anti chrebp  (Cell Signaling Technology Inc)

Journal: Frontiers in Endocrinology

Article Title: Integrated causal inference, kidney transcriptomics, and experimental validation identify ChREBP ( MLXIPL ) as a driver of maladaptive metabolic remodeling in diabetic kidney disease

doi: 10.3389/fendo.2026.1809567

Figure Lengend Snippet: Experimental validation of MLXIPL upregulation and metabolic network consistency in diabetic models. (A–C) Assessment of ChREBP expression in kidney tissues from db/m and db/db mice. Representative Western blots (A) and densitometric quantification (B) of ChREBP protein levels. For animal Western blot analyses, densitometric quantification was performed using all 12 mice per group. Full-length immunoblot images are provided in Supplementary Figure 4 . (C) Relative mRNA expression of Mlxipl . (D–F) Assessment of ChREBP expression in primary proximal tubular epithelial cells (PTECs) under normal glucose (NC) and high glucose (HG) conditions. Representative Western blots (D) , protein quantification (E) , and mRNA levels (F) . (G) Representative immunohistochemistry (IHC) staining of ChREBP in mouse kidney sections. Scale bar: 100 μm. (H) Representative immunofluorescence (IF) staining of ChREBP (green) in PTECs; nuclei were counterstained with DAPI (blue). Scale bar: 50 μm. (I) Relative mRNA expression of MLXIPL -interacting metabolic genes in mouse kidneys. (J) Pearson correlation analysis between Mlxipl expression and downstream metabolic targets in kidney tissues.Data are presented as mean ± SD. *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001.

Article Snippet: Sections were blocked with 1% BSA and incubated with anti-ChREBP antibody (Novus Biologicals, NB400-135; IHC dilution 1:200), followed by appropriate secondary antibodies and chromogenic development.

Techniques: Biomarker Discovery, Expressing, Western Blot, Immunohistochemistry, Immunofluorescence, Staining

Journal: Journal of Lipid Research

Article Title: LYPLAL1 rare loss-of-function variants in humans and deletion in human hepatoma cells protect against MASLD

doi: 10.1016/j.jlr.2026.101013

Figure Lengend Snippet: LYPLAL1 knockout alters the expression of metabolic regulators and mitochondrial β-oxidation processes. A: mRNA levels of transcription factors MLXIPL and PPARα without oleic acid (OA) and with 200 μM OA. B and C: mRNA levels of (B) de novo lipogenesis genes and (C) β-oxidation genes with and without 200 μM OA treatment. D: Representative histograms and relative mean fluorescence intensity (MFI) showing protein levels of major β-oxidation enzymes ACADVL, ACADM, and HADHA without oleic acid and with 200 μM OA. E: Seahorse XF assay for mitochondrial oxygen consumption rate (OCR) in vehicle or etomoxir treated HuH-7 and LYPLAL1 KO cells without oleic acid and with 200 μM OA. Port A: Etomoxir (4 μM), port B: Oligomycin (1.5 μM), port C: FCCP (0.5 μM), and port D: Rotenone/antimycin A (0.5 μM). F: Maximal oxygen consumption rate (OCR) with vehicle or etomoxir treated HuH-7 and LYPLAL1 KO cells without oleic acid and with 200 μM OA. LYP KO = LYPLAL1 KO, Eto = Etomoxir. G: Vehicle treated (<1% DMSO) and etomoxir treated (100 μM) HuH-7 and LYPLAL1 KO cells with 200 μM OA. Cells were treated with etomoxir and oleic acid for 24 h. Data represented as mean ± S.E.M. ns: P > 0.05, ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, ∗∗∗∗ P < 0.0001.

Article Snippet: Probes used: GAPDH (Hs02786624_g1), ELF1 (Hs01111177_m1), MLXIPL (Hs00975714_m1), PPARα (Hs00947536_m1), ACACA (Hs01046047_m1), ACLY (Hs00982738_m1), FASN (Hs01005622_m1), SCD (Hs01682761_m1), CPT1A (Hs00912671_m1), ACADL (Hs00155630_m1), ACADM (Hs00936584_m1), ACADVL (Hs00825606_g1), EHHADH (Hs00157347_m1), HADHA (Hs00426191_m1), CD36 (Hs00354519_m1), and FABP1 (Hs00155026_m1).

Techniques: Knock-Out, Expressing, Fluorescence, XF Assay

Journal: Journal of Lipid Research

Article Title: LYPLAL1 rare loss-of-function variants in humans and deletion in human hepatoma cells protect against MASLD

doi: 10.1016/j.jlr.2026.101013

Figure Lengend Snippet: Effects of CRISPRa induced LYPLAL1 overexpression on lipid accumulation. A: Relative mRNA levels of LYPLAL1 and (B) Representative images of HuH-7 expressing dCas9-SAM (left column marked as vector) and LYPLAL1a (right column) cells stained with Hoechst (blue), CellMask (red), and LipidTOX™ Green (green). Images shown for cells treated with 250 μM oleic acid (OA). Scale bars = 50 μm. C: Quantified integrated intensity (using CellProfiler) of lipid-stained cells at various doses of oleic acid. D: Relative mRNA levels of transcription factors MLXIPL and PPARα and β-oxidation regulator CPT1A without oleic acid and with 200 μM OA. Data represented as mean ± S.E.M. ns: P > 0.05, ∗ P < 0.05, ∗∗ P < 0.01, ∗∗∗ P < 0.001, ∗∗∗∗ P < 0.0001.

Article Snippet: Probes used: GAPDH (Hs02786624_g1), ELF1 (Hs01111177_m1), MLXIPL (Hs00975714_m1), PPARα (Hs00947536_m1), ACACA (Hs01046047_m1), ACLY (Hs00982738_m1), FASN (Hs01005622_m1), SCD (Hs01682761_m1), CPT1A (Hs00912671_m1), ACADL (Hs00155630_m1), ACADM (Hs00936584_m1), ACADVL (Hs00825606_g1), EHHADH (Hs00157347_m1), HADHA (Hs00426191_m1), CD36 (Hs00354519_m1), and FABP1 (Hs00155026_m1).

Techniques: Over Expression, Expressing, Plasmid Preparation, Staining