Journal: Journal of pharmacological sciences

Article Title: Oligo-peptide I-C-F-6 inhibits hepatic stellate cell activation and ameliorates CCl 4 -induced liver fibrosis by suppressing NF-κB signaling and Wnt/β-catenin signaling.

doi: 10.1016/j.jphs.2018.01.003

Figure Lengend Snippet: Fig. 3. The effects of oligo-peptide I-C-F-6 on HSC activation markers and cytokine levels. (A) The immunohistochemistry of TGF-b1 and a-SMA. Magnification, 200. (B) The effects of oligo-peptide I-C-F-6 on TGF-b1 and a-SMA levels in vitro. The data are expressed as the means ± SD of three independent experiments. *P < 0.05, **P < 0.01 compared with 0 mg/ mL. (C) The effects of oligo-peptide I-C-F-6 on TGF-b1 and a-SMA levels in vivo. (DeG) Serum levels of CTGF, TNF-a, VEGF, TGF-b1. Data are expressed as means ± SD (n ¼ 6e8). #P < 0.05, ##P < 0.01 compared with the control group; *P < 0.05, **P < 0.01 compared with the CCl4 group.

Article Snippet: The MMP-2, MMP-9, TIPM-1, CTGF, TGF-b1, TNF-a, and VEGF ELISA kits were purchased from Cusabio Biotech (Wuhan, China).

Techniques: Activation Assay, Immunohistochemistry, In Vitro, In Vivo, Control

Journal: Molecular Pharmaceutics

Article Title: NQO2 Is a Reactive Oxygen Species Generating Off-Target for Acetaminophen

doi: 10.1021/mp5004866

Figure Lengend Snippet: NQO2 protein and mRNA levels in normal human tissues. Tissue Western blot displays unknown NQO2 variants in skeletal muscle. For quantifications, mRNA and protein levels were normalized to NQO2 in liver. See also Figure S3.

Article Snippet: Human Normal Tissue Blot II was obtained from ProSci Incorporated (Poway, CA) and stained with NQO2 antibody.

Techniques: Western Blot

Journal: Scientific Reports

Article Title: Tracing the invisible mutant ADNP protein in Helsmoortel-Van der Aa syndrome patients

doi: 10.1038/s41598-024-65608-x

Figure Lengend Snippet: Overview of the reported ADNP antibodies with indication of the observed molecular weights and tested sample materials.

Article Snippet: Adult human brain (NB820-59177), human brain cerebellum (NB820-59180), human brain frontal lobe (NB820- 59186), and human brain hippocampus whole tissue lysates (NB820-59187) from a healthy 45-year-old male subject were purchased from Novus Biologicals.

Techniques: Molecular Weight, Transfection, Expressing, Construct

Journal: Scientific Reports

Article Title: Tracing the invisible mutant ADNP protein in Helsmoortel-Van der Aa syndrome patients

doi: 10.1038/s41598-024-65608-x

Figure Lengend Snippet: A polyclonal N-terminal ADNP antibody from Aviva Systems detects ADNP specifically in murine and rat tissues and suggests proteolytic processing of the protein in the human brain. Cerebellum, frontal cortex or lobe, hippocampus and whole brains of control mice, rats and humans were lysed in RIPA buffer and used as protein samples for the assessment of N-terminal antibody of Aviva systems. (A – C) The predicted molecular weight of ADNP is 124 kDa. The antibody recognizes ADNP in a range of 145 kDa with (E) additional lower mass signal of 85 kDa in all human brain regions. (B – D – F) Western blot analysis of the blocking peptide competition assay. Supplementation of the immunization peptide in a 5 × excess to antibody concentration reduced the signal observed at 145 kDa in all tested cell lines. Importantly, the 85 kDa band suggestive for proteolytic cleavage as well as degraded ADNP signal disappeared completely after immunization peptide supplementation. GAPDH was used as a loading control.

Article Snippet: Adult human brain (NB820-59177), human brain cerebellum (NB820-59180), human brain frontal lobe (NB820- 59186), and human brain hippocampus whole tissue lysates (NB820-59187) from a healthy 45-year-old male subject were purchased from Novus Biologicals.

Techniques: Control, Molecular Weight, Western Blot, Blocking Assay, Competitive Binding Assay, Concentration Assay

Journal: Scientific Reports

Article Title: Tracing the invisible mutant ADNP protein in Helsmoortel-Van der Aa syndrome patients

doi: 10.1038/s41598-024-65608-x

Figure Lengend Snippet: Different C-terminal ADNP antibodies detect ADNP in the range of 150 kDa and suggest proteolytic processing of the protein in the brain. Cerebellum, frontal cortex or lobe, hippocampus and whole brains of control mice, rats, and humans were lysed in RIPA buffer and used as protein samples for the assessment with three C-terminal antibodies with the optimized dilutions listed in Table . GAPDH was used as a loading control. The predicted molecular weight of ADNP is 124 kDa. ( A ) C ) Murine samples indicate detection of ADNP in the range of 150 kDa with bands suggesting proteolytic processing at 50 kDa. ( D – F ) Rat samples indicate detection of ADNP in the range of 150 kDa with bands indicating proteolytic processing at 82 kDa after incubation with the C-terminal Abcam antibody. ( G – I ) Human brain samples indicate detection of ADNP at different molecular weights of 124 – 150 kDa in the adult frontal lobe and hippocampus and highlight the antibody differences in detection of ADNP. The three tested antibodies showed strong band signals at lower molecular weights, which could indicate proteolytic cleavage or degradation of the protein.

Article Snippet: Adult human brain (NB820-59177), human brain cerebellum (NB820-59180), human brain frontal lobe (NB820- 59186), and human brain hippocampus whole tissue lysates (NB820-59187) from a healthy 45-year-old male subject were purchased from Novus Biologicals.

Techniques: Control, Molecular Weight, Incubation