagram of structural domains and truncation mutants of USP25. (K) HEK293 cells were co-transfected with indicated plasmids for 24 h. Cell lysates were immunoprecipitated with anti-FLAG antibody and further analysed by Western blot with indicated antibodies.
2 Ig Anti Lamin B Antibody Proteintech, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti c myc antibodies  (Proteintech)
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USP25 interacts with RIPK1 through the USP domain. (A) Schematic diagram of the proteomic screening for USP25-interacting proteins. (B) Two-dimensional plot of USP25-binding proteins, with the Y axis showing protein intensity and the X axis showing protein molecular weight. (C) List of potential substrates with unique peptides ≥2 identified by the mass spectrometry analysis. (D–E) Whole cell lysates of BMDMs were immunoprecipitated with anti-USP25 (D) or anti-RIPK1 (E) antibodies, followed by Western blot analysis. Rabbit IgG served as negative control. (F–G) HEK293 cells were co-transfected with <t>FLAG-USP25</t> and MYC-RIPK1 plasmids for 24 h. Whole-cell lysates were immunoprecipitated with <t>anti-FLAG</t> (F) or anti-MYC (G) antibodies, followed by Western blot analysis. (H) BMDMs were left untreated or treated with ox-LDL (50 μg/mL) for 30 min before lysis. Whole-cell lysates were immunoprecipitated with anti-USP25 antibody, followed by Western blot analysis. (I) Subcellular distribution of USP25 (red) and RIPK1 (green) in BMDMs treated with or without ox-LDL (50 μg/mL) for 30 min was detected by immunofluorescence. Scale bar: 5 μm. (J) Schematic diagram of structural domains and truncation mutants of USP25. (K) HEK293 cells were co-transfected with indicated plasmids for 24 h. Cell lysates were immunoprecipitated with anti-FLAG antibody and further analysed by Western blot with indicated antibodies.
Anti C Myc Antibodies, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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anti sirt2 antibodies  (Proteintech)
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USP25 interacts with RIPK1 through the USP domain. (A) Schematic diagram of the proteomic screening for USP25-interacting proteins. (B) Two-dimensional plot of USP25-binding proteins, with the Y axis showing protein intensity and the X axis showing protein molecular weight. (C) List of potential substrates with unique peptides ≥2 identified by the mass spectrometry analysis. (D–E) Whole cell lysates of BMDMs were immunoprecipitated with anti-USP25 (D) or anti-RIPK1 (E) antibodies, followed by Western blot analysis. Rabbit IgG served as negative control. (F–G) HEK293 cells were co-transfected with <t>FLAG-USP25</t> and MYC-RIPK1 plasmids for 24 h. Whole-cell lysates were immunoprecipitated with <t>anti-FLAG</t> (F) or anti-MYC (G) antibodies, followed by Western blot analysis. (H) BMDMs were left untreated or treated with ox-LDL (50 μg/mL) for 30 min before lysis. Whole-cell lysates were immunoprecipitated with anti-USP25 antibody, followed by Western blot analysis. (I) Subcellular distribution of USP25 (red) and RIPK1 (green) in BMDMs treated with or without ox-LDL (50 μg/mL) for 30 min was detected by immunofluorescence. Scale bar: 5 μm. (J) Schematic diagram of structural domains and truncation mutants of USP25. (K) HEK293 cells were co-transfected with indicated plasmids for 24 h. Cell lysates were immunoprecipitated with anti-FLAG antibody and further analysed by Western blot with indicated antibodies.
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USP25 interacts with RIPK1 through the USP domain. (A) Schematic diagram of the proteomic screening for USP25-interacting proteins. (B) Two-dimensional plot of USP25-binding proteins, with the Y axis showing protein intensity and the X axis showing protein molecular weight. (C) List of potential substrates with unique peptides ≥2 identified by the mass spectrometry analysis. (D–E) Whole cell lysates of BMDMs were immunoprecipitated with anti-USP25 (D) or anti-RIPK1 (E) antibodies, followed by Western blot analysis. Rabbit IgG served as negative control. (F–G) HEK293 cells were co-transfected with <t>FLAG-USP25</t> and MYC-RIPK1 plasmids for 24 h. Whole-cell lysates were immunoprecipitated with <t>anti-FLAG</t> (F) or anti-MYC (G) antibodies, followed by Western blot analysis. (H) BMDMs were left untreated or treated with ox-LDL (50 μg/mL) for 30 min before lysis. Whole-cell lysates were immunoprecipitated with anti-USP25 antibody, followed by Western blot analysis. (I) Subcellular distribution of USP25 (red) and RIPK1 (green) in BMDMs treated with or without ox-LDL (50 μg/mL) for 30 min was detected by immunofluorescence. Scale bar: 5 μm. (J) Schematic diagram of structural domains and truncation mutants of USP25. (K) HEK293 cells were co-transfected with indicated plasmids for 24 h. Cell lysates were immunoprecipitated with anti-FLAG antibody and further analysed by Western blot with indicated antibodies.
Anti Myc, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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USP25 interacts with RIPK1 through the USP domain. (A) Schematic diagram of the proteomic screening for USP25-interacting proteins. (B) Two-dimensional plot of USP25-binding proteins, with the Y axis showing protein intensity and the X axis showing protein molecular weight. (C) List of potential substrates with unique peptides ≥2 identified by the mass spectrometry analysis. (D–E) Whole cell lysates of BMDMs were immunoprecipitated with anti-USP25 (D) or anti-RIPK1 (E) antibodies, followed by Western blot analysis. Rabbit IgG served as negative control. (F–G) HEK293 cells were co-transfected with <t>FLAG-USP25</t> and MYC-RIPK1 plasmids for 24 h. Whole-cell lysates were immunoprecipitated with <t>anti-FLAG</t> (F) or anti-MYC (G) antibodies, followed by Western blot analysis. (H) BMDMs were left untreated or treated with ox-LDL (50 μg/mL) for 30 min before lysis. Whole-cell lysates were immunoprecipitated with anti-USP25 antibody, followed by Western blot analysis. (I) Subcellular distribution of USP25 (red) and RIPK1 (green) in BMDMs treated with or without ox-LDL (50 μg/mL) for 30 min was detected by immunofluorescence. Scale bar: 5 μm. (J) Schematic diagram of structural domains and truncation mutants of USP25. (K) HEK293 cells were co-transfected with indicated plasmids for 24 h. Cell lysates were immunoprecipitated with anti-FLAG antibody and further analysed by Western blot with indicated antibodies.
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USP25 interacts with RIPK1 through the USP domain. (A) Schematic diagram of the proteomic screening for USP25-interacting proteins. (B) Two-dimensional plot of USP25-binding proteins, with the Y axis showing protein intensity and the X axis showing protein molecular weight. (C) List of potential substrates with unique peptides ≥2 identified by the mass spectrometry analysis. (D–E) Whole cell lysates of BMDMs were immunoprecipitated with anti-USP25 (D) or anti-RIPK1 (E) antibodies, followed by Western blot analysis. Rabbit IgG served as negative control. (F–G) HEK293 cells were co-transfected with <t>FLAG-USP25</t> and MYC-RIPK1 plasmids for 24 h. Whole-cell lysates were immunoprecipitated with <t>anti-FLAG</t> (F) or anti-MYC (G) antibodies, followed by Western blot analysis. (H) BMDMs were left untreated or treated with ox-LDL (50 μg/mL) for 30 min before lysis. Whole-cell lysates were immunoprecipitated with anti-USP25 antibody, followed by Western blot analysis. (I) Subcellular distribution of USP25 (red) and RIPK1 (green) in BMDMs treated with or without ox-LDL (50 μg/mL) for 30 min was detected by immunofluorescence. Scale bar: 5 μm. (J) Schematic diagram of structural domains and truncation mutants of USP25. (K) HEK293 cells were co-transfected with indicated plasmids for 24 h. Cell lysates were immunoprecipitated with anti-FLAG antibody and further analysed by Western blot with indicated antibodies.
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USP25 interacts with RIPK1 through the USP domain. (A) Schematic diagram of the proteomic screening for USP25-interacting proteins. (B) Two-dimensional plot of USP25-binding proteins, with the Y axis showing protein intensity and the X axis showing protein molecular weight. (C) List of potential substrates with unique peptides ≥2 identified by the mass spectrometry analysis. (D–E) Whole cell lysates of BMDMs were immunoprecipitated with anti-USP25 (D) or anti-RIPK1 (E) antibodies, followed by Western blot analysis. Rabbit IgG served as negative control. (F–G) HEK293 cells were co-transfected with FLAG-USP25 and MYC-RIPK1 plasmids for 24 h. Whole-cell lysates were immunoprecipitated with anti-FLAG (F) or anti-MYC (G) antibodies, followed by Western blot analysis. (H) BMDMs were left untreated or treated with ox-LDL (50 μg/mL) for 30 min before lysis. Whole-cell lysates were immunoprecipitated with anti-USP25 antibody, followed by Western blot analysis. (I) Subcellular distribution of USP25 (red) and RIPK1 (green) in BMDMs treated with or without ox-LDL (50 μg/mL) for 30 min was detected by immunofluorescence. Scale bar: 5 μm. (J) Schematic diagram of structural domains and truncation mutants of USP25. (K) HEK293 cells were co-transfected with indicated plasmids for 24 h. Cell lysates were immunoprecipitated with anti-FLAG antibody and further analysed by Western blot with indicated antibodies.

Journal: eBioMedicine

Article Title: USP25 regulates atherosclerosis by restricting RIPK1-mediated inflammatory responses

doi: 10.1016/j.ebiom.2026.106213

Figure Lengend Snippet: USP25 interacts with RIPK1 through the USP domain. (A) Schematic diagram of the proteomic screening for USP25-interacting proteins. (B) Two-dimensional plot of USP25-binding proteins, with the Y axis showing protein intensity and the X axis showing protein molecular weight. (C) List of potential substrates with unique peptides ≥2 identified by the mass spectrometry analysis. (D–E) Whole cell lysates of BMDMs were immunoprecipitated with anti-USP25 (D) or anti-RIPK1 (E) antibodies, followed by Western blot analysis. Rabbit IgG served as negative control. (F–G) HEK293 cells were co-transfected with FLAG-USP25 and MYC-RIPK1 plasmids for 24 h. Whole-cell lysates were immunoprecipitated with anti-FLAG (F) or anti-MYC (G) antibodies, followed by Western blot analysis. (H) BMDMs were left untreated or treated with ox-LDL (50 μg/mL) for 30 min before lysis. Whole-cell lysates were immunoprecipitated with anti-USP25 antibody, followed by Western blot analysis. (I) Subcellular distribution of USP25 (red) and RIPK1 (green) in BMDMs treated with or without ox-LDL (50 μg/mL) for 30 min was detected by immunofluorescence. Scale bar: 5 μm. (J) Schematic diagram of structural domains and truncation mutants of USP25. (K) HEK293 cells were co-transfected with indicated plasmids for 24 h. Cell lysates were immunoprecipitated with anti-FLAG antibody and further analysed by Western blot with indicated antibodies.

Article Snippet: Antibodies against FLAG (Cat#: 20543-1-AP, 1: 1000, RRID: AB_11232216 ), MYC (Cat#: 60003-2-Ig, 1: 1000, RRID: AB_2734122 ), HA (Cat#: 51064-2-AP, 1: 1000, RRID: AB_11042321 ), CD36 (Cat#: 18836-1-AP, 1:1000, RRID: AB_10597244 ), ASK1 (Cat#: 28201-1-AP, 1: 1000, RRID: AB_2782957 ), MLKL (Cat#: 66675-1-Ig, 1:1000, RRID: AB_2882029 ), and p-ASK1 (Cat#: 28846-1-AP, 1: 1000, RRID: AB_2881220 ) were purchased from Proteintech (Wuhan, China).

Techniques: Binding Assay, Molecular Weight, Mass Spectrometry, Immunoprecipitation, Western Blot, Negative Control, Transfection, Lysis, Immunofluorescence