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mouse anti human lamp1  (Developmental Studies Hybridoma Bank)


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    Developmental Studies Hybridoma Bank mouse anti human lamp1
    (A) Schematic representation of the v-ATPase complex highlighting the subunits analyzed in this study: V 0 a1 (membrane-embedded V 0 domain) and V 1 B2 (cytosolic V 1 domain). Fluorescent proteins (FP) were fused to the C-terminus of the V 0 a1 subunit and the N-terminus of the V 1 B2 subunit. (B) Immunofluorescence microscopy of HeLa cells stably transfected with V 0 a1–eGFP or AcGFP–V 1 B2 constructs. Single-channel images are shown in grayscale, with DAPI (nuclei) shown in blue. (C) Quantification of the peripheral/perinuclear mean intensity of V 0 a1–GFP and AcGFP–V 1 B2 from experiments such as that shown in panel B (n=29-32 cells from three independent experiments). (D,F) Immunofluorescence microscopy showing co-localization of stably expressed V 0 a1–eGFP (green) (D) or AcGFP–V 1 B2 (green) (F) with endogenous <t>LAMP1</t> (magenta). Nuclei were stained with DAPI (blue). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively. (E,G) Quantification of the co-localization between LAMP1 and V 0 a1–eGFP (E) or AcGFP–V 1 B2 (G) in total, perinuclear, and peripheral regions, expressed as Pearson’s correlation coefficient (Pearson’s r), from experiments such as those shown in panels D and F ( n =22 cells from three independent experiments). (H) Live-cell images of HeLa cells showing the co-localization of transiently co-expressed V 0 a1–mScarlet3 (magenta) and AcGFP–V 1 B2 (green). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively . (I) Quantification of Pearson’s correlation coefficients between V 0 a1–mScarlet3 and AcGFP–V 1 B2 from experiments such as that shown in panel H ( n =23 cells from three independent experiments). All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Welch’s t-test for panel C, and Friedman test with Dunn’s multiple comparisons test for panels E, G, and I. Actual P values are indicated in the figure. Scale bars: 10μm.
    Mouse Anti Human Lamp1, supplied by Developmental Studies Hybridoma Bank, used in various techniques. Bioz Stars score: 96/100, based on 201 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Images

    1) Product Images from "Spatial Regulation of Lysosomal Vesicle Acidification Along the Axon via mRAVE-Dependent v-ATPase Assembly"

    Article Title: Spatial Regulation of Lysosomal Vesicle Acidification Along the Axon via mRAVE-Dependent v-ATPase Assembly

    Journal: bioRxiv

    doi: 10.64898/2025.12.22.696043

    (A) Schematic representation of the v-ATPase complex highlighting the subunits analyzed in this study: V 0 a1 (membrane-embedded V 0 domain) and V 1 B2 (cytosolic V 1 domain). Fluorescent proteins (FP) were fused to the C-terminus of the V 0 a1 subunit and the N-terminus of the V 1 B2 subunit. (B) Immunofluorescence microscopy of HeLa cells stably transfected with V 0 a1–eGFP or AcGFP–V 1 B2 constructs. Single-channel images are shown in grayscale, with DAPI (nuclei) shown in blue. (C) Quantification of the peripheral/perinuclear mean intensity of V 0 a1–GFP and AcGFP–V 1 B2 from experiments such as that shown in panel B (n=29-32 cells from three independent experiments). (D,F) Immunofluorescence microscopy showing co-localization of stably expressed V 0 a1–eGFP (green) (D) or AcGFP–V 1 B2 (green) (F) with endogenous LAMP1 (magenta). Nuclei were stained with DAPI (blue). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively. (E,G) Quantification of the co-localization between LAMP1 and V 0 a1–eGFP (E) or AcGFP–V 1 B2 (G) in total, perinuclear, and peripheral regions, expressed as Pearson’s correlation coefficient (Pearson’s r), from experiments such as those shown in panels D and F ( n =22 cells from three independent experiments). (H) Live-cell images of HeLa cells showing the co-localization of transiently co-expressed V 0 a1–mScarlet3 (magenta) and AcGFP–V 1 B2 (green). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively . (I) Quantification of Pearson’s correlation coefficients between V 0 a1–mScarlet3 and AcGFP–V 1 B2 from experiments such as that shown in panel H ( n =23 cells from three independent experiments). All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Welch’s t-test for panel C, and Friedman test with Dunn’s multiple comparisons test for panels E, G, and I. Actual P values are indicated in the figure. Scale bars: 10μm.
    Figure Legend Snippet: (A) Schematic representation of the v-ATPase complex highlighting the subunits analyzed in this study: V 0 a1 (membrane-embedded V 0 domain) and V 1 B2 (cytosolic V 1 domain). Fluorescent proteins (FP) were fused to the C-terminus of the V 0 a1 subunit and the N-terminus of the V 1 B2 subunit. (B) Immunofluorescence microscopy of HeLa cells stably transfected with V 0 a1–eGFP or AcGFP–V 1 B2 constructs. Single-channel images are shown in grayscale, with DAPI (nuclei) shown in blue. (C) Quantification of the peripheral/perinuclear mean intensity of V 0 a1–GFP and AcGFP–V 1 B2 from experiments such as that shown in panel B (n=29-32 cells from three independent experiments). (D,F) Immunofluorescence microscopy showing co-localization of stably expressed V 0 a1–eGFP (green) (D) or AcGFP–V 1 B2 (green) (F) with endogenous LAMP1 (magenta). Nuclei were stained with DAPI (blue). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively. (E,G) Quantification of the co-localization between LAMP1 and V 0 a1–eGFP (E) or AcGFP–V 1 B2 (G) in total, perinuclear, and peripheral regions, expressed as Pearson’s correlation coefficient (Pearson’s r), from experiments such as those shown in panels D and F ( n =22 cells from three independent experiments). (H) Live-cell images of HeLa cells showing the co-localization of transiently co-expressed V 0 a1–mScarlet3 (magenta) and AcGFP–V 1 B2 (green). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively . (I) Quantification of Pearson’s correlation coefficients between V 0 a1–mScarlet3 and AcGFP–V 1 B2 from experiments such as that shown in panel H ( n =23 cells from three independent experiments). All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Welch’s t-test for panel C, and Friedman test with Dunn’s multiple comparisons test for panels E, G, and I. Actual P values are indicated in the figure. Scale bars: 10μm.

    Techniques Used: Membrane, Immunofluorescence, Microscopy, Stable Transfection, Transfection, Construct, Staining

    (A,C) Immunofluorescence microscopy showing co-localization of stably expressed V 0 a1–eGFP (green) (A) or AcGFP–V 1 B2 (green) (C) with endogenous LAMP1 (magenta) in U2OS cells. Nuclei were stained with DAPI (blue). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively. (B,D) Quantification of the co-localization between LAMP1 and V 0 a1–eGFP (B) or AcGFP–V 1 B2 (D) in total, perinuclear, and peripheral regions, expressed as Pearson’s correlation coefficients (Pearson’s r), from experiments such as those shown in panels A and C ( n =23-25 cells from three independent experiments). (E) Single frame live-cell images of HeLa cells showing the co-localization of stably expressed V 0 a1–eGFP (green) with LysoTracker (magenta). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively . (F) Quantification of the co-localization between LysoTracker and V 0 a1–eGFP in total, perinuclear, and peripheral regions, expressed as Pearson’s r, from experiments such as those shown in panel E ( n =18-19 cells from two independent experiments). All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Friedman test with Dunn’s multiple comparisons test. Actual P values are indicated in the figure. Scale bars: 10 μm.
    Figure Legend Snippet: (A,C) Immunofluorescence microscopy showing co-localization of stably expressed V 0 a1–eGFP (green) (A) or AcGFP–V 1 B2 (green) (C) with endogenous LAMP1 (magenta) in U2OS cells. Nuclei were stained with DAPI (blue). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively. (B,D) Quantification of the co-localization between LAMP1 and V 0 a1–eGFP (B) or AcGFP–V 1 B2 (D) in total, perinuclear, and peripheral regions, expressed as Pearson’s correlation coefficients (Pearson’s r), from experiments such as those shown in panels A and C ( n =23-25 cells from three independent experiments). (E) Single frame live-cell images of HeLa cells showing the co-localization of stably expressed V 0 a1–eGFP (green) with LysoTracker (magenta). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively . (F) Quantification of the co-localization between LysoTracker and V 0 a1–eGFP in total, perinuclear, and peripheral regions, expressed as Pearson’s r, from experiments such as those shown in panel E ( n =18-19 cells from two independent experiments). All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Friedman test with Dunn’s multiple comparisons test. Actual P values are indicated in the figure. Scale bars: 10 μm.

    Techniques Used: Immunofluorescence, Microscopy, Stable Transfection, Staining

    (A) Schematic representation of the isolation, transfection, and processing of embryonic rat hippocampal neurons. (B) Immunofluorescence microscopy of DIV7 rat hippocampal neurons transiently transfected with a plasmid encoding V 0 a1–eGFP and immunostained for the endogenous lysosomal membrane protein LAMP1 (magenta) and axon initial segment (AIS) protein ankyrin G (AnkG) (blue). Magnified views of the boxed 30-μm axonal segments are shown at right. (C) Quantification of V 0 a1–eGFP, LAMP1, and V 0 a1–eGFP-positive LAMP1 vesicles per 30 μm axon length from experiments such as that shown in panel B ( n =18 neurons from ≥4 cultures prepared from two rats). (D) Immunofluorescence microscopy of DIV7 rat hippocampal neurons transfected with a plasmid encoding AcGFP–V 1 B2 and immunostained for endogenous LAMP1 (magenta) and ankyrin G (blue). Magnified views of the boxed 30-μm axonal segments are shown at right. (E) Quantification of AcGFP–V 1 B2, LAMP1, and AcGFP–V 1 B2-positive LAMP1 vesicles per 30 μm axon length from experiments such as that shown in panel D ( n =16 neurons from ≥4 cultures prepared from two rats). (F) Immunofluorescence microscopy of DIV7 rat hippocampal neurons co-transfected with plasmids encoding V 0 a1–eGFP and mCherry–V 1 B2. Magnified views of the boxed 30-μm axonal segments are shown at right. (G) Quantification of V 0 a1–eGFP, mCherry–V 1 B2, and mCherry–V 1 B2-positive V 0 a1–eGFP vesicles per 30 μm axon length from experiments such as that shown in panel F ( n =17 neurons from ≥4 cultures prepared from two rats). All the axonal segments analyzed correspond to the mid-axon and are located approximately 40-200 μm from the soma. All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Friedman test with Dunn’s multiple comparisons test. Actual P values are indicated in the figure. Scale bars: 20 μm.
    Figure Legend Snippet: (A) Schematic representation of the isolation, transfection, and processing of embryonic rat hippocampal neurons. (B) Immunofluorescence microscopy of DIV7 rat hippocampal neurons transiently transfected with a plasmid encoding V 0 a1–eGFP and immunostained for the endogenous lysosomal membrane protein LAMP1 (magenta) and axon initial segment (AIS) protein ankyrin G (AnkG) (blue). Magnified views of the boxed 30-μm axonal segments are shown at right. (C) Quantification of V 0 a1–eGFP, LAMP1, and V 0 a1–eGFP-positive LAMP1 vesicles per 30 μm axon length from experiments such as that shown in panel B ( n =18 neurons from ≥4 cultures prepared from two rats). (D) Immunofluorescence microscopy of DIV7 rat hippocampal neurons transfected with a plasmid encoding AcGFP–V 1 B2 and immunostained for endogenous LAMP1 (magenta) and ankyrin G (blue). Magnified views of the boxed 30-μm axonal segments are shown at right. (E) Quantification of AcGFP–V 1 B2, LAMP1, and AcGFP–V 1 B2-positive LAMP1 vesicles per 30 μm axon length from experiments such as that shown in panel D ( n =16 neurons from ≥4 cultures prepared from two rats). (F) Immunofluorescence microscopy of DIV7 rat hippocampal neurons co-transfected with plasmids encoding V 0 a1–eGFP and mCherry–V 1 B2. Magnified views of the boxed 30-μm axonal segments are shown at right. (G) Quantification of V 0 a1–eGFP, mCherry–V 1 B2, and mCherry–V 1 B2-positive V 0 a1–eGFP vesicles per 30 μm axon length from experiments such as that shown in panel F ( n =17 neurons from ≥4 cultures prepared from two rats). All the axonal segments analyzed correspond to the mid-axon and are located approximately 40-200 μm from the soma. All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Friedman test with Dunn’s multiple comparisons test. Actual P values are indicated in the figure. Scale bars: 20 μm.

    Techniques Used: Isolation, Transfection, Immunofluorescence, Microscopy, Plasmid Preparation, Membrane

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    Immunofluorescence:

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    Article Snippet: .. Anti-human LAMP1 (DSHB; #H4A3) and Anti-human EEA1 (CST; #3288) antibody was used for immunofluorescence microscopy. .. Anti-mouse I-A/I-E (or MHC-II) (clone 2G9) FITC (BD Pharmingen; #553623) antibody was used for immunofluorescence microscopy and flow cytometry.

    Microscopy:

    Article Title: GH18 family glycoside hydrolase Chitinase A of Salmonella enhances virulence by facilitating invasion and modulating host immune responses
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    Cell Signaling Technology Inc anti human 365 lamp1 rabbit monoclonal
    (A) Schematic representation of the v-ATPase complex highlighting the subunits analyzed in this study: V 0 a1 (membrane-embedded V 0 domain) and V 1 B2 (cytosolic V 1 domain). Fluorescent proteins (FP) were fused to the C-terminus of the V 0 a1 subunit and the N-terminus of the V 1 B2 subunit. (B) Immunofluorescence microscopy of HeLa cells stably transfected with V 0 a1–eGFP or AcGFP–V 1 B2 constructs. Single-channel images are shown in grayscale, with DAPI (nuclei) shown in blue. (C) Quantification of the peripheral/perinuclear mean intensity of V 0 a1–GFP and AcGFP–V 1 B2 from experiments such as that shown in panel B (n=29-32 cells from three independent experiments). (D,F) Immunofluorescence microscopy showing co-localization of stably expressed V 0 a1–eGFP (green) (D) or AcGFP–V 1 B2 (green) (F) with endogenous <t>LAMP1</t> (magenta). Nuclei were stained with DAPI (blue). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively. (E,G) Quantification of the co-localization between LAMP1 and V 0 a1–eGFP (E) or AcGFP–V 1 B2 (G) in total, perinuclear, and peripheral regions, expressed as Pearson’s correlation coefficient (Pearson’s r), from experiments such as those shown in panels D and F ( n =22 cells from three independent experiments). (H) Live-cell images of HeLa cells showing the co-localization of transiently co-expressed V 0 a1–mScarlet3 (magenta) and AcGFP–V 1 B2 (green). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively . (I) Quantification of Pearson’s correlation coefficients between V 0 a1–mScarlet3 and AcGFP–V 1 B2 from experiments such as that shown in panel H ( n =23 cells from three independent experiments). All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Welch’s t-test for panel C, and Friedman test with Dunn’s multiple comparisons test for panels E, G, and I. Actual P values are indicated in the figure. Scale bars: 10μm.
    Anti Human 365 Lamp1 Rabbit Monoclonal, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Evaluation of candidate biomarkers found in proteomic analysis of fEVs. ( a ) Heat map showing proteomic analysis quantitative values of 57 candidate biomarker proteins for CRC in fEVs selected from published articles. ( b ) Western blotting comparison of protein levels in fEVs and faecal suspensions of HC and CRC groups for candidate biomarker proteins, <t>LAMP1,</t> OLFM4, LGALS3BP, and S100A9. *The indicated band size predicted from the amino acid sequence. HC, healthy control; CRC, colorectal cancer; fEV, faecal extracellular vesicle.
    Anti Human Lamp1 Rabbit Monoclonal, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    rabbit anti human lamp1 monoclonal antibody d2d11  (Cell Signaling Technology Inc)
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    Evaluation of candidate biomarkers found in proteomic analysis of fEVs. ( a ) Heat map showing proteomic analysis quantitative values of 57 candidate biomarker proteins for CRC in fEVs selected from published articles. ( b ) Western blotting comparison of protein levels in fEVs and faecal suspensions of HC and CRC groups for candidate biomarker proteins, <t>LAMP1,</t> OLFM4, LGALS3BP, and S100A9. *The indicated band size predicted from the amino acid sequence. HC, healthy control; CRC, colorectal cancer; fEV, faecal extracellular vesicle.
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    APOE4-associated lysosomal protein changes occur in human AD brains and neurons. (A) Schematic of lysosomal proximity ligation assay, whereby proximity ligation occurs between lumenal lysosomal <t>LAMP1</t> and the profiled protein of interest (P.O.I). (B) Quantification of cellular proximity ligation assay (PLA) signal in iPSC-derived neurons across three independent differentiations and experiments. LAMP1-LAMP1 was used as a positive control, while lysosomal LGALS3BP and TMED5 localization profiled by PLA with LAMP1. Data points indicate lysosomal PLA signal within individual neurons. (C) Representative images for panel B. (D) Representative images of neuronal LGALS3BP-LAMP1 PLA in the AD brain. (E) Quantification of lysosomal LGALS3BP in the AD brain across two different cases per genotype, analyzed on a cellular level within a lysosomal mask based on PLA signal and LAMP1 immunoreactivity. (F) Representative images of neuronal TMED5-LAMP1 PLA in the AD brain. (G) Quantification of lysosomal TMED5 in the AD brain across two different cases per genotype, analyzed on a cellular level within a lysosomal mask based on PLA signal and LAMP1 immunoreactivity. (H-J) Plots showing APOE4 lysosome-associated proteins for individual patients from the BLSA cohort, showing (H) co-expression (nodes show dysregulated lysosomal proteins, edges denote highest protein co-expression), and their association with (I) APOE4 dosage and (J) AD diagnosis. (K-M) Plots showing APOE4-dysregulated lysosomal proteins for individual patients from the Banner cohort, showing (K) co-expression (nodes show dysregulated lysosomal proteins, edges denote highest protein co-expression), and their association with (L) APOE4 dosage and (M) AD diagnosis. * p < .05; **** p < .0005; * p < .0001.
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    APOE4-associated lysosomal protein changes occur in human AD brains and neurons. (A) Schematic of lysosomal proximity ligation assay, whereby proximity ligation occurs between lumenal lysosomal <t>LAMP1</t> and the profiled protein of interest (P.O.I). (B) Quantification of cellular proximity ligation assay (PLA) signal in iPSC-derived neurons across three independent differentiations and experiments. LAMP1-LAMP1 was used as a positive control, while lysosomal LGALS3BP and TMED5 localization profiled by PLA with LAMP1. Data points indicate lysosomal PLA signal within individual neurons. (C) Representative images for panel B. (D) Representative images of neuronal LGALS3BP-LAMP1 PLA in the AD brain. (E) Quantification of lysosomal LGALS3BP in the AD brain across two different cases per genotype, analyzed on a cellular level within a lysosomal mask based on PLA signal and LAMP1 immunoreactivity. (F) Representative images of neuronal TMED5-LAMP1 PLA in the AD brain. (G) Quantification of lysosomal TMED5 in the AD brain across two different cases per genotype, analyzed on a cellular level within a lysosomal mask based on PLA signal and LAMP1 immunoreactivity. (H-J) Plots showing APOE4 lysosome-associated proteins for individual patients from the BLSA cohort, showing (H) co-expression (nodes show dysregulated lysosomal proteins, edges denote highest protein co-expression), and their association with (I) APOE4 dosage and (J) AD diagnosis. (K-M) Plots showing APOE4-dysregulated lysosomal proteins for individual patients from the Banner cohort, showing (K) co-expression (nodes show dysregulated lysosomal proteins, edges denote highest protein co-expression), and their association with (L) APOE4 dosage and (M) AD diagnosis. * p < .05; **** p < .0005; * p < .0001.
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    Image Search Results


    (A) Schematic representation of the v-ATPase complex highlighting the subunits analyzed in this study: V 0 a1 (membrane-embedded V 0 domain) and V 1 B2 (cytosolic V 1 domain). Fluorescent proteins (FP) were fused to the C-terminus of the V 0 a1 subunit and the N-terminus of the V 1 B2 subunit. (B) Immunofluorescence microscopy of HeLa cells stably transfected with V 0 a1–eGFP or AcGFP–V 1 B2 constructs. Single-channel images are shown in grayscale, with DAPI (nuclei) shown in blue. (C) Quantification of the peripheral/perinuclear mean intensity of V 0 a1–GFP and AcGFP–V 1 B2 from experiments such as that shown in panel B (n=29-32 cells from three independent experiments). (D,F) Immunofluorescence microscopy showing co-localization of stably expressed V 0 a1–eGFP (green) (D) or AcGFP–V 1 B2 (green) (F) with endogenous LAMP1 (magenta). Nuclei were stained with DAPI (blue). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively. (E,G) Quantification of the co-localization between LAMP1 and V 0 a1–eGFP (E) or AcGFP–V 1 B2 (G) in total, perinuclear, and peripheral regions, expressed as Pearson’s correlation coefficient (Pearson’s r), from experiments such as those shown in panels D and F ( n =22 cells from three independent experiments). (H) Live-cell images of HeLa cells showing the co-localization of transiently co-expressed V 0 a1–mScarlet3 (magenta) and AcGFP–V 1 B2 (green). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively . (I) Quantification of Pearson’s correlation coefficients between V 0 a1–mScarlet3 and AcGFP–V 1 B2 from experiments such as that shown in panel H ( n =23 cells from three independent experiments). All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Welch’s t-test for panel C, and Friedman test with Dunn’s multiple comparisons test for panels E, G, and I. Actual P values are indicated in the figure. Scale bars: 10μm.

    Journal: bioRxiv

    Article Title: Spatial Regulation of Lysosomal Vesicle Acidification Along the Axon via mRAVE-Dependent v-ATPase Assembly

    doi: 10.64898/2025.12.22.696043

    Figure Lengend Snippet: (A) Schematic representation of the v-ATPase complex highlighting the subunits analyzed in this study: V 0 a1 (membrane-embedded V 0 domain) and V 1 B2 (cytosolic V 1 domain). Fluorescent proteins (FP) were fused to the C-terminus of the V 0 a1 subunit and the N-terminus of the V 1 B2 subunit. (B) Immunofluorescence microscopy of HeLa cells stably transfected with V 0 a1–eGFP or AcGFP–V 1 B2 constructs. Single-channel images are shown in grayscale, with DAPI (nuclei) shown in blue. (C) Quantification of the peripheral/perinuclear mean intensity of V 0 a1–GFP and AcGFP–V 1 B2 from experiments such as that shown in panel B (n=29-32 cells from three independent experiments). (D,F) Immunofluorescence microscopy showing co-localization of stably expressed V 0 a1–eGFP (green) (D) or AcGFP–V 1 B2 (green) (F) with endogenous LAMP1 (magenta). Nuclei were stained with DAPI (blue). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively. (E,G) Quantification of the co-localization between LAMP1 and V 0 a1–eGFP (E) or AcGFP–V 1 B2 (G) in total, perinuclear, and peripheral regions, expressed as Pearson’s correlation coefficient (Pearson’s r), from experiments such as those shown in panels D and F ( n =22 cells from three independent experiments). (H) Live-cell images of HeLa cells showing the co-localization of transiently co-expressed V 0 a1–mScarlet3 (magenta) and AcGFP–V 1 B2 (green). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively . (I) Quantification of Pearson’s correlation coefficients between V 0 a1–mScarlet3 and AcGFP–V 1 B2 from experiments such as that shown in panel H ( n =23 cells from three independent experiments). All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Welch’s t-test for panel C, and Friedman test with Dunn’s multiple comparisons test for panels E, G, and I. Actual P values are indicated in the figure. Scale bars: 10μm.

    Article Snippet: Primary antibodies: mouse anti-DMXL2 (Proteintech, Cat. 66891-2-Ig, 1:1,000 for IB), rabbit anti-ATP6V0A1 (Novus Biologicals, Cat. NBP1-89342, 1:1,000 for IB), rabbit anti-ATP6V1B2 (Abcam, Cat. ab73404, 1:1,000 for IB), mouse anti-human LAMP1 (DSHB, Cat. H4A3, 1:1,000 for IF), mouse anti-rat LAMP1 (6H2, generated in-house, 1:1 culture supernatant for IF), chicken anti-GFP (Invitrogen, Cat. A10262, 1:1,000 for IF), rat anti-mCherry (Invitrogen, Cat. M11217, 1:500 for IF), goat anti-ankyrin G (Santa Cruz Biotechnology, Cat. sc-31778, 1:100 for IF), rabbit anti-LC3 (Cell Signaling, Cat. 3868, 1:200 for IF) and anti-pan-neurofascin (extracellular) antibody (A12/18) (Antibodies Inc, Cat. 74-172) labeled with the mix-n-Stain Neurofascin CF647 Antibody Labeling Kit (Biotium, Cat. 92238), according to the manufacturer’s protocol (to label the axon initial segment for live-cell imaging).

    Techniques: Membrane, Immunofluorescence, Microscopy, Stable Transfection, Transfection, Construct, Staining

    (A,C) Immunofluorescence microscopy showing co-localization of stably expressed V 0 a1–eGFP (green) (A) or AcGFP–V 1 B2 (green) (C) with endogenous LAMP1 (magenta) in U2OS cells. Nuclei were stained with DAPI (blue). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively. (B,D) Quantification of the co-localization between LAMP1 and V 0 a1–eGFP (B) or AcGFP–V 1 B2 (D) in total, perinuclear, and peripheral regions, expressed as Pearson’s correlation coefficients (Pearson’s r), from experiments such as those shown in panels A and C ( n =23-25 cells from three independent experiments). (E) Single frame live-cell images of HeLa cells showing the co-localization of stably expressed V 0 a1–eGFP (green) with LysoTracker (magenta). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively . (F) Quantification of the co-localization between LysoTracker and V 0 a1–eGFP in total, perinuclear, and peripheral regions, expressed as Pearson’s r, from experiments such as those shown in panel E ( n =18-19 cells from two independent experiments). All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Friedman test with Dunn’s multiple comparisons test. Actual P values are indicated in the figure. Scale bars: 10 μm.

    Journal: bioRxiv

    Article Title: Spatial Regulation of Lysosomal Vesicle Acidification Along the Axon via mRAVE-Dependent v-ATPase Assembly

    doi: 10.64898/2025.12.22.696043

    Figure Lengend Snippet: (A,C) Immunofluorescence microscopy showing co-localization of stably expressed V 0 a1–eGFP (green) (A) or AcGFP–V 1 B2 (green) (C) with endogenous LAMP1 (magenta) in U2OS cells. Nuclei were stained with DAPI (blue). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively. (B,D) Quantification of the co-localization between LAMP1 and V 0 a1–eGFP (B) or AcGFP–V 1 B2 (D) in total, perinuclear, and peripheral regions, expressed as Pearson’s correlation coefficients (Pearson’s r), from experiments such as those shown in panels A and C ( n =23-25 cells from three independent experiments). (E) Single frame live-cell images of HeLa cells showing the co-localization of stably expressed V 0 a1–eGFP (green) with LysoTracker (magenta). Magnified views of the boxed areas in the peripheral and perinuclear regions are shown at left and right, respectively . (F) Quantification of the co-localization between LysoTracker and V 0 a1–eGFP in total, perinuclear, and peripheral regions, expressed as Pearson’s r, from experiments such as those shown in panel E ( n =18-19 cells from two independent experiments). All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Friedman test with Dunn’s multiple comparisons test. Actual P values are indicated in the figure. Scale bars: 10 μm.

    Article Snippet: Primary antibodies: mouse anti-DMXL2 (Proteintech, Cat. 66891-2-Ig, 1:1,000 for IB), rabbit anti-ATP6V0A1 (Novus Biologicals, Cat. NBP1-89342, 1:1,000 for IB), rabbit anti-ATP6V1B2 (Abcam, Cat. ab73404, 1:1,000 for IB), mouse anti-human LAMP1 (DSHB, Cat. H4A3, 1:1,000 for IF), mouse anti-rat LAMP1 (6H2, generated in-house, 1:1 culture supernatant for IF), chicken anti-GFP (Invitrogen, Cat. A10262, 1:1,000 for IF), rat anti-mCherry (Invitrogen, Cat. M11217, 1:500 for IF), goat anti-ankyrin G (Santa Cruz Biotechnology, Cat. sc-31778, 1:100 for IF), rabbit anti-LC3 (Cell Signaling, Cat. 3868, 1:200 for IF) and anti-pan-neurofascin (extracellular) antibody (A12/18) (Antibodies Inc, Cat. 74-172) labeled with the mix-n-Stain Neurofascin CF647 Antibody Labeling Kit (Biotium, Cat. 92238), according to the manufacturer’s protocol (to label the axon initial segment for live-cell imaging).

    Techniques: Immunofluorescence, Microscopy, Stable Transfection, Staining

    (A) Schematic representation of the isolation, transfection, and processing of embryonic rat hippocampal neurons. (B) Immunofluorescence microscopy of DIV7 rat hippocampal neurons transiently transfected with a plasmid encoding V 0 a1–eGFP and immunostained for the endogenous lysosomal membrane protein LAMP1 (magenta) and axon initial segment (AIS) protein ankyrin G (AnkG) (blue). Magnified views of the boxed 30-μm axonal segments are shown at right. (C) Quantification of V 0 a1–eGFP, LAMP1, and V 0 a1–eGFP-positive LAMP1 vesicles per 30 μm axon length from experiments such as that shown in panel B ( n =18 neurons from ≥4 cultures prepared from two rats). (D) Immunofluorescence microscopy of DIV7 rat hippocampal neurons transfected with a plasmid encoding AcGFP–V 1 B2 and immunostained for endogenous LAMP1 (magenta) and ankyrin G (blue). Magnified views of the boxed 30-μm axonal segments are shown at right. (E) Quantification of AcGFP–V 1 B2, LAMP1, and AcGFP–V 1 B2-positive LAMP1 vesicles per 30 μm axon length from experiments such as that shown in panel D ( n =16 neurons from ≥4 cultures prepared from two rats). (F) Immunofluorescence microscopy of DIV7 rat hippocampal neurons co-transfected with plasmids encoding V 0 a1–eGFP and mCherry–V 1 B2. Magnified views of the boxed 30-μm axonal segments are shown at right. (G) Quantification of V 0 a1–eGFP, mCherry–V 1 B2, and mCherry–V 1 B2-positive V 0 a1–eGFP vesicles per 30 μm axon length from experiments such as that shown in panel F ( n =17 neurons from ≥4 cultures prepared from two rats). All the axonal segments analyzed correspond to the mid-axon and are located approximately 40-200 μm from the soma. All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Friedman test with Dunn’s multiple comparisons test. Actual P values are indicated in the figure. Scale bars: 20 μm.

    Journal: bioRxiv

    Article Title: Spatial Regulation of Lysosomal Vesicle Acidification Along the Axon via mRAVE-Dependent v-ATPase Assembly

    doi: 10.64898/2025.12.22.696043

    Figure Lengend Snippet: (A) Schematic representation of the isolation, transfection, and processing of embryonic rat hippocampal neurons. (B) Immunofluorescence microscopy of DIV7 rat hippocampal neurons transiently transfected with a plasmid encoding V 0 a1–eGFP and immunostained for the endogenous lysosomal membrane protein LAMP1 (magenta) and axon initial segment (AIS) protein ankyrin G (AnkG) (blue). Magnified views of the boxed 30-μm axonal segments are shown at right. (C) Quantification of V 0 a1–eGFP, LAMP1, and V 0 a1–eGFP-positive LAMP1 vesicles per 30 μm axon length from experiments such as that shown in panel B ( n =18 neurons from ≥4 cultures prepared from two rats). (D) Immunofluorescence microscopy of DIV7 rat hippocampal neurons transfected with a plasmid encoding AcGFP–V 1 B2 and immunostained for endogenous LAMP1 (magenta) and ankyrin G (blue). Magnified views of the boxed 30-μm axonal segments are shown at right. (E) Quantification of AcGFP–V 1 B2, LAMP1, and AcGFP–V 1 B2-positive LAMP1 vesicles per 30 μm axon length from experiments such as that shown in panel D ( n =16 neurons from ≥4 cultures prepared from two rats). (F) Immunofluorescence microscopy of DIV7 rat hippocampal neurons co-transfected with plasmids encoding V 0 a1–eGFP and mCherry–V 1 B2. Magnified views of the boxed 30-μm axonal segments are shown at right. (G) Quantification of V 0 a1–eGFP, mCherry–V 1 B2, and mCherry–V 1 B2-positive V 0 a1–eGFP vesicles per 30 μm axon length from experiments such as that shown in panel F ( n =17 neurons from ≥4 cultures prepared from two rats). All the axonal segments analyzed correspond to the mid-axon and are located approximately 40-200 μm from the soma. All quantitative data are represented as the mean ± SD. Statistical significance was assessed using the Friedman test with Dunn’s multiple comparisons test. Actual P values are indicated in the figure. Scale bars: 20 μm.

    Article Snippet: Primary antibodies: mouse anti-DMXL2 (Proteintech, Cat. 66891-2-Ig, 1:1,000 for IB), rabbit anti-ATP6V0A1 (Novus Biologicals, Cat. NBP1-89342, 1:1,000 for IB), rabbit anti-ATP6V1B2 (Abcam, Cat. ab73404, 1:1,000 for IB), mouse anti-human LAMP1 (DSHB, Cat. H4A3, 1:1,000 for IF), mouse anti-rat LAMP1 (6H2, generated in-house, 1:1 culture supernatant for IF), chicken anti-GFP (Invitrogen, Cat. A10262, 1:1,000 for IF), rat anti-mCherry (Invitrogen, Cat. M11217, 1:500 for IF), goat anti-ankyrin G (Santa Cruz Biotechnology, Cat. sc-31778, 1:100 for IF), rabbit anti-LC3 (Cell Signaling, Cat. 3868, 1:200 for IF) and anti-pan-neurofascin (extracellular) antibody (A12/18) (Antibodies Inc, Cat. 74-172) labeled with the mix-n-Stain Neurofascin CF647 Antibody Labeling Kit (Biotium, Cat. 92238), according to the manufacturer’s protocol (to label the axon initial segment for live-cell imaging).

    Techniques: Isolation, Transfection, Immunofluorescence, Microscopy, Plasmid Preparation, Membrane

    Evaluation of candidate biomarkers found in proteomic analysis of fEVs. ( a ) Heat map showing proteomic analysis quantitative values of 57 candidate biomarker proteins for CRC in fEVs selected from published articles. ( b ) Western blotting comparison of protein levels in fEVs and faecal suspensions of HC and CRC groups for candidate biomarker proteins, LAMP1, OLFM4, LGALS3BP, and S100A9. *The indicated band size predicted from the amino acid sequence. HC, healthy control; CRC, colorectal cancer; fEV, faecal extracellular vesicle.

    Journal: Scientific Reports

    Article Title: Proteomic analysis revealed the potential usefulness of faecal extracellular vesicles in colorectal cancer diagnosis

    doi: 10.1038/s41598-026-35255-5

    Figure Lengend Snippet: Evaluation of candidate biomarkers found in proteomic analysis of fEVs. ( a ) Heat map showing proteomic analysis quantitative values of 57 candidate biomarker proteins for CRC in fEVs selected from published articles. ( b ) Western blotting comparison of protein levels in fEVs and faecal suspensions of HC and CRC groups for candidate biomarker proteins, LAMP1, OLFM4, LGALS3BP, and S100A9. *The indicated band size predicted from the amino acid sequence. HC, healthy control; CRC, colorectal cancer; fEV, faecal extracellular vesicle.

    Article Snippet: Protein-transferred membranes were blocked with PVDF Blocking Reagent for Can Get Signal (TOYOBO, Osaka, Japan) and then reacted with one of the following primary antibodies: anti-human Alix Rabbit polyclonal (Proteintech, Rosemont, IL, USA), anti-human CD63 Rabbit polyclonal (Proteintech), anti-human CD9 Rabbit polyclonal (Proteintech), anti-human LAMP1 Rabbit monoclonal (Cell Signalling Technology, Danvers, MA, USA), anti-human OLFM4 Rabbit monoclonal (Cell Signalling Technology), anti-human LGALS3BP Rabbit polyclonal (Proteintech), anti-human S100A9 Rabbit monoclonal (Cell Signalling Technology) antibody.

    Techniques: Biomarker Discovery, Western Blot, Comparison, Sequencing, Control

    Validation of candidate biomarker proteins using different HC groups. ( a ) Measurement of extracellular vesicle levels in faecal suspensions from eight HCs, different from the samples used for proteomic analysis, and three faeces samples from patients with CRC, same as samples used for proteome analysis, using a sandwich assay system with a monoclonal antibody against CD63. ( b ) Comparison of the levels of candidate biomarker proteins, LAMP1, OLFM4, LGALS3BP, and S100A9, in fEVs from HC and CRC groups using western blotting. *The indicated band size predicted from the amino acid sequence. ( c ) Western blot band intensity in ( b ) was quantified and represented in box-and-whisker plots. HC, healthy control; CRC, colorectal cancer; fEV, faecal extracellular vesicle.

    Journal: Scientific Reports

    Article Title: Proteomic analysis revealed the potential usefulness of faecal extracellular vesicles in colorectal cancer diagnosis

    doi: 10.1038/s41598-026-35255-5

    Figure Lengend Snippet: Validation of candidate biomarker proteins using different HC groups. ( a ) Measurement of extracellular vesicle levels in faecal suspensions from eight HCs, different from the samples used for proteomic analysis, and three faeces samples from patients with CRC, same as samples used for proteome analysis, using a sandwich assay system with a monoclonal antibody against CD63. ( b ) Comparison of the levels of candidate biomarker proteins, LAMP1, OLFM4, LGALS3BP, and S100A9, in fEVs from HC and CRC groups using western blotting. *The indicated band size predicted from the amino acid sequence. ( c ) Western blot band intensity in ( b ) was quantified and represented in box-and-whisker plots. HC, healthy control; CRC, colorectal cancer; fEV, faecal extracellular vesicle.

    Article Snippet: Protein-transferred membranes were blocked with PVDF Blocking Reagent for Can Get Signal (TOYOBO, Osaka, Japan) and then reacted with one of the following primary antibodies: anti-human Alix Rabbit polyclonal (Proteintech, Rosemont, IL, USA), anti-human CD63 Rabbit polyclonal (Proteintech), anti-human CD9 Rabbit polyclonal (Proteintech), anti-human LAMP1 Rabbit monoclonal (Cell Signalling Technology, Danvers, MA, USA), anti-human OLFM4 Rabbit monoclonal (Cell Signalling Technology), anti-human LGALS3BP Rabbit polyclonal (Proteintech), anti-human S100A9 Rabbit monoclonal (Cell Signalling Technology) antibody.

    Techniques: Biomarker Discovery, Comparison, Western Blot, Sequencing, Whisker Assay, Control

    APOE4-associated lysosomal protein changes occur in human AD brains and neurons. (A) Schematic of lysosomal proximity ligation assay, whereby proximity ligation occurs between lumenal lysosomal LAMP1 and the profiled protein of interest (P.O.I). (B) Quantification of cellular proximity ligation assay (PLA) signal in iPSC-derived neurons across three independent differentiations and experiments. LAMP1-LAMP1 was used as a positive control, while lysosomal LGALS3BP and TMED5 localization profiled by PLA with LAMP1. Data points indicate lysosomal PLA signal within individual neurons. (C) Representative images for panel B. (D) Representative images of neuronal LGALS3BP-LAMP1 PLA in the AD brain. (E) Quantification of lysosomal LGALS3BP in the AD brain across two different cases per genotype, analyzed on a cellular level within a lysosomal mask based on PLA signal and LAMP1 immunoreactivity. (F) Representative images of neuronal TMED5-LAMP1 PLA in the AD brain. (G) Quantification of lysosomal TMED5 in the AD brain across two different cases per genotype, analyzed on a cellular level within a lysosomal mask based on PLA signal and LAMP1 immunoreactivity. (H-J) Plots showing APOE4 lysosome-associated proteins for individual patients from the BLSA cohort, showing (H) co-expression (nodes show dysregulated lysosomal proteins, edges denote highest protein co-expression), and their association with (I) APOE4 dosage and (J) AD diagnosis. (K-M) Plots showing APOE4-dysregulated lysosomal proteins for individual patients from the Banner cohort, showing (K) co-expression (nodes show dysregulated lysosomal proteins, edges denote highest protein co-expression), and their association with (L) APOE4 dosage and (M) AD diagnosis. * p < .05; **** p < .0005; * p < .0001.

    Journal: Autophagy

    Article Title: Lysosomal proteomics reveals mechanisms of neuronal APOE4-associated lysosomal dysfunction

    doi: 10.1080/15548627.2025.2576613

    Figure Lengend Snippet: APOE4-associated lysosomal protein changes occur in human AD brains and neurons. (A) Schematic of lysosomal proximity ligation assay, whereby proximity ligation occurs between lumenal lysosomal LAMP1 and the profiled protein of interest (P.O.I). (B) Quantification of cellular proximity ligation assay (PLA) signal in iPSC-derived neurons across three independent differentiations and experiments. LAMP1-LAMP1 was used as a positive control, while lysosomal LGALS3BP and TMED5 localization profiled by PLA with LAMP1. Data points indicate lysosomal PLA signal within individual neurons. (C) Representative images for panel B. (D) Representative images of neuronal LGALS3BP-LAMP1 PLA in the AD brain. (E) Quantification of lysosomal LGALS3BP in the AD brain across two different cases per genotype, analyzed on a cellular level within a lysosomal mask based on PLA signal and LAMP1 immunoreactivity. (F) Representative images of neuronal TMED5-LAMP1 PLA in the AD brain. (G) Quantification of lysosomal TMED5 in the AD brain across two different cases per genotype, analyzed on a cellular level within a lysosomal mask based on PLA signal and LAMP1 immunoreactivity. (H-J) Plots showing APOE4 lysosome-associated proteins for individual patients from the BLSA cohort, showing (H) co-expression (nodes show dysregulated lysosomal proteins, edges denote highest protein co-expression), and their association with (I) APOE4 dosage and (J) AD diagnosis. (K-M) Plots showing APOE4-dysregulated lysosomal proteins for individual patients from the Banner cohort, showing (K) co-expression (nodes show dysregulated lysosomal proteins, edges denote highest protein co-expression), and their association with (L) APOE4 dosage and (M) AD diagnosis. * p < .05; **** p < .0005; * p < .0001.

    Article Snippet: The cells were stained with mouse anti-HA antibodies (BioLegend, 901501) diluted 1:1000, rat anti-mouse LAMP1 antibodies (Santa Cruz Biotechnology, sc-19992) diluted 1:100, or mouse anti-human LAMP1 antibodies (Santa Cruz Biotechnology, sc-20011) diluted 1:800 in BB-S overnight at 4°C, washed three times with PBS, and stained with either anti-mouse Alexa Fluor 488 (Thermo Fisher Scientific, A11001)-, anti-rabbit Alexa Fluor 488 (Thermo Fisher Scientific, A21206)-, anti-mouse Alexa Fluor 555 (Thermo Fisher Scientific, A31570 )-, anti-rabbit Alexa Fluor 555 (Thermo Fisher Scientific, A21428)-, or anti-rat fluorescein (Vector Laboratories, FI-4000)-conjugated secondary antibodies diluted 1:500 in BB-S for 2 h at room temperature.

    Techniques: Proximity Ligation Assay, Ligation, Derivative Assay, Positive Control, Expressing, Biomarker Discovery