chip grade anti h3k18la Search Results


chip grade anti h3k18la  (Proteintech)
96
Proteintech chip grade anti h3k18la
<t>H3K18la</t> binds to the KRT19 promoter to upregulate KRT19 expression in NSCLC cells A The protein expression of H3K18la in clinical NSCLC tissues and paired normal tissues ( n = 3) were determined by immunoblot B ChIP-seq <t>with</t> <t>anti-H3K18la</t> was performed on NCI-H1299 cells, and input was served as control. IGV tracks for KRT19 from ChIP-seq data ( GSE245990 ) were shown C A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 16 h, the binding of H3K18la to the KRT19 promoter regions (a, b) in control and lactate-treated A549 cells was determined by ChIP-PCR D PC-9 cells were treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 16 h. The enrichment of H3K18la in the KRT19 promoter regions (a, b) in different groups of PC-9 cells was measured by ChIP-PCR E A549 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and then stimulated with or without lactate (40 mM, LA group) for another 16 h, the luciferase activities were determined F PC-9 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and treated with or without 2-DG (20 mM) or oxamate (10 mM, Oxa) for another 16 h. The luciferase activities were determined G-H A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 24 h, KRT19 mRNA (G) and protein (H) expression was determined by RT-PCR and immunoblot, respectively I-J KRT19 mRNA (I) and protein (J) levels in PC-9 cells treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 24 h were measured K-L PC-9 cells were transfected with siLDHA and siLDHB (siLDHA/B group) or control siRNA (si-NC group) K KRT19 mRNA expression in PC-9 cells (si-NC, siLDHA/B) was determined by RT-PCR L KRT19, LDHA, LDHB and H3K18la protein levels in different groups of PC-9 cells were measured using immunoblot. Data are shown as mean ± S.E.M. and analyzed by Student’s t -test (A, C-L). * p < 0.05; ** p < 0.01; *** p < 0.001. All experiments were repeated two (B) or three times (C-L)
Chip Grade Anti H3k18la, 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
https://www.bioz.com/product/chip+grade+anti+h3k18la/pmc12802155-102-6-15?v=Proteintech
Average 96 stars, based on 1 article reviews
chip grade anti h3k18la - by Bioz Stars, 2026-08
96/100 stars
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anti-p53  (CancerTools Org)
99
CancerTools Org anti-p53
<t>H3K18la</t> binds to the KRT19 promoter to upregulate KRT19 expression in NSCLC cells A The protein expression of H3K18la in clinical NSCLC tissues and paired normal tissues ( n = 3) were determined by immunoblot B ChIP-seq <t>with</t> <t>anti-H3K18la</t> was performed on NCI-H1299 cells, and input was served as control. IGV tracks for KRT19 from ChIP-seq data ( GSE245990 ) were shown C A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 16 h, the binding of H3K18la to the KRT19 promoter regions (a, b) in control and lactate-treated A549 cells was determined by ChIP-PCR D PC-9 cells were treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 16 h. The enrichment of H3K18la in the KRT19 promoter regions (a, b) in different groups of PC-9 cells was measured by ChIP-PCR E A549 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and then stimulated with or without lactate (40 mM, LA group) for another 16 h, the luciferase activities were determined F PC-9 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and treated with or without 2-DG (20 mM) or oxamate (10 mM, Oxa) for another 16 h. The luciferase activities were determined G-H A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 24 h, KRT19 mRNA (G) and protein (H) expression was determined by RT-PCR and immunoblot, respectively I-J KRT19 mRNA (I) and protein (J) levels in PC-9 cells treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 24 h were measured K-L PC-9 cells were transfected with siLDHA and siLDHB (siLDHA/B group) or control siRNA (si-NC group) K KRT19 mRNA expression in PC-9 cells (si-NC, siLDHA/B) was determined by RT-PCR L KRT19, LDHA, LDHB and H3K18la protein levels in different groups of PC-9 cells were measured using immunoblot. Data are shown as mean ± S.E.M. and analyzed by Student’s t -test (A, C-L). * p < 0.05; ** p < 0.01; *** p < 0.001. All experiments were repeated two (B) or three times (C-L)
Anti P53, supplied by CancerTools Org, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/chip+grade+anti+h3k18la/custom%40151142%4041345704?v=CancerTools+Org
Average 99 stars, based on 1 article reviews
anti-p53 - by Bioz Stars, 2026-08
99/100 stars
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anti-h3k9ac antibody  (PTM Biolabs)
90
PTM Biolabs anti-h3k9ac antibody
<t>H3K18la</t> binds to the KRT19 promoter to upregulate KRT19 expression in NSCLC cells A The protein expression of H3K18la in clinical NSCLC tissues and paired normal tissues ( n = 3) were determined by immunoblot B ChIP-seq <t>with</t> <t>anti-H3K18la</t> was performed on NCI-H1299 cells, and input was served as control. IGV tracks for KRT19 from ChIP-seq data ( GSE245990 ) were shown C A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 16 h, the binding of H3K18la to the KRT19 promoter regions (a, b) in control and lactate-treated A549 cells was determined by ChIP-PCR D PC-9 cells were treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 16 h. The enrichment of H3K18la in the KRT19 promoter regions (a, b) in different groups of PC-9 cells was measured by ChIP-PCR E A549 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and then stimulated with or without lactate (40 mM, LA group) for another 16 h, the luciferase activities were determined F PC-9 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and treated with or without 2-DG (20 mM) or oxamate (10 mM, Oxa) for another 16 h. The luciferase activities were determined G-H A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 24 h, KRT19 mRNA (G) and protein (H) expression was determined by RT-PCR and immunoblot, respectively I-J KRT19 mRNA (I) and protein (J) levels in PC-9 cells treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 24 h were measured K-L PC-9 cells were transfected with siLDHA and siLDHB (siLDHA/B group) or control siRNA (si-NC group) K KRT19 mRNA expression in PC-9 cells (si-NC, siLDHA/B) was determined by RT-PCR L KRT19, LDHA, LDHB and H3K18la protein levels in different groups of PC-9 cells were measured using immunoblot. Data are shown as mean ± S.E.M. and analyzed by Student’s t -test (A, C-L). * p < 0.05; ** p < 0.01; *** p < 0.001. All experiments were repeated two (B) or three times (C-L)
Anti H3k9ac Antibody, supplied by PTM Biolabs, 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/chip+grade+anti+h3k18la/pm35735108-208-29-31?v=PTM+Biolabs
Average 90 stars, based on 1 article reviews
anti-h3k9ac antibody - by Bioz Stars, 2026-08
90/100 stars
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anti-h3k18la  (PTM Biolabs)
90
PTM Biolabs anti-h3k18la
<t>H3K18la</t> binds to the KRT19 promoter to upregulate KRT19 expression in NSCLC cells A The protein expression of H3K18la in clinical NSCLC tissues and paired normal tissues ( n = 3) were determined by immunoblot B ChIP-seq <t>with</t> <t>anti-H3K18la</t> was performed on NCI-H1299 cells, and input was served as control. IGV tracks for KRT19 from ChIP-seq data ( GSE245990 ) were shown C A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 16 h, the binding of H3K18la to the KRT19 promoter regions (a, b) in control and lactate-treated A549 cells was determined by ChIP-PCR D PC-9 cells were treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 16 h. The enrichment of H3K18la in the KRT19 promoter regions (a, b) in different groups of PC-9 cells was measured by ChIP-PCR E A549 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and then stimulated with or without lactate (40 mM, LA group) for another 16 h, the luciferase activities were determined F PC-9 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and treated with or without 2-DG (20 mM) or oxamate (10 mM, Oxa) for another 16 h. The luciferase activities were determined G-H A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 24 h, KRT19 mRNA (G) and protein (H) expression was determined by RT-PCR and immunoblot, respectively I-J KRT19 mRNA (I) and protein (J) levels in PC-9 cells treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 24 h were measured K-L PC-9 cells were transfected with siLDHA and siLDHB (siLDHA/B group) or control siRNA (si-NC group) K KRT19 mRNA expression in PC-9 cells (si-NC, siLDHA/B) was determined by RT-PCR L KRT19, LDHA, LDHB and H3K18la protein levels in different groups of PC-9 cells were measured using immunoblot. Data are shown as mean ± S.E.M. and analyzed by Student’s t -test (A, C-L). * p < 0.05; ** p < 0.01; *** p < 0.001. All experiments were repeated two (B) or three times (C-L)
Anti H3k18la, supplied by PTM Biolabs, 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/chip+grade+anti+h3k18la/pmc11492558-133-36-38?v=PTM+Biolabs
Average 90 stars, based on 1 article reviews
anti-h3k18la - by Bioz Stars, 2026-08
90/100 stars
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cell lysis  (Proteintech)
96
Proteintech cell lysis
<t>H3K18la</t> binds to the KRT19 promoter to upregulate KRT19 expression in NSCLC cells A The protein expression of H3K18la in clinical NSCLC tissues and paired normal tissues ( n = 3) were determined by immunoblot B ChIP-seq <t>with</t> <t>anti-H3K18la</t> was performed on NCI-H1299 cells, and input was served as control. IGV tracks for KRT19 from ChIP-seq data ( GSE245990 ) were shown C A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 16 h, the binding of H3K18la to the KRT19 promoter regions (a, b) in control and lactate-treated A549 cells was determined by ChIP-PCR D PC-9 cells were treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 16 h. The enrichment of H3K18la in the KRT19 promoter regions (a, b) in different groups of PC-9 cells was measured by ChIP-PCR E A549 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and then stimulated with or without lactate (40 mM, LA group) for another 16 h, the luciferase activities were determined F PC-9 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and treated with or without 2-DG (20 mM) or oxamate (10 mM, Oxa) for another 16 h. The luciferase activities were determined G-H A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 24 h, KRT19 mRNA (G) and protein (H) expression was determined by RT-PCR and immunoblot, respectively I-J KRT19 mRNA (I) and protein (J) levels in PC-9 cells treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 24 h were measured K-L PC-9 cells were transfected with siLDHA and siLDHB (siLDHA/B group) or control siRNA (si-NC group) K KRT19 mRNA expression in PC-9 cells (si-NC, siLDHA/B) was determined by RT-PCR L KRT19, LDHA, LDHB and H3K18la protein levels in different groups of PC-9 cells were measured using immunoblot. Data are shown as mean ± S.E.M. and analyzed by Student’s t -test (A, C-L). * p < 0.05; ** p < 0.01; *** p < 0.001. All experiments were repeated two (B) or three times (C-L)
Cell Lysis, 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
https://www.bioz.com/product/chip+grade+anti+h3k18la/pmc12802155-102-1-15?v=Proteintech
Average 96 stars, based on 1 article reviews
cell lysis - by Bioz Stars, 2026-08
96/100 stars
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anti igg  (Proteintech)
96
Proteintech anti igg
<t>H3K18la</t> binds to the KRT19 promoter to upregulate KRT19 expression in NSCLC cells A The protein expression of H3K18la in clinical NSCLC tissues and paired normal tissues ( n = 3) were determined by immunoblot B ChIP-seq <t>with</t> <t>anti-H3K18la</t> was performed on NCI-H1299 cells, and input was served as control. IGV tracks for KRT19 from ChIP-seq data ( GSE245990 ) were shown C A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 16 h, the binding of H3K18la to the KRT19 promoter regions (a, b) in control and lactate-treated A549 cells was determined by ChIP-PCR D PC-9 cells were treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 16 h. The enrichment of H3K18la in the KRT19 promoter regions (a, b) in different groups of PC-9 cells was measured by ChIP-PCR E A549 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and then stimulated with or without lactate (40 mM, LA group) for another 16 h, the luciferase activities were determined F PC-9 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and treated with or without 2-DG (20 mM) or oxamate (10 mM, Oxa) for another 16 h. The luciferase activities were determined G-H A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 24 h, KRT19 mRNA (G) and protein (H) expression was determined by RT-PCR and immunoblot, respectively I-J KRT19 mRNA (I) and protein (J) levels in PC-9 cells treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 24 h were measured K-L PC-9 cells were transfected with siLDHA and siLDHB (siLDHA/B group) or control siRNA (si-NC group) K KRT19 mRNA expression in PC-9 cells (si-NC, siLDHA/B) was determined by RT-PCR L KRT19, LDHA, LDHB and H3K18la protein levels in different groups of PC-9 cells were measured using immunoblot. Data are shown as mean ± S.E.M. and analyzed by Student’s t -test (A, C-L). * p < 0.05; ** p < 0.01; *** p < 0.001. All experiments were repeated two (B) or three times (C-L)
Anti Igg, 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
https://www.bioz.com/product/chip+grade+anti+h3k18la/pmc12078822-128-6-8?v=Proteintech
Average 96 stars, based on 1 article reviews
anti igg - by Bioz Stars, 2026-08
96/100 stars
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anti wtap antibodies  (Proteintech)
96
Proteintech anti wtap antibodies
The role of <t>WTAP</t> in hepatic steatosis in vivo by AAV8 tail vein injection . A) Schematic diagram of study design using the AAV8-WTAP injection to mimic the overexpression of WTAP in C57BL/6 mice, n = 5 per group; B) Western blotting of WTAP expression in C57/BL6 mice treated with AAV8-WTAP or AAV8-Blank. n = 5 per group; C) Representative images of the gross appearance in the liver histology (1 cm), quantification of the liver index (%), H&E (100 μm), F4/80 antibody (100 μm), Masson staining (100 μm), and ORO staining (100 μm); D-I) Serum concentration of ALT (U/L) (D), AST (U/L) (E), triglyceride (mg/dL) (F), cholesterol (mg/dL) (G), LDL (mg/dL) (H), and HDL (mg/dl) (I) in C57/BL6 mice treated with AAV8-WTAP or AAV8-Blank. n = 5 per group; J) Representative quantitative PCR analysis with key genes involved in lipogenesis, FAO and OXPHOS metabolism in C57/BL6 mice treated with AAV8-WTAP or AAV8-Blank. n = 5 per group; K) Schematic diagram of study design using AAV8-shWTAP to mimic the inhibition of WTAP in C57BL/6 mice; L) Western blotting of WTAP expression in C57/BL6 mice treated with AAV8-shWTAP, AAV8-shWTAP + H. pylori SS1 infection, AAV8-shBlank, and AAV8-shWTAP + H. pylori infection. n = 5 per group; M) Representative images of the gross appearance in the liver histology (1 cm), quantification of the liver index (%), H&E (100 μm), F4/80 antibody (100 μm), Masson staining (100 μm), and oil red staining (100 μm). N -Q) Serum concentration of ALT (U/L) ( N ), AST (U/L) (O), triglyceride (mmol/L) ( P ), and cholesterol (mmol/L) (Q) in C57/BL6 mice treated with AAV8-shWTAP, AAV8-shWTAP + H. pylori SS1 infection, AAV8-shBlank, and AAV8-shWTAP + H. pylori infection. n = 5 per group. Statistical analysis was performed using Two-tailed Student's t -test (two groups) and one-way analysis of variance (ANOVA) (multiple groups) followed by Bonferroni's test. *p < 0.05; **p < 0.01; and ***p < 0.001 .
Anti Wtap 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
https://www.bioz.com/product/chip+grade+anti+h3k18la/pmc12710952-97-14-16?v=Proteintech
Average 96 stars, based on 1 article reviews
anti wtap antibodies - by Bioz Stars, 2026-08
96/100 stars
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hdac1  (Proteintech)
96
Proteintech hdac1
tRF-31R9J weakens histone lactylation and acetylation modification by binding to the <t>histone</t> <t>deacetylase</t> <t>HDAC1.</t> A The interacting protein of tRF-31R9J was identified through RNA pull-down. B The enrichment of HDAC1 was validated by WB. C Molecular docking was employed to construct a model of the interaction between tRF-31R9J and HDAC1. D IF and FISH were employed to validate the co-localization of tRF-31R9J and HDAC1. E WB was performed to validate the knockdown efficiency of HDAC1 ( N = 3). F The levels of histone lactylation modification were detected by WB ( N = 3). G The lactylation level was further verified by IF. H WB was performed to assess the expression of ferroptosis key molecules ( N = 3). * P < 0.05, ** P < 0.01
Hdac1, 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
https://www.bioz.com/product/chip+grade+anti+h3k18la/pmc11748747-85-18-19?v=Proteintech
Average 96 stars, based on 1 article reviews
hdac1 - by Bioz Stars, 2026-08
96/100 stars
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gli3  (Proteintech)
93
Proteintech gli3
A The expression of COL27A1, SLFNL1, SEMA5A, and <t>GLI3</t> in macrophages was assessed by RT-qPCR. B ChIP-qPCR with anti-H3K18la antibody was performed to assess changes in histone lactylation levels at the GLI3 locus in macrophages following lactate treatment. C A dual-luciferase reporter assay was conducted to verify the enrichment sites of histone lactylation. D IF using an anti-H3K18la antibody combined with FISH targeting GLI3 DNA was carried out to demonstrate the colocalization of histone lactylation and GLI3 DNA in macrophages. E – G The interference efficiency of GLI3 was detected using RT-qPCR ( E ) and WB ( F – G ). H The level of CD80, MCP-1, and iNOS after GLI3 knockdown was evaluated using RT-qPCR. I The effect of GLI3 on the expression of M2 polarization markers CD163, MRC-2, and Arg-1 in macrophages was investigated by RT-qPCR. J The levels of IL-10, TNF-α, and IL-1β after GLI3 knockdown were detected using ELISA. K , L IF was employed to examine the expression of CD86 and CD206 after GLI3 knockdown. Data are represented as mean ± SEM. Two-tailed Student’s t test ( A – C and G – J ) or one-way ANOVA ( E ). * P < 0.05, ** P < 0.01.
Gli3, supplied by Proteintech, 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/chip+grade+anti+h3k18la/pmc12603228-320-25-26?v=Proteintech
Average 93 stars, based on 1 article reviews
gli3 - by Bioz Stars, 2026-08
93/100 stars
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applications atf6 proteintech  (Proteintech)
96
Proteintech applications atf6 proteintech
A The expression of COL27A1, SLFNL1, SEMA5A, and <t>GLI3</t> in macrophages was assessed by RT-qPCR. B ChIP-qPCR with anti-H3K18la antibody was performed to assess changes in histone lactylation levels at the GLI3 locus in macrophages following lactate treatment. C A dual-luciferase reporter assay was conducted to verify the enrichment sites of histone lactylation. D IF using an anti-H3K18la antibody combined with FISH targeting GLI3 DNA was carried out to demonstrate the colocalization of histone lactylation and GLI3 DNA in macrophages. E – G The interference efficiency of GLI3 was detected using RT-qPCR ( E ) and WB ( F – G ). H The level of CD80, MCP-1, and iNOS after GLI3 knockdown was evaluated using RT-qPCR. I The effect of GLI3 on the expression of M2 polarization markers CD163, MRC-2, and Arg-1 in macrophages was investigated by RT-qPCR. J The levels of IL-10, TNF-α, and IL-1β after GLI3 knockdown were detected using ELISA. K , L IF was employed to examine the expression of CD86 and CD206 after GLI3 knockdown. Data are represented as mean ± SEM. Two-tailed Student’s t test ( A – C and G – J ) or one-way ANOVA ( E ). * P < 0.05, ** P < 0.01.
Applications Atf6 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
https://www.bioz.com/product/chip+grade+anti+h3k18la/pm41575611-77-57-59?v=Proteintech
Average 96 stars, based on 1 article reviews
applications atf6 proteintech - by Bioz Stars, 2026-08
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anti rabbit igg antibody servicebio g1213  (Servicebio Inc)
86
Servicebio Inc anti rabbit igg antibody servicebio g1213
A The expression of COL27A1, SLFNL1, SEMA5A, and <t>GLI3</t> in macrophages was assessed by RT-qPCR. B ChIP-qPCR with anti-H3K18la antibody was performed to assess changes in histone lactylation levels at the GLI3 locus in macrophages following lactate treatment. C A dual-luciferase reporter assay was conducted to verify the enrichment sites of histone lactylation. D IF using an anti-H3K18la antibody combined with FISH targeting GLI3 DNA was carried out to demonstrate the colocalization of histone lactylation and GLI3 DNA in macrophages. E – G The interference efficiency of GLI3 was detected using RT-qPCR ( E ) and WB ( F – G ). H The level of CD80, MCP-1, and iNOS after GLI3 knockdown was evaluated using RT-qPCR. I The effect of GLI3 on the expression of M2 polarization markers CD163, MRC-2, and Arg-1 in macrophages was investigated by RT-qPCR. J The levels of IL-10, TNF-α, and IL-1β after GLI3 knockdown were detected using ELISA. K , L IF was employed to examine the expression of CD86 and CD206 after GLI3 knockdown. Data are represented as mean ± SEM. Two-tailed Student’s t test ( A – C and G – J ) or one-way ANOVA ( E ). * P < 0.05, ** P < 0.01.
Anti Rabbit Igg Antibody Servicebio G1213, supplied by Servicebio Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/chip+grade+anti+h3k18la/pm41617670-286-175-178?v=Servicebio+Inc
Average 86 stars, based on 1 article reviews
anti rabbit igg antibody servicebio g1213 - by Bioz Stars, 2026-08
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cd68 proteintech 25747 1 ap  (Proteintech)
96
Proteintech cd68 proteintech 25747 1 ap
A The expression of COL27A1, SLFNL1, SEMA5A, and <t>GLI3</t> in macrophages was assessed by RT-qPCR. B ChIP-qPCR with anti-H3K18la antibody was performed to assess changes in histone lactylation levels at the GLI3 locus in macrophages following lactate treatment. C A dual-luciferase reporter assay was conducted to verify the enrichment sites of histone lactylation. D IF using an anti-H3K18la antibody combined with FISH targeting GLI3 DNA was carried out to demonstrate the colocalization of histone lactylation and GLI3 DNA in macrophages. E – G The interference efficiency of GLI3 was detected using RT-qPCR ( E ) and WB ( F – G ). H The level of CD80, MCP-1, and iNOS after GLI3 knockdown was evaluated using RT-qPCR. I The effect of GLI3 on the expression of M2 polarization markers CD163, MRC-2, and Arg-1 in macrophages was investigated by RT-qPCR. J The levels of IL-10, TNF-α, and IL-1β after GLI3 knockdown were detected using ELISA. K , L IF was employed to examine the expression of CD86 and CD206 after GLI3 knockdown. Data are represented as mean ± SEM. Two-tailed Student’s t test ( A – C and G – J ) or one-way ANOVA ( E ). * P < 0.05, ** P < 0.01.
Cd68 Proteintech 25747 1 Ap, 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
https://www.bioz.com/product/chip+grade+anti+h3k18la/pm41617670-286-142-143?v=Proteintech
Average 96 stars, based on 1 article reviews
cd68 proteintech 25747 1 ap - by Bioz Stars, 2026-08
96/100 stars
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H3K18la binds to the KRT19 promoter to upregulate KRT19 expression in NSCLC cells A The protein expression of H3K18la in clinical NSCLC tissues and paired normal tissues ( n = 3) were determined by immunoblot B ChIP-seq with anti-H3K18la was performed on NCI-H1299 cells, and input was served as control. IGV tracks for KRT19 from ChIP-seq data ( GSE245990 ) were shown C A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 16 h, the binding of H3K18la to the KRT19 promoter regions (a, b) in control and lactate-treated A549 cells was determined by ChIP-PCR D PC-9 cells were treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 16 h. The enrichment of H3K18la in the KRT19 promoter regions (a, b) in different groups of PC-9 cells was measured by ChIP-PCR E A549 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and then stimulated with or without lactate (40 mM, LA group) for another 16 h, the luciferase activities were determined F PC-9 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and treated with or without 2-DG (20 mM) or oxamate (10 mM, Oxa) for another 16 h. The luciferase activities were determined G-H A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 24 h, KRT19 mRNA (G) and protein (H) expression was determined by RT-PCR and immunoblot, respectively I-J KRT19 mRNA (I) and protein (J) levels in PC-9 cells treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 24 h were measured K-L PC-9 cells were transfected with siLDHA and siLDHB (siLDHA/B group) or control siRNA (si-NC group) K KRT19 mRNA expression in PC-9 cells (si-NC, siLDHA/B) was determined by RT-PCR L KRT19, LDHA, LDHB and H3K18la protein levels in different groups of PC-9 cells were measured using immunoblot. Data are shown as mean ± S.E.M. and analyzed by Student’s t -test (A, C-L). * p < 0.05; ** p < 0.01; *** p < 0.001. All experiments were repeated two (B) or three times (C-L)

Journal: Journal of Experimental & Clinical Cancer Research : CR

Article Title: Lactylation-driven KRT19 promotes non-small cell lung cancer progression by suppressing cellular senescence

doi: 10.1186/s13046-025-03602-5

Figure Lengend Snippet: H3K18la binds to the KRT19 promoter to upregulate KRT19 expression in NSCLC cells A The protein expression of H3K18la in clinical NSCLC tissues and paired normal tissues ( n = 3) were determined by immunoblot B ChIP-seq with anti-H3K18la was performed on NCI-H1299 cells, and input was served as control. IGV tracks for KRT19 from ChIP-seq data ( GSE245990 ) were shown C A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 16 h, the binding of H3K18la to the KRT19 promoter regions (a, b) in control and lactate-treated A549 cells was determined by ChIP-PCR D PC-9 cells were treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 16 h. The enrichment of H3K18la in the KRT19 promoter regions (a, b) in different groups of PC-9 cells was measured by ChIP-PCR E A549 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and then stimulated with or without lactate (40 mM, LA group) for another 16 h, the luciferase activities were determined F PC-9 cells were co-transfected with pRL-TK and pGL3-basic or pGL3- KRT19- Luc plasmids for 48 h, and treated with or without 2-DG (20 mM) or oxamate (10 mM, Oxa) for another 16 h. The luciferase activities were determined G-H A549 cells were incubated with lactate (40 mM, LA group) or vehicle (Control group) for 24 h, KRT19 mRNA (G) and protein (H) expression was determined by RT-PCR and immunoblot, respectively I-J KRT19 mRNA (I) and protein (J) levels in PC-9 cells treated with 2-DG (20 mM, 2-DG group), oxamate (10 mM, Oxa group) or vehicle (Control group) for 24 h were measured K-L PC-9 cells were transfected with siLDHA and siLDHB (siLDHA/B group) or control siRNA (si-NC group) K KRT19 mRNA expression in PC-9 cells (si-NC, siLDHA/B) was determined by RT-PCR L KRT19, LDHA, LDHB and H3K18la protein levels in different groups of PC-9 cells were measured using immunoblot. Data are shown as mean ± S.E.M. and analyzed by Student’s t -test (A, C-L). * p < 0.05; ** p < 0.01; *** p < 0.001. All experiments were repeated two (B) or three times (C-L)

Article Snippet: Then, cell lysis was immunoprecipitated with ChIP-grade anti-H3K18la (PTM-1427RM, PTM BIO) or anti-p53 antibody (10442-1-AP, Proteintech) overnight at 4 °C, followed by washing, elution and cross-link reversal using the ChIP Assay Kit (P2078, Beyotime).

Techniques: Expressing, Western Blot, ChIP-sequencing, Control, Incubation, Binding Assay, Transfection, Luciferase, Reverse Transcription Polymerase Chain Reaction

The role of WTAP in hepatic steatosis in vivo by AAV8 tail vein injection . A) Schematic diagram of study design using the AAV8-WTAP injection to mimic the overexpression of WTAP in C57BL/6 mice, n = 5 per group; B) Western blotting of WTAP expression in C57/BL6 mice treated with AAV8-WTAP or AAV8-Blank. n = 5 per group; C) Representative images of the gross appearance in the liver histology (1 cm), quantification of the liver index (%), H&E (100 μm), F4/80 antibody (100 μm), Masson staining (100 μm), and ORO staining (100 μm); D-I) Serum concentration of ALT (U/L) (D), AST (U/L) (E), triglyceride (mg/dL) (F), cholesterol (mg/dL) (G), LDL (mg/dL) (H), and HDL (mg/dl) (I) in C57/BL6 mice treated with AAV8-WTAP or AAV8-Blank. n = 5 per group; J) Representative quantitative PCR analysis with key genes involved in lipogenesis, FAO and OXPHOS metabolism in C57/BL6 mice treated with AAV8-WTAP or AAV8-Blank. n = 5 per group; K) Schematic diagram of study design using AAV8-shWTAP to mimic the inhibition of WTAP in C57BL/6 mice; L) Western blotting of WTAP expression in C57/BL6 mice treated with AAV8-shWTAP, AAV8-shWTAP + H. pylori SS1 infection, AAV8-shBlank, and AAV8-shWTAP + H. pylori infection. n = 5 per group; M) Representative images of the gross appearance in the liver histology (1 cm), quantification of the liver index (%), H&E (100 μm), F4/80 antibody (100 μm), Masson staining (100 μm), and oil red staining (100 μm). N -Q) Serum concentration of ALT (U/L) ( N ), AST (U/L) (O), triglyceride (mmol/L) ( P ), and cholesterol (mmol/L) (Q) in C57/BL6 mice treated with AAV8-shWTAP, AAV8-shWTAP + H. pylori SS1 infection, AAV8-shBlank, and AAV8-shWTAP + H. pylori infection. n = 5 per group. Statistical analysis was performed using Two-tailed Student's t -test (two groups) and one-way analysis of variance (ANOVA) (multiple groups) followed by Bonferroni's test. *p < 0.05; **p < 0.01; and ***p < 0.001 .

Journal: Gut Microbes

Article Title: Helicobacter pylori infection aggravates hepatic steatosis by lactylation-driven WTAP-mediated m 6 A modification

doi: 10.1080/19490976.2025.2599543

Figure Lengend Snippet: The role of WTAP in hepatic steatosis in vivo by AAV8 tail vein injection . A) Schematic diagram of study design using the AAV8-WTAP injection to mimic the overexpression of WTAP in C57BL/6 mice, n = 5 per group; B) Western blotting of WTAP expression in C57/BL6 mice treated with AAV8-WTAP or AAV8-Blank. n = 5 per group; C) Representative images of the gross appearance in the liver histology (1 cm), quantification of the liver index (%), H&E (100 μm), F4/80 antibody (100 μm), Masson staining (100 μm), and ORO staining (100 μm); D-I) Serum concentration of ALT (U/L) (D), AST (U/L) (E), triglyceride (mg/dL) (F), cholesterol (mg/dL) (G), LDL (mg/dL) (H), and HDL (mg/dl) (I) in C57/BL6 mice treated with AAV8-WTAP or AAV8-Blank. n = 5 per group; J) Representative quantitative PCR analysis with key genes involved in lipogenesis, FAO and OXPHOS metabolism in C57/BL6 mice treated with AAV8-WTAP or AAV8-Blank. n = 5 per group; K) Schematic diagram of study design using AAV8-shWTAP to mimic the inhibition of WTAP in C57BL/6 mice; L) Western blotting of WTAP expression in C57/BL6 mice treated with AAV8-shWTAP, AAV8-shWTAP + H. pylori SS1 infection, AAV8-shBlank, and AAV8-shWTAP + H. pylori infection. n = 5 per group; M) Representative images of the gross appearance in the liver histology (1 cm), quantification of the liver index (%), H&E (100 μm), F4/80 antibody (100 μm), Masson staining (100 μm), and oil red staining (100 μm). N -Q) Serum concentration of ALT (U/L) ( N ), AST (U/L) (O), triglyceride (mmol/L) ( P ), and cholesterol (mmol/L) (Q) in C57/BL6 mice treated with AAV8-shWTAP, AAV8-shWTAP + H. pylori SS1 infection, AAV8-shBlank, and AAV8-shWTAP + H. pylori infection. n = 5 per group. Statistical analysis was performed using Two-tailed Student's t -test (two groups) and one-way analysis of variance (ANOVA) (multiple groups) followed by Bonferroni's test. *p < 0.05; **p < 0.01; and ***p < 0.001 .

Article Snippet: Samples were then incubated with primary antibodies, including anti-F4/80 antibodies (Servicebio, GB113373 ; 1:200), anti-WTAP antibodies (Proteintech, 10200-1-AP; 1:200), anti-H3K18la-antibodies (PTM-bio, PTM-1427RM; 1:200), anti-Pan-Kla-antibodies (PTM-bio, PTM-1401RM; 1:200) overnight at 4 °C.

Techniques: In Vivo, Injection, Over Expression, Western Blot, Expressing, Staining, Concentration Assay, Real-time Polymerase Chain Reaction, Inhibition, Infection, Two Tailed Test

H. pylori infection promotes glycolysis and regulates WTAP expression via histone lactylation . A) Volcano plot of significantly-changed metabolites and KEGG analysis of remarkably changed pathways from untargeted metabolomics analysis; B) Lactic acid level of liver tissues in C57BL/6 mice with or without H. pylori SS1 infection, n = 5 per group; C) The glycolytic capability of HepG2 cells co-cultured with or without H. pylori OMVs using ECAR curve, n = 3 per group; D) Mitochondrial oxidative capacity was measured after HepG2 cells co-cultured with or without H. pylori OMVs using OCR curve, n = 3 per group; E) Intracellular ROS levels of HepG2 cells co-cultured with or without H. pylori 26695 OMVs in a dose or time-dependent manner, n = 3 per group; F-G) mRNA and protein expression of LDHA and LDHB in liver tissues or HepG2 cells following H. pylori 26695 infection using qRT-PCR (F) and Western blot (G) analysis, n = 3 per group. H) mRNA and protein expression of WTAP in HepG2 cells after lactate treatment, n = 3 per group; I) Representative images of Silver staining-MS of lactylated proteins; J) Pan-lysine lactylation levels in cells were measured at indicated times with 10 ug/ml H. pylori 26695 OMVs or after the indicated dose treatment for 24 h and lysine lactylation levels of H3 were detected under the same conditions. K) ChIP-qPCR using anti-H3K18la antibodies validates H3K18la enrichment in peak 1 and peak 2 within the promoter region of WTAP in HepG2. L) WTAP mRNA and protein level after 2-DG and oxamate treatment, n = 3 per group. M) ChIP-qPCR using anti-H3K18la antibodies validates H3K18la enrichment in HepG2 cells after 2-DG or oxamate treatment or si-LDHA/B transfection. N ) WTAP mRNA and protein level in HepG2 cells after si-LDHA/B transfection with or without Nala addition, n = 3 per group. Statistical analysis was performed using Two-tailed Student's t -test (two groups) and one-way analysis of variance (ANOVA) (multiple groups) followed by Bonferroni's test. *p < 0.05; **p < 0.01; and ***p < 0.001 .

Journal: Gut Microbes

Article Title: Helicobacter pylori infection aggravates hepatic steatosis by lactylation-driven WTAP-mediated m 6 A modification

doi: 10.1080/19490976.2025.2599543

Figure Lengend Snippet: H. pylori infection promotes glycolysis and regulates WTAP expression via histone lactylation . A) Volcano plot of significantly-changed metabolites and KEGG analysis of remarkably changed pathways from untargeted metabolomics analysis; B) Lactic acid level of liver tissues in C57BL/6 mice with or without H. pylori SS1 infection, n = 5 per group; C) The glycolytic capability of HepG2 cells co-cultured with or without H. pylori OMVs using ECAR curve, n = 3 per group; D) Mitochondrial oxidative capacity was measured after HepG2 cells co-cultured with or without H. pylori OMVs using OCR curve, n = 3 per group; E) Intracellular ROS levels of HepG2 cells co-cultured with or without H. pylori 26695 OMVs in a dose or time-dependent manner, n = 3 per group; F-G) mRNA and protein expression of LDHA and LDHB in liver tissues or HepG2 cells following H. pylori 26695 infection using qRT-PCR (F) and Western blot (G) analysis, n = 3 per group. H) mRNA and protein expression of WTAP in HepG2 cells after lactate treatment, n = 3 per group; I) Representative images of Silver staining-MS of lactylated proteins; J) Pan-lysine lactylation levels in cells were measured at indicated times with 10 ug/ml H. pylori 26695 OMVs or after the indicated dose treatment for 24 h and lysine lactylation levels of H3 were detected under the same conditions. K) ChIP-qPCR using anti-H3K18la antibodies validates H3K18la enrichment in peak 1 and peak 2 within the promoter region of WTAP in HepG2. L) WTAP mRNA and protein level after 2-DG and oxamate treatment, n = 3 per group. M) ChIP-qPCR using anti-H3K18la antibodies validates H3K18la enrichment in HepG2 cells after 2-DG or oxamate treatment or si-LDHA/B transfection. N ) WTAP mRNA and protein level in HepG2 cells after si-LDHA/B transfection with or without Nala addition, n = 3 per group. Statistical analysis was performed using Two-tailed Student's t -test (two groups) and one-way analysis of variance (ANOVA) (multiple groups) followed by Bonferroni's test. *p < 0.05; **p < 0.01; and ***p < 0.001 .

Article Snippet: Samples were then incubated with primary antibodies, including anti-F4/80 antibodies (Servicebio, GB113373 ; 1:200), anti-WTAP antibodies (Proteintech, 10200-1-AP; 1:200), anti-H3K18la-antibodies (PTM-bio, PTM-1427RM; 1:200), anti-Pan-Kla-antibodies (PTM-bio, PTM-1401RM; 1:200) overnight at 4 °C.

Techniques: Infection, Expressing, Cell Culture, Quantitative RT-PCR, Western Blot, Silver Staining, ChIP-qPCR, Transfection, Two Tailed Test

Direct lactylation of WTAP enhanced the capture of m6A-modified RNA. A) MOE is used to predict the binding affinity between the WTAP protein and L-lactate; B) Illustration of WTAP Kla sites derived from HepG2 cells identified by LC-MS; C) Lactylation of WTAP in 293 T cells was confirmed by IP method. 293 T cells transfected with FLAG-WTAP, treated with ddH2O or 25 mM L-lactic acid for 24 h. The cells were lysed for SDS pre-treated immunoprecipitation with anti-FLAG antibody followed by western blotting; D) Lactylation of WTAP in HepG2 was confirmed by IP method. HepG2 co-cultured with OMVs or treated with 25 mM LA for 24 h. The cells were lysed for SDS pre-treated immunoprecipitation with anti-METTL3 antibody followed by western blotting; E) FLAG-WTAP, with Myc-METTL3 or Myc-METTL14 were transfected into 293 T cells for 24 h. Then cells were treated with 25 mM L-lactic acid for 24 h. Lysates were used for IP with anti-FLAG antibody, followed by western blotting; F) FLAG-WTAP, with Myc-METTL3 or Myc-METTL14 were transfected into 293 T cells for 24 h. Then cells were treated with 25 mM L-lactic acid for 24 h. Cells were harvested for immunofluorescence staining and further photographed by laser scanning confocal microscopy. Scale bars, 20 mm; G) HepG2 were treated with 25 mM L-lactic acid for 24 h. Cells were harvested for immunofluorescence staining (20 mm) and further photographed by laser scanning confocal microscopy; H) Western blotting analysis of the distribution in nuclear and cytoplasmic fractions of WTAP in HepG2 treated with or without 25 mM L-lactic acid for 24 h. I) Western blotting analysis of WTAP in HepG2 with or without lactic acid treated with 0.1 mg/mL CHX for indicated time; J) FLAG-WTAP was transfected into 293 T cells for 24 h. Then cells were treated with L-lactic acid or Nala for 24 h. Cells were 254 nm UV-crosslinked before harvesting. Lysates were used for SDS pre-treated immunoprecipitation with anti-FLAG antibody, followed by western blotting to detect indicated targets. K) FLAG-WTAP (WT), FLAG-WTAP (K99R), FLAG-WTAP (K134R), and FLAG-WTAP (K99R and K134R) were transfected into 293 T cells for 24 h. Then cells were treated with L-lactic acid for 24 h. Cells were 254 nm UV-crosslinked before harvesting. Lysates were used for SDS pre-treated immunoprecipitation with anti-FLAG antibody, followed by western blotting to detect indicated targets; L) Western blotting analysis of WTAP in 293 T cells transfected with FLAG-WTAP (WT) and FLAG-WTAP (K99R and K134R) with or without lactic acid treated with 0.1 mg/mL CHX for indicated time.

Journal: Gut Microbes

Article Title: Helicobacter pylori infection aggravates hepatic steatosis by lactylation-driven WTAP-mediated m 6 A modification

doi: 10.1080/19490976.2025.2599543

Figure Lengend Snippet: Direct lactylation of WTAP enhanced the capture of m6A-modified RNA. A) MOE is used to predict the binding affinity between the WTAP protein and L-lactate; B) Illustration of WTAP Kla sites derived from HepG2 cells identified by LC-MS; C) Lactylation of WTAP in 293 T cells was confirmed by IP method. 293 T cells transfected with FLAG-WTAP, treated with ddH2O or 25 mM L-lactic acid for 24 h. The cells were lysed for SDS pre-treated immunoprecipitation with anti-FLAG antibody followed by western blotting; D) Lactylation of WTAP in HepG2 was confirmed by IP method. HepG2 co-cultured with OMVs or treated with 25 mM LA for 24 h. The cells were lysed for SDS pre-treated immunoprecipitation with anti-METTL3 antibody followed by western blotting; E) FLAG-WTAP, with Myc-METTL3 or Myc-METTL14 were transfected into 293 T cells for 24 h. Then cells were treated with 25 mM L-lactic acid for 24 h. Lysates were used for IP with anti-FLAG antibody, followed by western blotting; F) FLAG-WTAP, with Myc-METTL3 or Myc-METTL14 were transfected into 293 T cells for 24 h. Then cells were treated with 25 mM L-lactic acid for 24 h. Cells were harvested for immunofluorescence staining and further photographed by laser scanning confocal microscopy. Scale bars, 20 mm; G) HepG2 were treated with 25 mM L-lactic acid for 24 h. Cells were harvested for immunofluorescence staining (20 mm) and further photographed by laser scanning confocal microscopy; H) Western blotting analysis of the distribution in nuclear and cytoplasmic fractions of WTAP in HepG2 treated with or without 25 mM L-lactic acid for 24 h. I) Western blotting analysis of WTAP in HepG2 with or without lactic acid treated with 0.1 mg/mL CHX for indicated time; J) FLAG-WTAP was transfected into 293 T cells for 24 h. Then cells were treated with L-lactic acid or Nala for 24 h. Cells were 254 nm UV-crosslinked before harvesting. Lysates were used for SDS pre-treated immunoprecipitation with anti-FLAG antibody, followed by western blotting to detect indicated targets. K) FLAG-WTAP (WT), FLAG-WTAP (K99R), FLAG-WTAP (K134R), and FLAG-WTAP (K99R and K134R) were transfected into 293 T cells for 24 h. Then cells were treated with L-lactic acid for 24 h. Cells were 254 nm UV-crosslinked before harvesting. Lysates were used for SDS pre-treated immunoprecipitation with anti-FLAG antibody, followed by western blotting to detect indicated targets; L) Western blotting analysis of WTAP in 293 T cells transfected with FLAG-WTAP (WT) and FLAG-WTAP (K99R and K134R) with or without lactic acid treated with 0.1 mg/mL CHX for indicated time.

Article Snippet: Samples were then incubated with primary antibodies, including anti-F4/80 antibodies (Servicebio, GB113373 ; 1:200), anti-WTAP antibodies (Proteintech, 10200-1-AP; 1:200), anti-H3K18la-antibodies (PTM-bio, PTM-1427RM; 1:200), anti-Pan-Kla-antibodies (PTM-bio, PTM-1401RM; 1:200) overnight at 4 °C.

Techniques: Modification, Binding Assay, Derivative Assay, Liquid Chromatography with Mass Spectroscopy, Transfection, Immunoprecipitation, Western Blot, Cell Culture, Immunofluorescence, Staining, Confocal Microscopy

H. pylori- induced hepatic steatosis in HFDHP mice is alleviated after H. pylori eradication. A) Schematic diagram of the animal experiment; C57BL/6 mice with HFD diets were divided into HFDHP ( H. pylori SS1 infection) and HFDHPe ( H. pylori eradication) groups; n = 5 per group; B−F) Serum concentration of glucose (mg/dL) (B), insulin (pg/mL) (C), triglyceride (mg/dL) (D), cholesterol (mg/dL) (E), and LDL (mg/dL) (F) in H. pylori -infected C57/BL6 mice eradicated with triple therapy or placebo. n = 5 per group; G) Representative images of the gross appearance in the liver histology (1 cm), quantification of the liver index (%), H&E (100μm), F4/80 antibody (100μm), Masson staining (100μm), and ORO staining (100μm). Histogram plots of weight (g), liver index (%), average liver balloon diameters (μm), number of F4/80 positive cells (%), CVF (%), and oil red lipid contents (%) of H. pylori -infected C57/BL6 mice eradicated with triple therapy or placebo. n = 5 per group; H) Representative quantitative PCR analysis with key genes involved in lipogenesis, FAO and OXPHOS metabolism in H. pylori -infected C57/BL6 mice eradicated with triple therapy or placebo. n = 5 per group; I−J) Immunofluorescence staining of Pan-Kla (I) and H3k18la (J) expression in H. pylori -infected C57/BL6 mice eradicated with triple therapy or placebo. n = 5 per group; K) Western blotting of WTAP and GLUT3 expression in H. pylori -infected C57/BL6 mice eradicated with triple therapy or placebo. n = 5 per group. Statistical analysis was performed using Two-tailed Student's t -test. *p < 0.05; **p < 0.01; and ***p < 0.001 .

Journal: Gut Microbes

Article Title: Helicobacter pylori infection aggravates hepatic steatosis by lactylation-driven WTAP-mediated m 6 A modification

doi: 10.1080/19490976.2025.2599543

Figure Lengend Snippet: H. pylori- induced hepatic steatosis in HFDHP mice is alleviated after H. pylori eradication. A) Schematic diagram of the animal experiment; C57BL/6 mice with HFD diets were divided into HFDHP ( H. pylori SS1 infection) and HFDHPe ( H. pylori eradication) groups; n = 5 per group; B−F) Serum concentration of glucose (mg/dL) (B), insulin (pg/mL) (C), triglyceride (mg/dL) (D), cholesterol (mg/dL) (E), and LDL (mg/dL) (F) in H. pylori -infected C57/BL6 mice eradicated with triple therapy or placebo. n = 5 per group; G) Representative images of the gross appearance in the liver histology (1 cm), quantification of the liver index (%), H&E (100μm), F4/80 antibody (100μm), Masson staining (100μm), and ORO staining (100μm). Histogram plots of weight (g), liver index (%), average liver balloon diameters (μm), number of F4/80 positive cells (%), CVF (%), and oil red lipid contents (%) of H. pylori -infected C57/BL6 mice eradicated with triple therapy or placebo. n = 5 per group; H) Representative quantitative PCR analysis with key genes involved in lipogenesis, FAO and OXPHOS metabolism in H. pylori -infected C57/BL6 mice eradicated with triple therapy or placebo. n = 5 per group; I−J) Immunofluorescence staining of Pan-Kla (I) and H3k18la (J) expression in H. pylori -infected C57/BL6 mice eradicated with triple therapy or placebo. n = 5 per group; K) Western blotting of WTAP and GLUT3 expression in H. pylori -infected C57/BL6 mice eradicated with triple therapy or placebo. n = 5 per group. Statistical analysis was performed using Two-tailed Student's t -test. *p < 0.05; **p < 0.01; and ***p < 0.001 .

Article Snippet: Samples were then incubated with primary antibodies, including anti-F4/80 antibodies (Servicebio, GB113373 ; 1:200), anti-WTAP antibodies (Proteintech, 10200-1-AP; 1:200), anti-H3K18la-antibodies (PTM-bio, PTM-1427RM; 1:200), anti-Pan-Kla-antibodies (PTM-bio, PTM-1401RM; 1:200) overnight at 4 °C.

Techniques: Infection, Concentration Assay, Staining, Real-time Polymerase Chain Reaction, Immunofluorescence, Expressing, Western Blot, Two Tailed Test

tRF-31R9J weakens histone lactylation and acetylation modification by binding to the histone deacetylase HDAC1. A The interacting protein of tRF-31R9J was identified through RNA pull-down. B The enrichment of HDAC1 was validated by WB. C Molecular docking was employed to construct a model of the interaction between tRF-31R9J and HDAC1. D IF and FISH were employed to validate the co-localization of tRF-31R9J and HDAC1. E WB was performed to validate the knockdown efficiency of HDAC1 ( N = 3). F The levels of histone lactylation modification were detected by WB ( N = 3). G The lactylation level was further verified by IF. H WB was performed to assess the expression of ferroptosis key molecules ( N = 3). * P < 0.05, ** P < 0.01

Journal: Clinical Epigenetics

Article Title: TEC-mediated tRF-31R9J regulates histone lactylation and acetylation by HDAC1 to suppress hepatocyte ferroptosis and improve non-alcoholic steatohepatitis

doi: 10.1186/s13148-025-01813-3

Figure Lengend Snippet: tRF-31R9J weakens histone lactylation and acetylation modification by binding to the histone deacetylase HDAC1. A The interacting protein of tRF-31R9J was identified through RNA pull-down. B The enrichment of HDAC1 was validated by WB. C Molecular docking was employed to construct a model of the interaction between tRF-31R9J and HDAC1. D IF and FISH were employed to validate the co-localization of tRF-31R9J and HDAC1. E WB was performed to validate the knockdown efficiency of HDAC1 ( N = 3). F The levels of histone lactylation modification were detected by WB ( N = 3). G The lactylation level was further verified by IF. H WB was performed to assess the expression of ferroptosis key molecules ( N = 3). * P < 0.05, ** P < 0.01

Article Snippet: Primary antibodies against GPX4 (Abcam, ab125066, 1:5000 dilution), ACSL4 (Abcam, ab155282, 1:50000 dilution), GAPDH (Proteintech, 60004-1-Ig, 1:10000 dilution), HDAC1 (Proteintech, 10197-1-AP, 1:10000 dilution), H3K18la (Jingjie PTM Biolab, PTM-1406RM, 1:1000 dilution), H3K18ac (Proteintech, 39129, 1:5000 dilution), Histone H3 (Abcam, ab8896, 1:15000 dilution), ATF3(Abcam, ab254268, 1:1000 dilution), ATF4(Abcam, ab270980, 1:1000 dilution), CHAC1(Proteintech, 15207-1-AP, 1:1000 dilution) were added and incubated at 4 °C overnight.

Techniques: Modification, Binding Assay, Histone Deacetylase Assay, Construct, Knockdown, Expressing

tRF-31R9J regulates histone lactylation levels near ferroptosis-inducing genes by interacting with HDAC1. A MA plot illustrated the changes in differential peaks of histone lactylation in genes enriched between control and lactate groups in GSE208727 (|Mval|> 1, p < 0.05). B The lactylation modification peaks on the ferroptosis-inducing genes ATF3, ATF4, and CHAC1 were visualized. C The regulation of histone lactylation by tRF-31R9J on ATF3, ATF4, and CHAC1 was verified by H3K18la ChIP-PCR and Gel electrophoresis. D H3K18la ChIP-qPCR was performed to validate the regulation of histone lactylation by tRF-31R9J on ATF3, ATF4, and CHAC1 genes ( N = 3). E WB was conducted to examine the influence of HDAC1 on the expression of ATF3, ATF4, and CHAC1 ( N = 3). F The effects of tRF-31R9J and lactate on the expression of ATF3, ATF4, and CHAC1 were validated by RT-qPCR ( N = 3). * P < 0.05, ** P < 0.01

Journal: Clinical Epigenetics

Article Title: TEC-mediated tRF-31R9J regulates histone lactylation and acetylation by HDAC1 to suppress hepatocyte ferroptosis and improve non-alcoholic steatohepatitis

doi: 10.1186/s13148-025-01813-3

Figure Lengend Snippet: tRF-31R9J regulates histone lactylation levels near ferroptosis-inducing genes by interacting with HDAC1. A MA plot illustrated the changes in differential peaks of histone lactylation in genes enriched between control and lactate groups in GSE208727 (|Mval|> 1, p < 0.05). B The lactylation modification peaks on the ferroptosis-inducing genes ATF3, ATF4, and CHAC1 were visualized. C The regulation of histone lactylation by tRF-31R9J on ATF3, ATF4, and CHAC1 was verified by H3K18la ChIP-PCR and Gel electrophoresis. D H3K18la ChIP-qPCR was performed to validate the regulation of histone lactylation by tRF-31R9J on ATF3, ATF4, and CHAC1 genes ( N = 3). E WB was conducted to examine the influence of HDAC1 on the expression of ATF3, ATF4, and CHAC1 ( N = 3). F The effects of tRF-31R9J and lactate on the expression of ATF3, ATF4, and CHAC1 were validated by RT-qPCR ( N = 3). * P < 0.05, ** P < 0.01

Article Snippet: Primary antibodies against GPX4 (Abcam, ab125066, 1:5000 dilution), ACSL4 (Abcam, ab155282, 1:50000 dilution), GAPDH (Proteintech, 60004-1-Ig, 1:10000 dilution), HDAC1 (Proteintech, 10197-1-AP, 1:10000 dilution), H3K18la (Jingjie PTM Biolab, PTM-1406RM, 1:1000 dilution), H3K18ac (Proteintech, 39129, 1:5000 dilution), Histone H3 (Abcam, ab8896, 1:15000 dilution), ATF3(Abcam, ab254268, 1:1000 dilution), ATF4(Abcam, ab270980, 1:1000 dilution), CHAC1(Proteintech, 15207-1-AP, 1:1000 dilution) were added and incubated at 4 °C overnight.

Techniques: Control, Modification, Nucleic Acid Electrophoresis, ChIP-qPCR, Expressing, Quantitative RT-PCR

A The expression of COL27A1, SLFNL1, SEMA5A, and GLI3 in macrophages was assessed by RT-qPCR. B ChIP-qPCR with anti-H3K18la antibody was performed to assess changes in histone lactylation levels at the GLI3 locus in macrophages following lactate treatment. C A dual-luciferase reporter assay was conducted to verify the enrichment sites of histone lactylation. D IF using an anti-H3K18la antibody combined with FISH targeting GLI3 DNA was carried out to demonstrate the colocalization of histone lactylation and GLI3 DNA in macrophages. E – G The interference efficiency of GLI3 was detected using RT-qPCR ( E ) and WB ( F – G ). H The level of CD80, MCP-1, and iNOS after GLI3 knockdown was evaluated using RT-qPCR. I The effect of GLI3 on the expression of M2 polarization markers CD163, MRC-2, and Arg-1 in macrophages was investigated by RT-qPCR. J The levels of IL-10, TNF-α, and IL-1β after GLI3 knockdown were detected using ELISA. K , L IF was employed to examine the expression of CD86 and CD206 after GLI3 knockdown. Data are represented as mean ± SEM. Two-tailed Student’s t test ( A – C and G – J ) or one-way ANOVA ( E ). * P < 0.05, ** P < 0.01.

Journal: Cell Death Discovery

Article Title: Histone lactylation-induced GLI3 activation drives macrophage M1 polarization and exosomal SERPINE1 release in abdominal aortic aneurysm progression

doi: 10.1038/s41420-025-02748-7

Figure Lengend Snippet: A The expression of COL27A1, SLFNL1, SEMA5A, and GLI3 in macrophages was assessed by RT-qPCR. B ChIP-qPCR with anti-H3K18la antibody was performed to assess changes in histone lactylation levels at the GLI3 locus in macrophages following lactate treatment. C A dual-luciferase reporter assay was conducted to verify the enrichment sites of histone lactylation. D IF using an anti-H3K18la antibody combined with FISH targeting GLI3 DNA was carried out to demonstrate the colocalization of histone lactylation and GLI3 DNA in macrophages. E – G The interference efficiency of GLI3 was detected using RT-qPCR ( E ) and WB ( F – G ). H The level of CD80, MCP-1, and iNOS after GLI3 knockdown was evaluated using RT-qPCR. I The effect of GLI3 on the expression of M2 polarization markers CD163, MRC-2, and Arg-1 in macrophages was investigated by RT-qPCR. J The levels of IL-10, TNF-α, and IL-1β after GLI3 knockdown were detected using ELISA. K , L IF was employed to examine the expression of CD86 and CD206 after GLI3 knockdown. Data are represented as mean ± SEM. Two-tailed Student’s t test ( A – C and G – J ) or one-way ANOVA ( E ). * P < 0.05, ** P < 0.01.

Article Snippet: The membrane was incubated with specific antibodies against Histone H3 (Arigo, ARG54767 , 1:2000 dilution), H3K18la (PTMBIO, PTM-1406RM, 1:2000 dilution), GAPDH (Proteintech, 60004-1-Lg, 1:2000 dilution), GLI3 (Proteintech, 28272-1-AP, 1:1000 dilution), Serpin E1 (Proteintech, 13801-1-AP, 1:1000 dilution), Alix (Proteintech, 12422-1-AP, 1:15000 dilution), CD9 (Proteintech, 20597-1-AP, 1:2000 dilution), CD63 (Proteintech, 25682-1-AP, 1:1000 dilution), and Tsg101 (Proteintech, 67381-1-lg, 1:10000 dilution) for 3 hours.

Techniques: Expressing, Quantitative RT-PCR, ChIP-qPCR, Luciferase, Reporter Assay, Knockdown, Enzyme-linked Immunosorbent Assay, Two Tailed Test

A ELISA was used to assess the regulation of GLI3 knockdown and lactate treatment on IL-1β, IL-10, and TNF-α in macrophages. B , C The impact of GLI3 knockdown and lactate treatment on CD206 and CD86 was assessed by IF. Data are represented as mean ± SEM. One-way ANOVA ( A ). ** P < 0.01.

Journal: Cell Death Discovery

Article Title: Histone lactylation-induced GLI3 activation drives macrophage M1 polarization and exosomal SERPINE1 release in abdominal aortic aneurysm progression

doi: 10.1038/s41420-025-02748-7

Figure Lengend Snippet: A ELISA was used to assess the regulation of GLI3 knockdown and lactate treatment on IL-1β, IL-10, and TNF-α in macrophages. B , C The impact of GLI3 knockdown and lactate treatment on CD206 and CD86 was assessed by IF. Data are represented as mean ± SEM. One-way ANOVA ( A ). ** P < 0.01.

Article Snippet: The membrane was incubated with specific antibodies against Histone H3 (Arigo, ARG54767 , 1:2000 dilution), H3K18la (PTMBIO, PTM-1406RM, 1:2000 dilution), GAPDH (Proteintech, 60004-1-Lg, 1:2000 dilution), GLI3 (Proteintech, 28272-1-AP, 1:1000 dilution), Serpin E1 (Proteintech, 13801-1-AP, 1:1000 dilution), Alix (Proteintech, 12422-1-AP, 1:15000 dilution), CD9 (Proteintech, 20597-1-AP, 1:2000 dilution), CD63 (Proteintech, 25682-1-AP, 1:1000 dilution), and Tsg101 (Proteintech, 67381-1-lg, 1:10000 dilution) for 3 hours.

Techniques: Enzyme-linked Immunosorbent Assay, Knockdown

Histone lactylation-mediated GLI3 activation promotes macrophage M1 polarization, and the subsequent secretion of exosomal SERPINE1 by M1 macrophages induces endothelial dysfunction and ultimately facilitates the progression of AAA.

Journal: Cell Death Discovery

Article Title: Histone lactylation-induced GLI3 activation drives macrophage M1 polarization and exosomal SERPINE1 release in abdominal aortic aneurysm progression

doi: 10.1038/s41420-025-02748-7

Figure Lengend Snippet: Histone lactylation-mediated GLI3 activation promotes macrophage M1 polarization, and the subsequent secretion of exosomal SERPINE1 by M1 macrophages induces endothelial dysfunction and ultimately facilitates the progression of AAA.

Article Snippet: The membrane was incubated with specific antibodies against Histone H3 (Arigo, ARG54767 , 1:2000 dilution), H3K18la (PTMBIO, PTM-1406RM, 1:2000 dilution), GAPDH (Proteintech, 60004-1-Lg, 1:2000 dilution), GLI3 (Proteintech, 28272-1-AP, 1:1000 dilution), Serpin E1 (Proteintech, 13801-1-AP, 1:1000 dilution), Alix (Proteintech, 12422-1-AP, 1:15000 dilution), CD9 (Proteintech, 20597-1-AP, 1:2000 dilution), CD63 (Proteintech, 25682-1-AP, 1:1000 dilution), and Tsg101 (Proteintech, 67381-1-lg, 1:10000 dilution) for 3 hours.

Techniques: Activation Assay