Journal: Chinese Medicine

Article Title: Matrine improves bile acid metabolism and reduces inflammatory and oxidative stress in colitis via the JAK2 pathway

doi: 10.1186/s13020-026-01387-z

Figure Lengend Snippet: Effects of matrine on intestinal pathology, inflammatory function, and JAK2 expression in experimental colitis mice Dextran Sulfate Sodium (DSS)-induced murine model of colitis was established in mice; matrine and 5-ASA treatment was administered as described. A – C Body weight and colon length were measured. D , E Histopathological alterations in colon tissues were evaluated using H & E staining; DAI scores were assigned according to the staining. F , G The levels of IL-1β, TNF-α, IL-6, MPO, NO, and MDA in colon tissues were examined using commercial assay kits. H , I The protein levels of JAK2 in mice colon tissues were determined using Immunohistochemical staining (IHC staining) and Immunoblotting. Magnification = 100 × or 200 × for IHC staining. J The protein levels of p-JAK2, p-STAT3, and STAT3 were detected using Immunoblotting. **p < 0.01, vs. PBS group; #p < 0.05, ##p < 0.01 vs. DSS group

Article Snippet: Membrane was blocked within Odyssey blocking buffer (LI-COR Bioscience, Lincoln, USA) for 1 h at room temperature (RT), and then incubated with primary antibodies against p-JAK2 (AP0917, Abclonal, Woburn, USA), JAK2 (AF6022, Affinitiy Bioscience, Changzhou, China), MRP3 (bs-0656R, Bioss, Beijing, China), MRP4 (DF6921, Affinity Bioscience), IL-1β [12242, Cell Signaling Technology (CST), Danvers, USA], TNF-α (11948, CST), IL-6 (CSB-PA06757A0RB, CUSABIO, Wuhan, China), p-STAT3 (AF3293, Affinity Bioscience), STAT3 (10253-2-AP, Proteintech, Wuhan, China), p-STAT1 (28977-1-AP, Protientech), STAT1 (10144-2-AP, Proteintech), FXR (M022312, Abmart, Shanghai, China), and GAPDH (endogenous control, 60004-1-Ig, Proteintech) overnight at 4 °C (dilution 1:1000).

Techniques: Expressing, Staining, Immunohistochemical staining, Immunohistochemistry, Western Blot

Journal: Chinese Medicine

Article Title: Matrine improves bile acid metabolism and reduces inflammatory and oxidative stress in colitis via the JAK2 pathway

doi: 10.1186/s13020-026-01387-z

Figure Lengend Snippet: Effects of JAK2 overexpression on intestinal epithelial cells upon inflammation MODE-K cells were transfected with a JAK2-overexpressing plasmid (JAK2 oe) or a control vector, with or without subsequent LPS stimulation. A The protein levels of JAK2 and p-JAK2 and the inflammatory factors IL-1β, TNF-α, and IL-6 were determined by Immunoblotting. B Cellular levels of MPO, NO, and MDA were measured using biochemical kits. C Intracellular ROS production was assessed by DCFH-DA staining and quantified with flow cytometry. D The protein levels of the bile acid metabolism-related factors FXR, MRP3 and MRP4 were examined by Immunoblotting. E The mRNA levels of MRP3, MRP4, OSTα, and OSTβ were measured by qRT-PCR. **p < 0.01 vs. Vector group; ##p < 0.01 vs. Vector group; &&p < 0.01 vs. LPS + Vector group

Article Snippet: Membrane was blocked within Odyssey blocking buffer (LI-COR Bioscience, Lincoln, USA) for 1 h at room temperature (RT), and then incubated with primary antibodies against p-JAK2 (AP0917, Abclonal, Woburn, USA), JAK2 (AF6022, Affinitiy Bioscience, Changzhou, China), MRP3 (bs-0656R, Bioss, Beijing, China), MRP4 (DF6921, Affinity Bioscience), IL-1β [12242, Cell Signaling Technology (CST), Danvers, USA], TNF-α (11948, CST), IL-6 (CSB-PA06757A0RB, CUSABIO, Wuhan, China), p-STAT3 (AF3293, Affinity Bioscience), STAT3 (10253-2-AP, Proteintech, Wuhan, China), p-STAT1 (28977-1-AP, Protientech), STAT1 (10144-2-AP, Proteintech), FXR (M022312, Abmart, Shanghai, China), and GAPDH (endogenous control, 60004-1-Ig, Proteintech) overnight at 4 °C (dilution 1:1000).

Techniques: Over Expression, Transfection, Plasmid Preparation, Control, Western Blot, Staining, Flow Cytometry, Quantitative RT-PCR

Journal: Chinese Medicine

Article Title: Matrine improves bile acid metabolism and reduces inflammatory and oxidative stress in colitis via the JAK2 pathway

doi: 10.1186/s13020-026-01387-z

Figure Lengend Snippet: Effects of matrine on intestinal epithelial cell function upon inflammation Mouse intestinal epithelial cell line, MODE-K, was stimulated with LPS with or without matrine treatment (1, 2, 3 mg/ml), and examined for the protein levels of IL-1β, TNF-α, and IL-6 using Immunoblotting ( A ); The levels of MPO, NO, and MDA using commercial kits ( B ); Intracellular ROS levels were detected by flow cytometry ( C ); The protein levels of FXR, MRP3 and MRP4 were examined using Immunoblotting ( D ); The mRNA levels of MRP3, MRP4, OSTα and OSTβ were examined using qRT-PCR ( E ); The protein levels of p-JAK2, JAK2, p-STAT3, STAT3, p-STAT1, and STAT1 using Immunoblotting ( F ). **p < 0.01, vs. PBS group; #p < 0.05, ##p < 0.01 vs. LPS group

Article Snippet: Membrane was blocked within Odyssey blocking buffer (LI-COR Bioscience, Lincoln, USA) for 1 h at room temperature (RT), and then incubated with primary antibodies against p-JAK2 (AP0917, Abclonal, Woburn, USA), JAK2 (AF6022, Affinitiy Bioscience, Changzhou, China), MRP3 (bs-0656R, Bioss, Beijing, China), MRP4 (DF6921, Affinity Bioscience), IL-1β [12242, Cell Signaling Technology (CST), Danvers, USA], TNF-α (11948, CST), IL-6 (CSB-PA06757A0RB, CUSABIO, Wuhan, China), p-STAT3 (AF3293, Affinity Bioscience), STAT3 (10253-2-AP, Proteintech, Wuhan, China), p-STAT1 (28977-1-AP, Protientech), STAT1 (10144-2-AP, Proteintech), FXR (M022312, Abmart, Shanghai, China), and GAPDH (endogenous control, 60004-1-Ig, Proteintech) overnight at 4 °C (dilution 1:1000).

Techniques: Cell Function Assay, Western Blot, Flow Cytometry, Quantitative RT-PCR

Journal: Chinese Medicine

Article Title: Matrine improves bile acid metabolism and reduces inflammatory and oxidative stress in colitis via the JAK2 pathway

doi: 10.1186/s13020-026-01387-z

Figure Lengend Snippet: Dynamic effects of matrine and JAK2 on intestinal epithelial cell function upon inflammation MODE-K cells were stimulated with LPS with or without matrine treatment (2 mg/ml), transfected with JAK2-overexpressing plasmid (JAK2 oe), and examined for the protein levels of IL-1β, TNF-α, and IL-6 using Immunoblotting ( A ); the levels of MPO, NO, and MDA using commercial kits ( B ); Intracellular ROS levels were detected by flow cytometry ( C ); The protein levels of FXR, MRP3 and MRP4 were examined using Immunoblotting ( D ); The mRNA levels of MRP3, MRP4, OSTα and OSTβ were examined using qRT-PCR ( E ); the protein levels of JAK2, p-STAT3, STAT3, p-STAT1, and STAT1 using Immunoblotting ( F ). **p < 0.01, vs. LPS group; #p < 0.05, ## p < 0.01 vs. LPS + matrine + vector group

Article Snippet: Membrane was blocked within Odyssey blocking buffer (LI-COR Bioscience, Lincoln, USA) for 1 h at room temperature (RT), and then incubated with primary antibodies against p-JAK2 (AP0917, Abclonal, Woburn, USA), JAK2 (AF6022, Affinitiy Bioscience, Changzhou, China), MRP3 (bs-0656R, Bioss, Beijing, China), MRP4 (DF6921, Affinity Bioscience), IL-1β [12242, Cell Signaling Technology (CST), Danvers, USA], TNF-α (11948, CST), IL-6 (CSB-PA06757A0RB, CUSABIO, Wuhan, China), p-STAT3 (AF3293, Affinity Bioscience), STAT3 (10253-2-AP, Proteintech, Wuhan, China), p-STAT1 (28977-1-AP, Protientech), STAT1 (10144-2-AP, Proteintech), FXR (M022312, Abmart, Shanghai, China), and GAPDH (endogenous control, 60004-1-Ig, Proteintech) overnight at 4 °C (dilution 1:1000).

Techniques: Cell Function Assay, Transfection, Plasmid Preparation, Western Blot, Flow Cytometry, Quantitative RT-PCR

Journal: bioRxiv

Article Title: EOLA1, a novel mitochondria-localized protein critical for heart functions via regulating mitochondrial translation

doi: 10.64898/2026.01.12.699056

Figure Lengend Snippet: a, Evolutionary analysis of the ASCH domain reveals high conservation across species. b, A scheme showing functional domains of EOLA1 in Homo sapiens (top) and Mus musculus (bottom). The ASCH domain is shown in red. c, Schematic diagram of sgRNA targeting mouse Eola1 locus. d, Western blotting analysis confirming Eola1 knockout clones in B16-F10 and HL-1 cell lines with anti-EOLA1 antibody. GAPDH was used as a loading control. e, Sanger sequencing results of Eola1 KO cell lines with genetic mutations introduced with the CRISPR/Cas9 system.

Article Snippet: The corresponding antibodies included anti-EOLA1 antibody (1:5000, CUSABIO, CSB-PA837446LA01HU), anti-HSP60 antibody (1:3000, Proteintech, 15282-1-AP), anti-Tom20 antibody (1:1000, ABclonal, A19403), anti-α-Tubulin antibody (1:3000, Proteintech, 80762-1-RR), anti-HistoneH1.2 antibody (1:1000, Proteintech, 19649-1-AP), anti-TUFM antibody (1:1000, SAB, 34669), anti-FLAG antibody (1:1000, Sigma, F1804), anti-MRPS15 antibody (1:1000, Proteintech, 17006-1-AP), anti-MRPL11 antibody (1:1000, Proteintech, 15543-1-AP), anti-ATP6 antibody (1:500, SAB, 31464), Anti-COX1 antibody (1:500, ABclonal, A23123), anti-MT-ND5 antibody (1:500, Proteintech, 55410-1-AP), anti-β-actin antibody (SAB, 52901), and anti-GAPDH antibody (1:5000, Proteintech, 10494-1-AP).

Techniques: Functional Assay, Western Blot, Knock-Out, Clone Assay, Control, Sequencing, CRISPR

Journal: bioRxiv

Article Title: EOLA1, a novel mitochondria-localized protein critical for heart functions via regulating mitochondrial translation

doi: 10.64898/2026.01.12.699056

Figure Lengend Snippet: a , Schematic diagram of screening strategy. Cell populations with sgRNA library were cultured in glucose medium or galactose medium (galactose was used to replace glucose) for 48 hours. Dead cells from galactose medium or living cells from glucose medium were collected to carry out next-generation sequencing for evaluating the abundance of sgRNAs. b , Genes essential for mitochondrial oxidative phosphorylation (OXPHOS) -linked energy metabolism were identified in the screening. A rank-ordered plot shows the RRA (Robust Rank Aggregation) scores and corresponding p -values from the CRISPR screening results. c , Fold change (FC) distribution of sgRNAs targeting Eola1, Sp1, Stat1, and Samhd1 as indicated in red (upregulated) and blue (downregulated) lines, overlaid on gray gradient depicting the overall distribution. d , e , Growth curves of wild-type (WT) and EOLA1 KO cells cultured in the medium of glucose ( d ) or galactose ( e ). f , Eola1 depletion dramatically induced cell apoptosis when cancer cells cultured in galactose medium. Representative flow cytometry images (left) and quantification analysis (right) of the apoptotic B16-F10 melanoma cells and HL-1 cells cultured in glucose medium or galactose medium for 48 hours. FITC: fluorescein isothiocyanate; PI: propidium iodide. Note: d , e , One-way ANOVA with Tukey’s test. f , two-tailed unpaired Student’s t-tests. * P <0.05, **** P <0.0001, ns: not significant. d , e , f , Data were presented as mean ± SD (n=3).

Article Snippet: The corresponding antibodies included anti-EOLA1 antibody (1:5000, CUSABIO, CSB-PA837446LA01HU), anti-HSP60 antibody (1:3000, Proteintech, 15282-1-AP), anti-Tom20 antibody (1:1000, ABclonal, A19403), anti-α-Tubulin antibody (1:3000, Proteintech, 80762-1-RR), anti-HistoneH1.2 antibody (1:1000, Proteintech, 19649-1-AP), anti-TUFM antibody (1:1000, SAB, 34669), anti-FLAG antibody (1:1000, Sigma, F1804), anti-MRPS15 antibody (1:1000, Proteintech, 17006-1-AP), anti-MRPL11 antibody (1:1000, Proteintech, 15543-1-AP), anti-ATP6 antibody (1:500, SAB, 31464), Anti-COX1 antibody (1:500, ABclonal, A23123), anti-MT-ND5 antibody (1:500, Proteintech, 55410-1-AP), anti-β-actin antibody (SAB, 52901), and anti-GAPDH antibody (1:5000, Proteintech, 10494-1-AP).

Techniques: Cell Culture, Next-Generation Sequencing, Phospho-proteomics, CRISPR, Flow Cytometry, Two Tailed Test

Journal: bioRxiv

Article Title: EOLA1, a novel mitochondria-localized protein critical for heart functions via regulating mitochondrial translation

doi: 10.64898/2026.01.12.699056

Figure Lengend Snippet: a, Evolutionary conservation of EOLA1’s N-terminal domain. Sequence alignment across diverse species reveals key conserved residues (red). b, Fluorescence imaging analysis of EOLA1 subcellular localization after N-terminal mitochondrial targeting signal (MTS) deletion (red). Mitochondria were labeled with TFAM (green). Exogenously expressed MTS-deficient EOLA1 (delMTS-EOLA1) carried a C-terminal FLAG-HA tag.

Article Snippet: The corresponding antibodies included anti-EOLA1 antibody (1:5000, CUSABIO, CSB-PA837446LA01HU), anti-HSP60 antibody (1:3000, Proteintech, 15282-1-AP), anti-Tom20 antibody (1:1000, ABclonal, A19403), anti-α-Tubulin antibody (1:3000, Proteintech, 80762-1-RR), anti-HistoneH1.2 antibody (1:1000, Proteintech, 19649-1-AP), anti-TUFM antibody (1:1000, SAB, 34669), anti-FLAG antibody (1:1000, Sigma, F1804), anti-MRPS15 antibody (1:1000, Proteintech, 17006-1-AP), anti-MRPL11 antibody (1:1000, Proteintech, 15543-1-AP), anti-ATP6 antibody (1:500, SAB, 31464), Anti-COX1 antibody (1:500, ABclonal, A23123), anti-MT-ND5 antibody (1:500, Proteintech, 55410-1-AP), anti-β-actin antibody (SAB, 52901), and anti-GAPDH antibody (1:5000, Proteintech, 10494-1-AP).

Techniques: Sequencing, Fluorescence, Imaging, Labeling

Journal: bioRxiv

Article Title: EOLA1, a novel mitochondria-localized protein critical for heart functions via regulating mitochondrial translation

doi: 10.64898/2026.01.12.699056

Figure Lengend Snippet: a, Mitochondrial proteins predicted by TargetP 2.0 in human and mouse (left), and their overlap with MitoCarta 3.0 annotations (right). b, Fluorescence analysis of the subcellular location of human EOLA1 protein (red), and HSP60 (green) was used as a marker for mitochondria. The exogenously expressed EOLA1 was tagged with a C-terminal FLAG and HA tandem epitope. c, Western blotting analysis of EOLA1 in the subcellular fractions of PLC/PRF/5 ( Homo sapiens , left) and B16-F10 melanoma cells ( Mus musculus , right). Tubulin was used as a cytoplasmic marker, Histone H1.2 as a nuclear marker, and HSP60 as a mitochondrial marker. d, Determination of EOLA1 sub-mitochondrial localization by Proteinase K digestion assay using purified mitochondria from HEK293T cells. PK, Protease K; IMM, inner mitochondrial membrane; OMM, outer mitochondrial membrane. e, f, Seahorse analysis of WT and Eola1 KO in B16-F10 melanoma cells ( e ) and HL-1 cells ( f ). Quantification of the basal respiration, maximal respiration, and spare respiratory capacity was performed for the indicated cells. g-i, Electron microscopy images ( g ) of WT cells (left) and Eola1 knockout cells (right). Higher-magnification views are presented in panel h . The relative circularity ratio of mitochondria was quantified ( i ). Mito: Mitochondria, N: nucleus. Note: e , f , One-way ANOVA with Tukey’s test. i , two-tailed unpaired Student’s t-tests. ** P <0.01, *** P <0.001, **** P <0.0001, ns: not significant. e , f , Data were presented as mean ± SD (n=6).

Article Snippet: The corresponding antibodies included anti-EOLA1 antibody (1:5000, CUSABIO, CSB-PA837446LA01HU), anti-HSP60 antibody (1:3000, Proteintech, 15282-1-AP), anti-Tom20 antibody (1:1000, ABclonal, A19403), anti-α-Tubulin antibody (1:3000, Proteintech, 80762-1-RR), anti-HistoneH1.2 antibody (1:1000, Proteintech, 19649-1-AP), anti-TUFM antibody (1:1000, SAB, 34669), anti-FLAG antibody (1:1000, Sigma, F1804), anti-MRPS15 antibody (1:1000, Proteintech, 17006-1-AP), anti-MRPL11 antibody (1:1000, Proteintech, 15543-1-AP), anti-ATP6 antibody (1:500, SAB, 31464), Anti-COX1 antibody (1:500, ABclonal, A23123), anti-MT-ND5 antibody (1:500, Proteintech, 55410-1-AP), anti-β-actin antibody (SAB, 52901), and anti-GAPDH antibody (1:5000, Proteintech, 10494-1-AP).

Techniques: Fluorescence, Marker, Western Blot, Purification, Membrane, Electron Microscopy, Knock-Out, Two Tailed Test

Journal: bioRxiv

Article Title: EOLA1, a novel mitochondria-localized protein critical for heart functions via regulating mitochondrial translation

doi: 10.64898/2026.01.12.699056

Figure Lengend Snippet: a, Pie chart representing the proportion of mitochondrial proteins identified in the EOLA1 interactome. b, EOLA1-interacting mitochondrial RNAs were identified via UV-RIP-seq. c, Protein levels of MRPS15 (mt-SSU marker) and MRPL11 (mt-LSU marker) were analyzed by Western blotting across fractions.

Article Snippet: The corresponding antibodies included anti-EOLA1 antibody (1:5000, CUSABIO, CSB-PA837446LA01HU), anti-HSP60 antibody (1:3000, Proteintech, 15282-1-AP), anti-Tom20 antibody (1:1000, ABclonal, A19403), anti-α-Tubulin antibody (1:3000, Proteintech, 80762-1-RR), anti-HistoneH1.2 antibody (1:1000, Proteintech, 19649-1-AP), anti-TUFM antibody (1:1000, SAB, 34669), anti-FLAG antibody (1:1000, Sigma, F1804), anti-MRPS15 antibody (1:1000, Proteintech, 17006-1-AP), anti-MRPL11 antibody (1:1000, Proteintech, 15543-1-AP), anti-ATP6 antibody (1:500, SAB, 31464), Anti-COX1 antibody (1:500, ABclonal, A23123), anti-MT-ND5 antibody (1:500, Proteintech, 55410-1-AP), anti-β-actin antibody (SAB, 52901), and anti-GAPDH antibody (1:5000, Proteintech, 10494-1-AP).

Techniques: Marker, Western Blot

Journal: bioRxiv

Article Title: EOLA1, a novel mitochondria-localized protein critical for heart functions via regulating mitochondrial translation

doi: 10.64898/2026.01.12.699056

Figure Lengend Snippet: a, b, Identification of EOLA1 interacting partners. EOLA1 complex was purified from EOLA1–FH stable cells using immunoaffinity purification. Eluted proteins were separated by SDS-PAGE and analyzed by silver staining ( a ). Western blotting analysis verified the mitochondrial Tu translation elongation factor (TUFM) as an EOLA1-binding partner ( b ). c-e, RNA immunoprecipitation (RIP) followed by qPCR demonstrates specific binding between EOLA1 and 12S mt-rRNA. Exogenous RIP-qPCR with ( c ) or without ( d ) UV crosslinking confirms direct RNA-protein interactions. Endogenous RIP-qPCR further validates this physiological association ( e ). The identification primers are provided in . f, g, EOLA1 affects mitochondrial mRNA translation. Sucrose gradient fractionation profiles of mitochondrial ribosomal subunits assessed by RT-PCR of 12S rRNA (mt-SSU) and 16S rRNA (mt-LSU) ( f , top). Distribution of mitochondrial-encoded mRNAs (ATP6, ND5, and COX1) measured by RT-PCR ( f , bottom), along with their corresponding protein levels measured by Western blotting. β-actin served as a loading control ( g ). The identification primers are provided in . h, Mitochondrial translation activity was assessed using the Mito-Click-iT assay. i, Mitochondrial-encoded mRNAs (mt-mRNAs) and ribosomal RNA levels (12S and 16S mt-rRNA) were quantified in control and EOLA1-knockout cells by RT-qPCR. The identification primers are provided in . Note: c , d , e , two-tailed unpaired Student’s t-tests. i , One-way ANOVA with Tukey’s test. *** P <0.001, **** P <0.0001. c , d , e , i , Data were presented as mean ± SD (n=3).

Article Snippet: The corresponding antibodies included anti-EOLA1 antibody (1:5000, CUSABIO, CSB-PA837446LA01HU), anti-HSP60 antibody (1:3000, Proteintech, 15282-1-AP), anti-Tom20 antibody (1:1000, ABclonal, A19403), anti-α-Tubulin antibody (1:3000, Proteintech, 80762-1-RR), anti-HistoneH1.2 antibody (1:1000, Proteintech, 19649-1-AP), anti-TUFM antibody (1:1000, SAB, 34669), anti-FLAG antibody (1:1000, Sigma, F1804), anti-MRPS15 antibody (1:1000, Proteintech, 17006-1-AP), anti-MRPL11 antibody (1:1000, Proteintech, 15543-1-AP), anti-ATP6 antibody (1:500, SAB, 31464), Anti-COX1 antibody (1:500, ABclonal, A23123), anti-MT-ND5 antibody (1:500, Proteintech, 55410-1-AP), anti-β-actin antibody (SAB, 52901), and anti-GAPDH antibody (1:5000, Proteintech, 10494-1-AP).

Techniques: Purification, Immunoaffinity Purification, SDS Page, Silver Staining, Western Blot, Binding Assay, RNA Immunoprecipitation, Fractionation, Reverse Transcription Polymerase Chain Reaction, Control, Activity Assay, Knock-Out, Quantitative RT-PCR, Two Tailed Test

Journal: bioRxiv

Article Title: EOLA1, a novel mitochondria-localized protein critical for heart functions via regulating mitochondrial translation

doi: 10.64898/2026.01.12.699056

Figure Lengend Snippet: a, EOLA1 protein deficiency in knockout mice was validated by Western blotting analysis. GAPDH was used as a loading control. b, Western blotting analysis revealed significantly lower levels of mitochondrial protein in Eola1 -/- hearts compared to Eola1 +/+ . GAPDH was used as a loading control. c, Typical ventricular borders at end-diastole were identified by B-mode echocardiography. d, e, Compared to Eola1 +/+ mice, both male ( d ) and female ( e ) Eola1 -/- mice demonstrated significant enlargement in ventricular long-axis length ( i ), short-axis length ( ii ), and cross-sectional area ( iii ). f, Representative images of left ventricular motion patterns identified by M-mode echocardiography. g, Compared to Eola1 +/+ mice, male Eola1 -/- mice demonstrated a significant decrease in ejection fraction ( i ), shortening fraction ( ii ), and stroke volume ( iv ) of left ventricle. Cardiac output ( iii ) of left ventricle also showed a decreasing trend. h, Compared to Eola1 +/+ mice, female Eola1 -/- mice demonstrated a significant decrease in ejection fraction ( i ), shortening fraction ( ii ), cardiac output ( iii ) and stroke volume ( iv ) of left ventricle. i, Eola1 knockout leads to thickening of the anterior wall ( i ) and thinning of the posterior wall ( ii ) of the left ventricle in male mice. j, Eola1 deficiency causes thinning of the posterior wall ( ii ) and a trend of thickening of the anterior wall ( i ) of the left ventricle in female mice. k, l, Eola1 deficiency increases heart rate of both male ( k ) and female ( l ) mice. Note: d , e , g-l , two-tailed unpaired Student’s t-tests. * P <0.05, ** P <0.01, *** P <0.001, **** P <0.0001, ns: not significant. Data were presented as mean ± SEM.

Article Snippet: The corresponding antibodies included anti-EOLA1 antibody (1:5000, CUSABIO, CSB-PA837446LA01HU), anti-HSP60 antibody (1:3000, Proteintech, 15282-1-AP), anti-Tom20 antibody (1:1000, ABclonal, A19403), anti-α-Tubulin antibody (1:3000, Proteintech, 80762-1-RR), anti-HistoneH1.2 antibody (1:1000, Proteintech, 19649-1-AP), anti-TUFM antibody (1:1000, SAB, 34669), anti-FLAG antibody (1:1000, Sigma, F1804), anti-MRPS15 antibody (1:1000, Proteintech, 17006-1-AP), anti-MRPL11 antibody (1:1000, Proteintech, 15543-1-AP), anti-ATP6 antibody (1:500, SAB, 31464), Anti-COX1 antibody (1:500, ABclonal, A23123), anti-MT-ND5 antibody (1:500, Proteintech, 55410-1-AP), anti-β-actin antibody (SAB, 52901), and anti-GAPDH antibody (1:5000, Proteintech, 10494-1-AP).

Techniques: Knock-Out, Western Blot, Control, Two Tailed Test

Journal: bioRxiv

Article Title: EOLA1, a novel mitochondria-localized protein critical for heart functions via regulating mitochondrial translation

doi: 10.64898/2026.01.12.699056

Figure Lengend Snippet: a, b, Schematic diagram of sgRNA targeting mouse Eola1 locus ( a ) and validation of Eola1 knockout in mice by PCR ( b ). The genotyping primers are provided in . c, Representative pictures of the Eola1 +/+ and Eola1 -/- mice. d, Comparison of body weight in female (left) and male (right) Eola1 +/+ and Eola1 -/- mice. e, Relative mRNA levels of mitochondrial-encoded transcripts were quantified by RT-qPCR in Eola1 +/+ and Eola1 -/- hearts. Note: e , two-tailed unpaired Student’s t-tests. **** P <0.0001, ns: not significant. Data were presented as mean ± SD (n=6).

Article Snippet: The corresponding antibodies included anti-EOLA1 antibody (1:5000, CUSABIO, CSB-PA837446LA01HU), anti-HSP60 antibody (1:3000, Proteintech, 15282-1-AP), anti-Tom20 antibody (1:1000, ABclonal, A19403), anti-α-Tubulin antibody (1:3000, Proteintech, 80762-1-RR), anti-HistoneH1.2 antibody (1:1000, Proteintech, 19649-1-AP), anti-TUFM antibody (1:1000, SAB, 34669), anti-FLAG antibody (1:1000, Sigma, F1804), anti-MRPS15 antibody (1:1000, Proteintech, 17006-1-AP), anti-MRPL11 antibody (1:1000, Proteintech, 15543-1-AP), anti-ATP6 antibody (1:500, SAB, 31464), Anti-COX1 antibody (1:500, ABclonal, A23123), anti-MT-ND5 antibody (1:500, Proteintech, 55410-1-AP), anti-β-actin antibody (SAB, 52901), and anti-GAPDH antibody (1:5000, Proteintech, 10494-1-AP).

Techniques: Biomarker Discovery, Knock-Out, Comparison, Quantitative RT-PCR, Two Tailed Test

Journal: bioRxiv

Article Title: EOLA1, a novel mitochondria-localized protein critical for heart functions via regulating mitochondrial translation

doi: 10.64898/2026.01.12.699056

Figure Lengend Snippet: EOLA1, a mitochondrial matrix protein identified by CRISPR screening, interacts with TUFM/12S mt-rRNA to promote the protein synthesis of OXPHOS subunits. Its loss impairs mt-mRNA translation and causes heart failure in mice, revealing a mitochondrial translation-cardiac function axis pivotal for cardiovascular homeostasis.

Article Snippet: The corresponding antibodies included anti-EOLA1 antibody (1:5000, CUSABIO, CSB-PA837446LA01HU), anti-HSP60 antibody (1:3000, Proteintech, 15282-1-AP), anti-Tom20 antibody (1:1000, ABclonal, A19403), anti-α-Tubulin antibody (1:3000, Proteintech, 80762-1-RR), anti-HistoneH1.2 antibody (1:1000, Proteintech, 19649-1-AP), anti-TUFM antibody (1:1000, SAB, 34669), anti-FLAG antibody (1:1000, Sigma, F1804), anti-MRPS15 antibody (1:1000, Proteintech, 17006-1-AP), anti-MRPL11 antibody (1:1000, Proteintech, 15543-1-AP), anti-ATP6 antibody (1:500, SAB, 31464), Anti-COX1 antibody (1:500, ABclonal, A23123), anti-MT-ND5 antibody (1:500, Proteintech, 55410-1-AP), anti-β-actin antibody (SAB, 52901), and anti-GAPDH antibody (1:5000, Proteintech, 10494-1-AP).

Techniques: CRISPR

Journal: Scientific Reports

Article Title: The von Willebrand factor stamps plasmatic extracellular vesicles from glioblastoma patients

doi: 10.1038/s41598-021-02254-7

Figure Lengend Snippet: VWF is transported in circulating EVs from GBM patients. ( A ) Equal volume of protein lysates from EV fractions, obtained with SEC followed by ultracentrifugation, and their corresponding plasma, from one GBM patient and one healthy donor, were separated by SDS-PAGE and analyzed by immunoblot for VWF, FCN3, and HSP70. Blots are representative of n = 3. ( B ) mRNA expression of von Willebrand factor (VWF) and ficolin-3 (FCN3) in healthy subjects and GBM patients estimated from The Cancer Genome Atlas (TCGA, n > 500 for GBM patients). ( C ) Anomalies currently reported in VWF and FCN3 genes. ( D ) Equal volume of protein lysates from EV fractions (3 GBM and 3 Healthy) were separated by SDS-PAGE and analyzed by immunoblot for VWF, GM130 (putative intracellular membrane protein contaminant), and Apolipoprotein A1 (APOA1, plasmatic protein). Healthy donor plasma and total cell lysate from GBM cells serve as controls. Blots are representative of n > 7 individual samples. ( E ) Densitometric analysis was performed on 7 and 8 independent EV preparations from Healthy and GBM liquid biopsies, respectively. ( F ) Concentration of VWF in plasmatic EVs from healthy donors and GBM patients (n = 20). Mann–Whitney test, * p < 0.05, ** p < 0.01, *** p < 0.001. S.D. are shown in panel E and S.E.M. in panel F.

Article Snippet: EVs were separated and concentrated from 500 μl of plasma as described above and the pellet was directly lysed in boiling Laemmli for 10 min. Proteins were resolved by SDS-PAGE, transferred onto nitrocellulose membranes and blotted with the following antibodies, all diluted at 1/1000: CD9 (EXOAB-CD9A-1, SBI), CD63 (EXOAB-CD63A-1, SBI), VWF (sc-53466, Santa Cruz), FCN3 (CL7767AP, Cedarlane) , Apolipoprotein A1 (sc-376818, Santa Cruz), HSP70 (EXOAB-HSP70A, SBI), and GM130 (ab52649, Abcam) diluted at 1/1000.

Techniques: Clinical Proteomics, SDS Page, Western Blot, Expressing, Membrane, Concentration Assay, MANN-WHITNEY