lin28 Search Results


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Bioss mouse protein lin 28 homolog a lin28a elisa kit
List of primers used to detect mRNA expression of long noncoding RNA binding proteins
Mouse Protein Lin 28 Homolog A Lin28a Elisa Kit, 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
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Thermo Fisher gene exp lin 28 dm01840272 m1
List of primers used to detect mRNA expression of long noncoding RNA binding proteins
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Santa Cruz Biotechnology lin28
List of primers used to detect mRNA expression of long noncoding RNA binding proteins
Lin28, supplied by Santa Cruz Biotechnology, 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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Addgene inc lin28 coding region
List of primers used to detect mRNA expression of long noncoding RNA binding proteins
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Addgene inc cn1390 raav dlx2 0 minbg syfp2 wpre3 bghpa
List of primers used to detect mRNA expression of long noncoding RNA binding proteins
Cn1390 Raav Dlx2 0 Minbg Syfp2 Wpre3 Bghpa, supplied by Addgene inc, 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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Proteintech rabbit igg anti human lin 28 homolog a
List of primers used to detect mRNA expression of long noncoding RNA binding proteins
Rabbit Igg Anti Human Lin 28 Homolog A, 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
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Proteintech lin28
Induction of HCSC from HBV‐expressing HepAD38 cells by LMD macrophages. a) GSEA analysis showing dysregulated pathway of regulating pluripotency of stem cells in the hepatocytes of the CHB mice at 12 mpi. b) Induction of Yamanaka factors ( Nanog , Oct4 , Klf4 , c‐Myc , <t>Lin28A</t> ) in HBV‐expressing HepAD38 cells treated by macrophages with or without LMD. THP‐derived macrophages were treated with HepAD38 (tet ‐ or tet + ) cells for 48 h, and then co‐cultured with another well of HBV‐expressing HepAD38 in a Transwell plate for another 48 h. The experiments were conducted in triplicate ( n = 3). c) The representative images of Nanog‐positive HCSC (red) surrounded by LXRα‐negative (low or absent of green) Kupffer cells (F4/80, grey) by mIF analysis of liver sections from the control and AAV‐HBV mice at 12 months and 27 months. d) LXR agonist GW3965 significantly reduced the increased mRNA level of pluripontency inducers in HBV‐expressing HepAD38 co‐cultured with LMD macrophages. The experiments were conducted in triplicate ( n = 3). e) The representative bright field images of spheroids formed from HBV‐expressing HepAD38 cells treated by the normal and LMD macrophages with or without GW3965. f) The average of Feret's diameter of the spheroids and the percentage of spheroids with a diameter larger than 50 µm were analyzed. The experiments were performed in triplicate ( n = 3). g) Western blot analysis of Yamanaka factors and the activation of STAT3, Akt, and Wnt3a signaling in HBV‐expressing HepAD38 cells treated by normal and LMD macrophages with or without GW3965. h) The induction of Nanog and Oct4 in LMD macrophage‐co‐cultured HBV + HepAD38 cells was reduced by knockdown of Stat3 . i) Knockdown of AKT had no effect on the expression of Nanog and Oct4 in LMD macrophage‐co‐cultured HBV + HepAD38 cells. j) The Venn diagram showed the overlapping differentially expressed proteins (DEPs) exhibiting opposite variation patterns before and after GW3965 addition within the macrophage‐HepAD38 crosstalk. The supernatants of the co‐culture system involving HepAD38/tet‐ and normal or LMD macrophages with or without GW3965 were subjected to Olink analysis and 7 DEPs who had opposite changing patterns before and after GW3965 treatment were selected. k) The inhibitory effect of neutralization of CCL19, CXCL10, or CXCL11 on the expression of Nanog and Oct4 in HepAD38/tet ‐ cells within the co‐culture system ( n = 3–6). Data are shown as mean ± SEM; * p< 0.05, ** p< 0.01, *** p< 0.001, **** p< 0.0001.
Lin28, 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
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Proteintech anti lin28b
Induction of HCSC from HBV‐expressing HepAD38 cells by LMD macrophages. a) GSEA analysis showing dysregulated pathway of regulating pluripotency of stem cells in the hepatocytes of the CHB mice at 12 mpi. b) Induction of Yamanaka factors ( Nanog , Oct4 , Klf4 , c‐Myc , <t>Lin28A</t> ) in HBV‐expressing HepAD38 cells treated by macrophages with or without LMD. THP‐derived macrophages were treated with HepAD38 (tet ‐ or tet + ) cells for 48 h, and then co‐cultured with another well of HBV‐expressing HepAD38 in a Transwell plate for another 48 h. The experiments were conducted in triplicate ( n = 3). c) The representative images of Nanog‐positive HCSC (red) surrounded by LXRα‐negative (low or absent of green) Kupffer cells (F4/80, grey) by mIF analysis of liver sections from the control and AAV‐HBV mice at 12 months and 27 months. d) LXR agonist GW3965 significantly reduced the increased mRNA level of pluripontency inducers in HBV‐expressing HepAD38 co‐cultured with LMD macrophages. The experiments were conducted in triplicate ( n = 3). e) The representative bright field images of spheroids formed from HBV‐expressing HepAD38 cells treated by the normal and LMD macrophages with or without GW3965. f) The average of Feret's diameter of the spheroids and the percentage of spheroids with a diameter larger than 50 µm were analyzed. The experiments were performed in triplicate ( n = 3). g) Western blot analysis of Yamanaka factors and the activation of STAT3, Akt, and Wnt3a signaling in HBV‐expressing HepAD38 cells treated by normal and LMD macrophages with or without GW3965. h) The induction of Nanog and Oct4 in LMD macrophage‐co‐cultured HBV + HepAD38 cells was reduced by knockdown of Stat3 . i) Knockdown of AKT had no effect on the expression of Nanog and Oct4 in LMD macrophage‐co‐cultured HBV + HepAD38 cells. j) The Venn diagram showed the overlapping differentially expressed proteins (DEPs) exhibiting opposite variation patterns before and after GW3965 addition within the macrophage‐HepAD38 crosstalk. The supernatants of the co‐culture system involving HepAD38/tet‐ and normal or LMD macrophages with or without GW3965 were subjected to Olink analysis and 7 DEPs who had opposite changing patterns before and after GW3965 treatment were selected. k) The inhibitory effect of neutralization of CCL19, CXCL10, or CXCL11 on the expression of Nanog and Oct4 in HepAD38/tet ‐ cells within the co‐culture system ( n = 3–6). Data are shown as mean ± SEM; * p< 0.05, ** p< 0.01, *** p< 0.001, **** p< 0.0001.
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Addgene inc ef1a lin28 ires puro plasmid
Induction of HCSC from HBV‐expressing HepAD38 cells by LMD macrophages. a) GSEA analysis showing dysregulated pathway of regulating pluripotency of stem cells in the hepatocytes of the CHB mice at 12 mpi. b) Induction of Yamanaka factors ( Nanog , Oct4 , Klf4 , c‐Myc , <t>Lin28A</t> ) in HBV‐expressing HepAD38 cells treated by macrophages with or without LMD. THP‐derived macrophages were treated with HepAD38 (tet ‐ or tet + ) cells for 48 h, and then co‐cultured with another well of HBV‐expressing HepAD38 in a Transwell plate for another 48 h. The experiments were conducted in triplicate ( n = 3). c) The representative images of Nanog‐positive HCSC (red) surrounded by LXRα‐negative (low or absent of green) Kupffer cells (F4/80, grey) by mIF analysis of liver sections from the control and AAV‐HBV mice at 12 months and 27 months. d) LXR agonist GW3965 significantly reduced the increased mRNA level of pluripontency inducers in HBV‐expressing HepAD38 co‐cultured with LMD macrophages. The experiments were conducted in triplicate ( n = 3). e) The representative bright field images of spheroids formed from HBV‐expressing HepAD38 cells treated by the normal and LMD macrophages with or without GW3965. f) The average of Feret's diameter of the spheroids and the percentage of spheroids with a diameter larger than 50 µm were analyzed. The experiments were performed in triplicate ( n = 3). g) Western blot analysis of Yamanaka factors and the activation of STAT3, Akt, and Wnt3a signaling in HBV‐expressing HepAD38 cells treated by normal and LMD macrophages with or without GW3965. h) The induction of Nanog and Oct4 in LMD macrophage‐co‐cultured HBV + HepAD38 cells was reduced by knockdown of Stat3 . i) Knockdown of AKT had no effect on the expression of Nanog and Oct4 in LMD macrophage‐co‐cultured HBV + HepAD38 cells. j) The Venn diagram showed the overlapping differentially expressed proteins (DEPs) exhibiting opposite variation patterns before and after GW3965 addition within the macrophage‐HepAD38 crosstalk. The supernatants of the co‐culture system involving HepAD38/tet‐ and normal or LMD macrophages with or without GW3965 were subjected to Olink analysis and 7 DEPs who had opposite changing patterns before and after GW3965 treatment were selected. k) The inhibitory effect of neutralization of CCL19, CXCL10, or CXCL11 on the expression of Nanog and Oct4 in HepAD38/tet ‐ cells within the co‐culture system ( n = 3–6). Data are shown as mean ± SEM; * p< 0.05, ** p< 0.01, *** p< 0.001, **** p< 0.0001.
Ef1a Lin28 Ires Puro Plasmid, supplied by Addgene inc, 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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Tocris compound lin28 1632
Induction of HCSC from HBV‐expressing HepAD38 cells by LMD macrophages. a) GSEA analysis showing dysregulated pathway of regulating pluripotency of stem cells in the hepatocytes of the CHB mice at 12 mpi. b) Induction of Yamanaka factors ( Nanog , Oct4 , Klf4 , c‐Myc , <t>Lin28A</t> ) in HBV‐expressing HepAD38 cells treated by macrophages with or without LMD. THP‐derived macrophages were treated with HepAD38 (tet ‐ or tet + ) cells for 48 h, and then co‐cultured with another well of HBV‐expressing HepAD38 in a Transwell plate for another 48 h. The experiments were conducted in triplicate ( n = 3). c) The representative images of Nanog‐positive HCSC (red) surrounded by LXRα‐negative (low or absent of green) Kupffer cells (F4/80, grey) by mIF analysis of liver sections from the control and AAV‐HBV mice at 12 months and 27 months. d) LXR agonist GW3965 significantly reduced the increased mRNA level of pluripontency inducers in HBV‐expressing HepAD38 co‐cultured with LMD macrophages. The experiments were conducted in triplicate ( n = 3). e) The representative bright field images of spheroids formed from HBV‐expressing HepAD38 cells treated by the normal and LMD macrophages with or without GW3965. f) The average of Feret's diameter of the spheroids and the percentage of spheroids with a diameter larger than 50 µm were analyzed. The experiments were performed in triplicate ( n = 3). g) Western blot analysis of Yamanaka factors and the activation of STAT3, Akt, and Wnt3a signaling in HBV‐expressing HepAD38 cells treated by normal and LMD macrophages with or without GW3965. h) The induction of Nanog and Oct4 in LMD macrophage‐co‐cultured HBV + HepAD38 cells was reduced by knockdown of Stat3 . i) Knockdown of AKT had no effect on the expression of Nanog and Oct4 in LMD macrophage‐co‐cultured HBV + HepAD38 cells. j) The Venn diagram showed the overlapping differentially expressed proteins (DEPs) exhibiting opposite variation patterns before and after GW3965 addition within the macrophage‐HepAD38 crosstalk. The supernatants of the co‐culture system involving HepAD38/tet‐ and normal or LMD macrophages with or without GW3965 were subjected to Olink analysis and 7 DEPs who had opposite changing patterns before and after GW3965 treatment were selected. k) The inhibitory effect of neutralization of CCL19, CXCL10, or CXCL11 on the expression of Nanog and Oct4 in HepAD38/tet ‐ cells within the co‐culture system ( n = 3–6). Data are shown as mean ± SEM; * p< 0.05, ** p< 0.01, *** p< 0.001, **** p< 0.0001.
Compound Lin28 1632, supplied by Tocris, used in various techniques. Bioz Stars score: 91/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Proteintech antibody against lin28a
The regulation of CAT in CoCl 2 -induced H9c2 cells through SIRT5-mediated <t>Lin28a.</t> ( A-B ) The H9c2 cells were pretreated with CAT (10, 20, and 40 µmol/L) for 24 h before stimulating with CoCl 2 (400 µmol/L) for 24 h. The expressions of Lin28a mRNA ( A ) and protein ( B ) were determined by qRT-PCR and western blotting, respectively. Original blots are presented in Supplementary Fig. 6B and the samples derive from the same experiment and that blots were processed in parallel. ( C-D ) The H9c2 cells were stimulated with CoCl 2 (400 µmol/L) for 24 h after transfecting with SIRT5 siRNA or NC siRNA and pretreating with CAT (20 µmol/L). The expressions of Lin28a mRNA ( C ) and protein ( D ) were determined by qRT-PCR and western blotting, respectively. Original blots are presented in Supplementary Fig. 6D and the samples derive from the same experiment and that blots were processed in parallel. Data indicated the mean of three independent experiments ± SEM, n = 3. *p < 0.05, **p < 0.01 vs. control group; # p < 0.05, ## p < 0.01 vs. CoCl 2 group; $ p < 0.05, $$ p < 0.01 vs. CoCl 2 + CAT group.
Antibody Against Lin28a, supplied by Proteintech, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Santa Cruz Biotechnology lin 28 sirna
The regulation of CAT in CoCl 2 -induced H9c2 cells through SIRT5-mediated <t>Lin28a.</t> ( A-B ) The H9c2 cells were pretreated with CAT (10, 20, and 40 µmol/L) for 24 h before stimulating with CoCl 2 (400 µmol/L) for 24 h. The expressions of Lin28a mRNA ( A ) and protein ( B ) were determined by qRT-PCR and western blotting, respectively. Original blots are presented in Supplementary Fig. 6B and the samples derive from the same experiment and that blots were processed in parallel. ( C-D ) The H9c2 cells were stimulated with CoCl 2 (400 µmol/L) for 24 h after transfecting with SIRT5 siRNA or NC siRNA and pretreating with CAT (20 µmol/L). The expressions of Lin28a mRNA ( C ) and protein ( D ) were determined by qRT-PCR and western blotting, respectively. Original blots are presented in Supplementary Fig. 6D and the samples derive from the same experiment and that blots were processed in parallel. Data indicated the mean of three independent experiments ± SEM, n = 3. *p < 0.05, **p < 0.01 vs. control group; # p < 0.05, ## p < 0.01 vs. CoCl 2 group; $ p < 0.05, $$ p < 0.01 vs. CoCl 2 + CAT group.
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Image Search Results


List of primers used to detect mRNA expression of long noncoding RNA binding proteins

Journal: World Journal of Gastroenterology

Article Title: Long noncoding RNA ZNFX1-AS1 promotes the invasion and proliferation of gastric cancer cells by regulating LIN28 and CAPR1N1

doi: 10.3748/wjg.v28.i34.4973

Figure Lengend Snippet: List of primers used to detect mRNA expression of long noncoding RNA binding proteins

Article Snippet: LIN28, CAPRIN1, CEA, and CK20 were detected by enzyme-linked immunosorbent assay (ELISA) using a Mouse Protein lin-28 homolog A (Lin28a) ELISA Kit (ELISAGenie, Dublin, Ireland), a Human Caprin 1 (CAPRIN1) ELISA Kit (Abbexa, Cambridge, United Kingdom), a CEA ELISA Kit (Bioss, United Kingdom) and CK20 ELISA kits (FKBIO, Chengdu, China), respectively.

Techniques: Expressing, RNA Binding Assay

The relative mRNA levels of genes encoding ZNFX1-AS1 binding proteins in transduced BGC823 and SGC7901 cells were determined by quantitative reverse transcription polymerase chain reaction. A: UFP1; B: eIF4AIII; C: IGF2BP1; D: FMRP; E: LIN28; F: IGF2BP2; G: FUS; H: ZC3H7B; I: IGF2BP3; J: CAPRIN1. AFAS1: ZNFX1-AS1. a P < 0.05; b P < 0.01.

Journal: World Journal of Gastroenterology

Article Title: Long noncoding RNA ZNFX1-AS1 promotes the invasion and proliferation of gastric cancer cells by regulating LIN28 and CAPR1N1

doi: 10.3748/wjg.v28.i34.4973

Figure Lengend Snippet: The relative mRNA levels of genes encoding ZNFX1-AS1 binding proteins in transduced BGC823 and SGC7901 cells were determined by quantitative reverse transcription polymerase chain reaction. A: UFP1; B: eIF4AIII; C: IGF2BP1; D: FMRP; E: LIN28; F: IGF2BP2; G: FUS; H: ZC3H7B; I: IGF2BP3; J: CAPRIN1. AFAS1: ZNFX1-AS1. a P < 0.05; b P < 0.01.

Article Snippet: LIN28, CAPRIN1, CEA, and CK20 were detected by enzyme-linked immunosorbent assay (ELISA) using a Mouse Protein lin-28 homolog A (Lin28a) ELISA Kit (ELISAGenie, Dublin, Ireland), a Human Caprin 1 (CAPRIN1) ELISA Kit (Abbexa, Cambridge, United Kingdom), a CEA ELISA Kit (Bioss, United Kingdom) and CK20 ELISA kits (FKBIO, Chengdu, China), respectively.

Techniques: Binding Assay, Reverse Transcription Polymerase Chain Reaction

The relative protein levels of LIN28 and CAPRIN1 in transduced BGC823 and SGC7901 cells were determined by enzyme-linked immunosorbent assay. A: The levels of CAPRIN1 in transduced BGC823 cells; B: The levels of CAPRIN1 in transduced SGC7901 cells; C: The levels of LIN28 in transduced BGC823 cells; D: The levels of LIN28 in transduced SGC7901 cells. a P < 0.05; b P < 0.01.

Journal: World Journal of Gastroenterology

Article Title: Long noncoding RNA ZNFX1-AS1 promotes the invasion and proliferation of gastric cancer cells by regulating LIN28 and CAPR1N1

doi: 10.3748/wjg.v28.i34.4973

Figure Lengend Snippet: The relative protein levels of LIN28 and CAPRIN1 in transduced BGC823 and SGC7901 cells were determined by enzyme-linked immunosorbent assay. A: The levels of CAPRIN1 in transduced BGC823 cells; B: The levels of CAPRIN1 in transduced SGC7901 cells; C: The levels of LIN28 in transduced BGC823 cells; D: The levels of LIN28 in transduced SGC7901 cells. a P < 0.05; b P < 0.01.

Article Snippet: LIN28, CAPRIN1, CEA, and CK20 were detected by enzyme-linked immunosorbent assay (ELISA) using a Mouse Protein lin-28 homolog A (Lin28a) ELISA Kit (ELISAGenie, Dublin, Ireland), a Human Caprin 1 (CAPRIN1) ELISA Kit (Abbexa, Cambridge, United Kingdom), a CEA ELISA Kit (Bioss, United Kingdom) and CK20 ELISA kits (FKBIO, Chengdu, China), respectively.

Techniques: Enzyme-linked Immunosorbent Assay

Effect of ZNFX1-AS1 on gastric cancer cell tumorigenesis in vivo . A: The expression of long noncoding RNA ZNFX1-AS1 in BALB/c nude mice was detected weekly by quantitative reverse transcription polymerase chain reaction; B and C: Images of tumors from BALB/c nude mice; D and E: Tumor size and weight were measured weekly; F: Expression of LIN28 and CAPRIN1 in tumors of BALB/c nude mice; G: Expression of carcinoembryonic antigen and CK20 in lymph nodes of BALB/c nude mice. CEA: Carcinoembryonic antigen; ZFAS1: ZNFX1-AS1. a P < 0.05; b P < 0.01; c P < 0.001.

Journal: World Journal of Gastroenterology

Article Title: Long noncoding RNA ZNFX1-AS1 promotes the invasion and proliferation of gastric cancer cells by regulating LIN28 and CAPR1N1

doi: 10.3748/wjg.v28.i34.4973

Figure Lengend Snippet: Effect of ZNFX1-AS1 on gastric cancer cell tumorigenesis in vivo . A: The expression of long noncoding RNA ZNFX1-AS1 in BALB/c nude mice was detected weekly by quantitative reverse transcription polymerase chain reaction; B and C: Images of tumors from BALB/c nude mice; D and E: Tumor size and weight were measured weekly; F: Expression of LIN28 and CAPRIN1 in tumors of BALB/c nude mice; G: Expression of carcinoembryonic antigen and CK20 in lymph nodes of BALB/c nude mice. CEA: Carcinoembryonic antigen; ZFAS1: ZNFX1-AS1. a P < 0.05; b P < 0.01; c P < 0.001.

Article Snippet: LIN28, CAPRIN1, CEA, and CK20 were detected by enzyme-linked immunosorbent assay (ELISA) using a Mouse Protein lin-28 homolog A (Lin28a) ELISA Kit (ELISAGenie, Dublin, Ireland), a Human Caprin 1 (CAPRIN1) ELISA Kit (Abbexa, Cambridge, United Kingdom), a CEA ELISA Kit (Bioss, United Kingdom) and CK20 ELISA kits (FKBIO, Chengdu, China), respectively.

Techniques: In Vivo, Expressing, Reverse Transcription Polymerase Chain Reaction

Induction of HCSC from HBV‐expressing HepAD38 cells by LMD macrophages. a) GSEA analysis showing dysregulated pathway of regulating pluripotency of stem cells in the hepatocytes of the CHB mice at 12 mpi. b) Induction of Yamanaka factors ( Nanog , Oct4 , Klf4 , c‐Myc , Lin28A ) in HBV‐expressing HepAD38 cells treated by macrophages with or without LMD. THP‐derived macrophages were treated with HepAD38 (tet ‐ or tet + ) cells for 48 h, and then co‐cultured with another well of HBV‐expressing HepAD38 in a Transwell plate for another 48 h. The experiments were conducted in triplicate ( n = 3). c) The representative images of Nanog‐positive HCSC (red) surrounded by LXRα‐negative (low or absent of green) Kupffer cells (F4/80, grey) by mIF analysis of liver sections from the control and AAV‐HBV mice at 12 months and 27 months. d) LXR agonist GW3965 significantly reduced the increased mRNA level of pluripontency inducers in HBV‐expressing HepAD38 co‐cultured with LMD macrophages. The experiments were conducted in triplicate ( n = 3). e) The representative bright field images of spheroids formed from HBV‐expressing HepAD38 cells treated by the normal and LMD macrophages with or without GW3965. f) The average of Feret's diameter of the spheroids and the percentage of spheroids with a diameter larger than 50 µm were analyzed. The experiments were performed in triplicate ( n = 3). g) Western blot analysis of Yamanaka factors and the activation of STAT3, Akt, and Wnt3a signaling in HBV‐expressing HepAD38 cells treated by normal and LMD macrophages with or without GW3965. h) The induction of Nanog and Oct4 in LMD macrophage‐co‐cultured HBV + HepAD38 cells was reduced by knockdown of Stat3 . i) Knockdown of AKT had no effect on the expression of Nanog and Oct4 in LMD macrophage‐co‐cultured HBV + HepAD38 cells. j) The Venn diagram showed the overlapping differentially expressed proteins (DEPs) exhibiting opposite variation patterns before and after GW3965 addition within the macrophage‐HepAD38 crosstalk. The supernatants of the co‐culture system involving HepAD38/tet‐ and normal or LMD macrophages with or without GW3965 were subjected to Olink analysis and 7 DEPs who had opposite changing patterns before and after GW3965 treatment were selected. k) The inhibitory effect of neutralization of CCL19, CXCL10, or CXCL11 on the expression of Nanog and Oct4 in HepAD38/tet ‐ cells within the co‐culture system ( n = 3–6). Data are shown as mean ± SEM; * p< 0.05, ** p< 0.01, *** p< 0.001, **** p< 0.0001.

Journal: Advanced Science

Article Title: CHB‐Induced Immune Zonation Chaos Elicited LXRα‐mediated Lipid Metabolism Disorders in Kupffer Cells to Induce Cancer Stem Cell Formation

doi: 10.1002/advs.202510275

Figure Lengend Snippet: Induction of HCSC from HBV‐expressing HepAD38 cells by LMD macrophages. a) GSEA analysis showing dysregulated pathway of regulating pluripotency of stem cells in the hepatocytes of the CHB mice at 12 mpi. b) Induction of Yamanaka factors ( Nanog , Oct4 , Klf4 , c‐Myc , Lin28A ) in HBV‐expressing HepAD38 cells treated by macrophages with or without LMD. THP‐derived macrophages were treated with HepAD38 (tet ‐ or tet + ) cells for 48 h, and then co‐cultured with another well of HBV‐expressing HepAD38 in a Transwell plate for another 48 h. The experiments were conducted in triplicate ( n = 3). c) The representative images of Nanog‐positive HCSC (red) surrounded by LXRα‐negative (low or absent of green) Kupffer cells (F4/80, grey) by mIF analysis of liver sections from the control and AAV‐HBV mice at 12 months and 27 months. d) LXR agonist GW3965 significantly reduced the increased mRNA level of pluripontency inducers in HBV‐expressing HepAD38 co‐cultured with LMD macrophages. The experiments were conducted in triplicate ( n = 3). e) The representative bright field images of spheroids formed from HBV‐expressing HepAD38 cells treated by the normal and LMD macrophages with or without GW3965. f) The average of Feret's diameter of the spheroids and the percentage of spheroids with a diameter larger than 50 µm were analyzed. The experiments were performed in triplicate ( n = 3). g) Western blot analysis of Yamanaka factors and the activation of STAT3, Akt, and Wnt3a signaling in HBV‐expressing HepAD38 cells treated by normal and LMD macrophages with or without GW3965. h) The induction of Nanog and Oct4 in LMD macrophage‐co‐cultured HBV + HepAD38 cells was reduced by knockdown of Stat3 . i) Knockdown of AKT had no effect on the expression of Nanog and Oct4 in LMD macrophage‐co‐cultured HBV + HepAD38 cells. j) The Venn diagram showed the overlapping differentially expressed proteins (DEPs) exhibiting opposite variation patterns before and after GW3965 addition within the macrophage‐HepAD38 crosstalk. The supernatants of the co‐culture system involving HepAD38/tet‐ and normal or LMD macrophages with or without GW3965 were subjected to Olink analysis and 7 DEPs who had opposite changing patterns before and after GW3965 treatment were selected. k) The inhibitory effect of neutralization of CCL19, CXCL10, or CXCL11 on the expression of Nanog and Oct4 in HepAD38/tet ‐ cells within the co‐culture system ( n = 3–6). Data are shown as mean ± SEM; * p< 0.05, ** p< 0.01, *** p< 0.001, **** p< 0.0001.

Article Snippet: Primary antibodies against LXRα (#14352‐1‐AP), ASGR1 (#11739‐1‐AP), BRCA1 (#22362‐1‐AP), BARD1 (#22964‐1‐AP), NANOG (#14295‐1‐AP), LIN28 (#11724‐1‐AP), OCT4 (#11263‐1‐AP), STAT3 (#10253‐1‐AP), WNT3A (#26744‐1‐AP), and CXCL9 (#22355‐1‐AP), were purchased from Proteintech (Wuhan, China).

Techniques: Expressing, Derivative Assay, Cell Culture, Control, Western Blot, Activation Assay, Knockdown, Co-Culture Assay, Neutralization

The regulation of CAT in CoCl 2 -induced H9c2 cells through SIRT5-mediated Lin28a. ( A-B ) The H9c2 cells were pretreated with CAT (10, 20, and 40 µmol/L) for 24 h before stimulating with CoCl 2 (400 µmol/L) for 24 h. The expressions of Lin28a mRNA ( A ) and protein ( B ) were determined by qRT-PCR and western blotting, respectively. Original blots are presented in Supplementary Fig. 6B and the samples derive from the same experiment and that blots were processed in parallel. ( C-D ) The H9c2 cells were stimulated with CoCl 2 (400 µmol/L) for 24 h after transfecting with SIRT5 siRNA or NC siRNA and pretreating with CAT (20 µmol/L). The expressions of Lin28a mRNA ( C ) and protein ( D ) were determined by qRT-PCR and western blotting, respectively. Original blots are presented in Supplementary Fig. 6D and the samples derive from the same experiment and that blots were processed in parallel. Data indicated the mean of three independent experiments ± SEM, n = 3. *p < 0.05, **p < 0.01 vs. control group; # p < 0.05, ## p < 0.01 vs. CoCl 2 group; $ p < 0.05, $$ p < 0.01 vs. CoCl 2 + CAT group.

Journal: Scientific Reports

Article Title: Catalpol improved energy metabolism and inflammation through the SIRT5-mediated signaling pathway to ameliorate myocardial injury

doi: 10.1038/s41598-024-80505-z

Figure Lengend Snippet: The regulation of CAT in CoCl 2 -induced H9c2 cells through SIRT5-mediated Lin28a. ( A-B ) The H9c2 cells were pretreated with CAT (10, 20, and 40 µmol/L) for 24 h before stimulating with CoCl 2 (400 µmol/L) for 24 h. The expressions of Lin28a mRNA ( A ) and protein ( B ) were determined by qRT-PCR and western blotting, respectively. Original blots are presented in Supplementary Fig. 6B and the samples derive from the same experiment and that blots were processed in parallel. ( C-D ) The H9c2 cells were stimulated with CoCl 2 (400 µmol/L) for 24 h after transfecting with SIRT5 siRNA or NC siRNA and pretreating with CAT (20 µmol/L). The expressions of Lin28a mRNA ( C ) and protein ( D ) were determined by qRT-PCR and western blotting, respectively. Original blots are presented in Supplementary Fig. 6D and the samples derive from the same experiment and that blots were processed in parallel. Data indicated the mean of three independent experiments ± SEM, n = 3. *p < 0.05, **p < 0.01 vs. control group; # p < 0.05, ## p < 0.01 vs. CoCl 2 group; $ p < 0.05, $$ p < 0.01 vs. CoCl 2 + CAT group.

Article Snippet: The antibody against Lin28a was obtained from Proteintech (Wuhan, China).

Techniques: Quantitative RT-PCR, Western Blot, Control

Primer sequences used for qRT-PCR.

Journal: Scientific Reports

Article Title: Catalpol improved energy metabolism and inflammation through the SIRT5-mediated signaling pathway to ameliorate myocardial injury

doi: 10.1038/s41598-024-80505-z

Figure Lengend Snippet: Primer sequences used for qRT-PCR.

Article Snippet: The antibody against Lin28a was obtained from Proteintech (Wuhan, China).

Techniques: