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anti mouse lamp2  (Developmental Studies Hybridoma Bank)


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    Structured Review

    Developmental Studies Hybridoma Bank anti mouse lamp2
    ( A ) Confocal microscopy of endogenous BMP (yellow) and <t>LAMP2</t> (magenta) immunofluorescence in wild-type (WT) and R1441G LRRK2 MEFs. Scale bar: 20 µm. Quantification of vesicular BMP intensity ( B ) and LAMP2 relative intensity ( C ) per cell area. Colored dots represent mean value from four independent experiments, and violin plots show the distribution of individual cell data. Significance determined by two-tailed paired t -test **p < 0.01, ***p < 0.001. ( D ) Representative transmission electron microscopy (TEM) images of multivesicular endosomes (MVE) from WT and R1441G LRRK2 MEFs. MVB periphery highlighted in yellow. Scale bar: 250 nm. ( E ) MVE area (µm 2 ) quantification in WT and R1441G LRRK2 mutant cells. Colored dots represent mean values from 3 independent experiments and violin plots show the distribution of individual cell data (35–45 cells/group). ( F ) Quantification of intraluminal vesicles (ILVs) per MVE in WT and R1441G LRRK2 MEF cells. The number of ILVs per MVE is binned in three groups and plotted as a percentage of MVE from the total population of each experiment independently. Data from 3 independent experiments (mean ± SEM). Significance determined by two-tailed unpaired t -test ( E ) and ordinary two-way ANOVA, uncorrected Fisher’s LSD ( F ). *p < 0.05, ****p < 0.0001. Figure 1—source data 1. IF images in panel A. Figure 1—source data 2. TEM images in panel D. Figure 1—source data 3. Plotted values in panels B, C, E, F.
    Anti Mouse Lamp2, supplied by Developmental Studies Hybridoma Bank, used in various techniques. Bioz Stars score: 94/100, based on 206 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/lamp+2/anti-LAMP-2/pmc13046380-3-2-9
    Average 94 stars, based on 206 article reviews
    anti mouse lamp2 - by Bioz Stars, 2026-11
    94/100 stars

    Images

    1) Product Images from "Extracellular vesicle-mediated release of bis(monoacylglycerol)phosphate is regulated by LRRK2 and glucocerebrosidase activity"

    Article Title: Extracellular vesicle-mediated release of bis(monoacylglycerol)phosphate is regulated by LRRK2 and glucocerebrosidase activity

    Journal: eLife

    doi: 10.7554/eLife.106330

    ( A ) Confocal microscopy of endogenous BMP (yellow) and LAMP2 (magenta) immunofluorescence in wild-type (WT) and R1441G LRRK2 MEFs. Scale bar: 20 µm. Quantification of vesicular BMP intensity ( B ) and LAMP2 relative intensity ( C ) per cell area. Colored dots represent mean value from four independent experiments, and violin plots show the distribution of individual cell data. Significance determined by two-tailed paired t -test **p < 0.01, ***p < 0.001. ( D ) Representative transmission electron microscopy (TEM) images of multivesicular endosomes (MVE) from WT and R1441G LRRK2 MEFs. MVB periphery highlighted in yellow. Scale bar: 250 nm. ( E ) MVE area (µm 2 ) quantification in WT and R1441G LRRK2 mutant cells. Colored dots represent mean values from 3 independent experiments and violin plots show the distribution of individual cell data (35–45 cells/group). ( F ) Quantification of intraluminal vesicles (ILVs) per MVE in WT and R1441G LRRK2 MEF cells. The number of ILVs per MVE is binned in three groups and plotted as a percentage of MVE from the total population of each experiment independently. Data from 3 independent experiments (mean ± SEM). Significance determined by two-tailed unpaired t -test ( E ) and ordinary two-way ANOVA, uncorrected Fisher’s LSD ( F ). *p < 0.05, ****p < 0.0001. Figure 1—source data 1. IF images in panel A. Figure 1—source data 2. TEM images in panel D. Figure 1—source data 3. Plotted values in panels B, C, E, F.
    Figure Legend Snippet: ( A ) Confocal microscopy of endogenous BMP (yellow) and LAMP2 (magenta) immunofluorescence in wild-type (WT) and R1441G LRRK2 MEFs. Scale bar: 20 µm. Quantification of vesicular BMP intensity ( B ) and LAMP2 relative intensity ( C ) per cell area. Colored dots represent mean value from four independent experiments, and violin plots show the distribution of individual cell data. Significance determined by two-tailed paired t -test **p < 0.01, ***p < 0.001. ( D ) Representative transmission electron microscopy (TEM) images of multivesicular endosomes (MVE) from WT and R1441G LRRK2 MEFs. MVB periphery highlighted in yellow. Scale bar: 250 nm. ( E ) MVE area (µm 2 ) quantification in WT and R1441G LRRK2 mutant cells. Colored dots represent mean values from 3 independent experiments and violin plots show the distribution of individual cell data (35–45 cells/group). ( F ) Quantification of intraluminal vesicles (ILVs) per MVE in WT and R1441G LRRK2 MEF cells. The number of ILVs per MVE is binned in three groups and plotted as a percentage of MVE from the total population of each experiment independently. Data from 3 independent experiments (mean ± SEM). Significance determined by two-tailed unpaired t -test ( E ) and ordinary two-way ANOVA, uncorrected Fisher’s LSD ( F ). *p < 0.05, ****p < 0.0001. Figure 1—source data 1. IF images in panel A. Figure 1—source data 2. TEM images in panel D. Figure 1—source data 3. Plotted values in panels B, C, E, F.

    Techniques Used: Confocal Microscopy, Immunofluorescence, Two Tailed Test, Transmission Assay, Electron Microscopy, Mutagenesis

    ( A ) Whole cell lysates (WCL) from wild-type (WT) and R1441G LRRK2 mouse embryonic fibroblast (MEF) cells treated with 200 nM MLi-2 for 24 hr were analyzed by immunoblotting. Representative images of LAMP2, phospho-Rab10, and α-Tubulin levels are shown. Molecular weight marker mobility is shown in kDa. ( B ) Flow cytometry measurement of GCase activity using PFB-FDGlu fluorescent GCase substrate in WT and R1441G LRRK2 mutant MEF cells treated with 300 µM conduritol β-epoxide (CBE) for 24 hr. WCL and isolated EVs from WT and R1441G LRRK2 mutant MEF cells treated with 200 nM MLi-2 ( C ) or 300 µM CBE ( G ) for 48 hr were analyzed by immunoblotting. Representative images of LAMP2, Flotillin-1, and α-Tubulin levels are shown. Molecular weight marker mobility is shown in kDa. Immunoblots for LAMP2 and Flotillin-1 in EV fractions required longer exposure times to visualize clear signals across all conditions. Quantification of LAMP2 and Flotillin-1 levels relative to R1441G LRRK2 MEF cells in WCL ( D , H ) and isolated EVs ( E , F , I, J ). Data from 6 to 8 independent experiments (mean ± SEM). Significance determined by Kruskal–Wallis test followed by an uncorrected Dunn’s post hoc test compared to R1441G LRRK2 control *p < 0.05, **p < 0.01, ***p < 0.001; ns, not significant. Figure 2—source data 1. Uncropped blots. Figure 2—source data 2. Annotated uncropped blots. Figure 2—source data 3. Plotted values in panels D–F, H–J.
    Figure Legend Snippet: ( A ) Whole cell lysates (WCL) from wild-type (WT) and R1441G LRRK2 mouse embryonic fibroblast (MEF) cells treated with 200 nM MLi-2 for 24 hr were analyzed by immunoblotting. Representative images of LAMP2, phospho-Rab10, and α-Tubulin levels are shown. Molecular weight marker mobility is shown in kDa. ( B ) Flow cytometry measurement of GCase activity using PFB-FDGlu fluorescent GCase substrate in WT and R1441G LRRK2 mutant MEF cells treated with 300 µM conduritol β-epoxide (CBE) for 24 hr. WCL and isolated EVs from WT and R1441G LRRK2 mutant MEF cells treated with 200 nM MLi-2 ( C ) or 300 µM CBE ( G ) for 48 hr were analyzed by immunoblotting. Representative images of LAMP2, Flotillin-1, and α-Tubulin levels are shown. Molecular weight marker mobility is shown in kDa. Immunoblots for LAMP2 and Flotillin-1 in EV fractions required longer exposure times to visualize clear signals across all conditions. Quantification of LAMP2 and Flotillin-1 levels relative to R1441G LRRK2 MEF cells in WCL ( D , H ) and isolated EVs ( E , F , I, J ). Data from 6 to 8 independent experiments (mean ± SEM). Significance determined by Kruskal–Wallis test followed by an uncorrected Dunn’s post hoc test compared to R1441G LRRK2 control *p < 0.05, **p < 0.01, ***p < 0.001; ns, not significant. Figure 2—source data 1. Uncropped blots. Figure 2—source data 2. Annotated uncropped blots. Figure 2—source data 3. Plotted values in panels D–F, H–J.

    Techniques Used: Western Blot, Molecular Weight, Marker, Flow Cytometry, Activity Assay, Mutagenesis, Isolation, Control

    ( A–C ) No significant differences in EV release between MLi-2/conduritol β-epoxide (CBE)-treated and untreated wild-type (WT) MEF cells. Quantification of LAMP2 and Flotillin-1 levels relative to WT control MEF cells in whole cell lysates (WCL) ( A ) and isolated EVs ( B–C ). Data from 7 to 8 independent experiments (mean ± SEM). Significance determined by ordinary one-way ANOVA, uncorrected Fisher’s LSD. ( D–E ) Characterization of WT or R1441G LRRK2 MEF-derived purified EVs by nanoparticle tracking analysis (NTA). ( D ) Representative plots of EV size distribution in each indicated condition. ( E ) Yield comparison of MEF-derived EVs from each indicated condition determined by NTA. Each colored dot represents an independent experiment. Figure 2—figure supplement 1—source data 1. Plotted values in panels A–C, E.
    Figure Legend Snippet: ( A–C ) No significant differences in EV release between MLi-2/conduritol β-epoxide (CBE)-treated and untreated wild-type (WT) MEF cells. Quantification of LAMP2 and Flotillin-1 levels relative to WT control MEF cells in whole cell lysates (WCL) ( A ) and isolated EVs ( B–C ). Data from 7 to 8 independent experiments (mean ± SEM). Significance determined by ordinary one-way ANOVA, uncorrected Fisher’s LSD. ( D–E ) Characterization of WT or R1441G LRRK2 MEF-derived purified EVs by nanoparticle tracking analysis (NTA). ( D ) Representative plots of EV size distribution in each indicated condition. ( E ) Yield comparison of MEF-derived EVs from each indicated condition determined by NTA. Each colored dot represents an independent experiment. Figure 2—figure supplement 1—source data 1. Plotted values in panels A–C, E.

    Techniques Used: Control, Isolation, Derivative Assay, Purification, Comparison

    ( A ) Whole cell lysates (WCL) and isolated EVs from wild-type (WT) mouse embryonic fibroblast (MEF) cells treated with 10 µM GW4869 or 10 nM bafilomycin-A1 (B-A1) for 24 hr were analyzed by immunoblotting. Representative immunoblots of LAMP2, Flotillin-1, and α-Tubulin are shown. Molecular weight marker mobility is shown in kDa. Ultra-performance liquid chromatography–tandem mass spectrometry (UPLC–MS/MS) determination of EV-associated di-18:1-BMP normalized to protein content from WT MEF cells treated with 10 µM GW4869 ( B ) or 10 nM B-A1 ( C ) for 24 hr. Data shown as fold change relative to WT control MEF cells. Only BMP isoforms that were detected are shown. Data from 6 independent experiments (mean ± SEM). Significance determined by two-tailed unpaired t -test; *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. Quantitation of BMP isoforms normalized to protein content in WCL from MEF WT cells treated with 10 µM GW4869 ( D ) or 10 nM B-A1 ( E ) for 24 hr. Data shown as fold change relative to WT control MEF cells. Only BMP isoforms that were detected are shown. Data from 3 independent experiments (mean ± SEM). Significance determined by two-tailed unpaired t -test; *p < 0.05, **p < 0.01, ***p < 0.001. Figure 6—source data 1. Uncropped blots. Figure 6—source data 2. Annotated uncropped blots. Figure 6—source data 3. Plotted values in panels B–E.
    Figure Legend Snippet: ( A ) Whole cell lysates (WCL) and isolated EVs from wild-type (WT) mouse embryonic fibroblast (MEF) cells treated with 10 µM GW4869 or 10 nM bafilomycin-A1 (B-A1) for 24 hr were analyzed by immunoblotting. Representative immunoblots of LAMP2, Flotillin-1, and α-Tubulin are shown. Molecular weight marker mobility is shown in kDa. Ultra-performance liquid chromatography–tandem mass spectrometry (UPLC–MS/MS) determination of EV-associated di-18:1-BMP normalized to protein content from WT MEF cells treated with 10 µM GW4869 ( B ) or 10 nM B-A1 ( C ) for 24 hr. Data shown as fold change relative to WT control MEF cells. Only BMP isoforms that were detected are shown. Data from 6 independent experiments (mean ± SEM). Significance determined by two-tailed unpaired t -test; *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. Quantitation of BMP isoforms normalized to protein content in WCL from MEF WT cells treated with 10 µM GW4869 ( D ) or 10 nM B-A1 ( E ) for 24 hr. Data shown as fold change relative to WT control MEF cells. Only BMP isoforms that were detected are shown. Data from 3 independent experiments (mean ± SEM). Significance determined by two-tailed unpaired t -test; *p < 0.05, **p < 0.01, ***p < 0.001. Figure 6—source data 1. Uncropped blots. Figure 6—source data 2. Annotated uncropped blots. Figure 6—source data 3. Plotted values in panels B–E.

    Techniques Used: Isolation, Western Blot, Molecular Weight, Marker, Liquid Chromatography, Mass Spectrometry, Tandem Mass Spectroscopy, Control, Two Tailed Test, Quantitation Assay

    Whole cell lysates (WCL) and isolated EVs from R1441G LRRK2 MEF cells treated with 10 µM GW4869 or 10 nM bafilomycin-A1 for 24 h were analyzed by immunoblotting. Representative images of LAMP2, Flotillin-1, and α-Tubulin levels are shown. Molecular weight marker mobility is shown in kDa. Figure 6—figure supplement 1—source data 1. Uncropped blots. Figure 6—figure supplement 1—source data 2. Annotated uncropped blots.
    Figure Legend Snippet: Whole cell lysates (WCL) and isolated EVs from R1441G LRRK2 MEF cells treated with 10 µM GW4869 or 10 nM bafilomycin-A1 for 24 h were analyzed by immunoblotting. Representative images of LAMP2, Flotillin-1, and α-Tubulin levels are shown. Molecular weight marker mobility is shown in kDa. Figure 6—figure supplement 1—source data 1. Uncropped blots. Figure 6—figure supplement 1—source data 2. Annotated uncropped blots.

    Techniques Used: Isolation, Western Blot, Molecular Weight, Marker

    Related Articles

    Saline:

    Article Title: Extracellular vesicle-mediated release of bis(monoacylglycerol)phosphate is regulated by LRRK2 and glucocerebrosidase activity
    Article Snippet: 0.167 mM Oleic acid (Cambridge Isotope Laboratories; catalog no. DLM-10012-0.001) and Docosahexaenoic acid (Cambridge Isotope Laboratories; catalog no. DLM-10012-0.001) were conjugated with 0.0278 mM fatty acid-free BSA (Sigma-Aldrich; A8806) at a 1:6 molar ratio. .. Primary antibodies diluted in phosphate-buffered saline (PBS) with 1% BSA (for immunofluorescence) or 5% skim milk (for immunoblotting) were mouse anti-lysobisphosphatidic acid (anti-BMP) clone 6C4 1:1000 (EMD Millipore; catalog no. MABT837), rat monoclonal anti-mouse LAMP2 1:500/1:1000 (Developmental Studies Hybridoma Bank; catalog no. GL2A7), mouse anti-Flotillin-1 1:1000 (BD Biosciences; catalog no. 610821), rabbit anti-phospho-Rab10 1:1000 (Abcam; catalog no. ab230261), mouse anti-α-Tubulin 1:10,000 (Sigma-Aldrich; catalog no. T5168), rabbit anti-CLN5 1:000 (Abcam; catalog no. ab170899), rabbit anti-phosphoLRRK2 1:000 (Abcam; catalog no. ab133450), rabbit anti-LAMP1 XP D2D11 1:1000 (Cell Signalling; catalog no. 9091), rabbit anti-CD63 [EPR22458-280] 1:500/1:1000 (Abcam; catalog no. AB252919 ), rabbit anti-LRRK2 1:500 (Abcam; catalog no. AB133474 ), mouse anti-calnexin 1:1000 (BD Transduction; 610523), and rabbit anti-GFP 1:500 (Abcam; catalog no. AB290). ..

    Immunofluorescence:

    Article Title: Extracellular vesicle-mediated release of bis(monoacylglycerol)phosphate is regulated by LRRK2 and glucocerebrosidase activity
    Article Snippet: 0.167 mM Oleic acid (Cambridge Isotope Laboratories; catalog no. DLM-10012-0.001) and Docosahexaenoic acid (Cambridge Isotope Laboratories; catalog no. DLM-10012-0.001) were conjugated with 0.0278 mM fatty acid-free BSA (Sigma-Aldrich; A8806) at a 1:6 molar ratio. .. Primary antibodies diluted in phosphate-buffered saline (PBS) with 1% BSA (for immunofluorescence) or 5% skim milk (for immunoblotting) were mouse anti-lysobisphosphatidic acid (anti-BMP) clone 6C4 1:1000 (EMD Millipore; catalog no. MABT837), rat monoclonal anti-mouse LAMP2 1:500/1:1000 (Developmental Studies Hybridoma Bank; catalog no. GL2A7), mouse anti-Flotillin-1 1:1000 (BD Biosciences; catalog no. 610821), rabbit anti-phospho-Rab10 1:1000 (Abcam; catalog no. ab230261), mouse anti-α-Tubulin 1:10,000 (Sigma-Aldrich; catalog no. T5168), rabbit anti-CLN5 1:000 (Abcam; catalog no. ab170899), rabbit anti-phosphoLRRK2 1:000 (Abcam; catalog no. ab133450), rabbit anti-LAMP1 XP D2D11 1:1000 (Cell Signalling; catalog no. 9091), rabbit anti-CD63 [EPR22458-280] 1:500/1:1000 (Abcam; catalog no. AB252919 ), rabbit anti-LRRK2 1:500 (Abcam; catalog no. AB133474 ), mouse anti-calnexin 1:1000 (BD Transduction; 610523), and rabbit anti-GFP 1:500 (Abcam; catalog no. AB290). ..

    Western Blot:

    Article Title: Extracellular vesicle-mediated release of bis(monoacylglycerol)phosphate is regulated by LRRK2 and glucocerebrosidase activity
    Article Snippet: 0.167 mM Oleic acid (Cambridge Isotope Laboratories; catalog no. DLM-10012-0.001) and Docosahexaenoic acid (Cambridge Isotope Laboratories; catalog no. DLM-10012-0.001) were conjugated with 0.0278 mM fatty acid-free BSA (Sigma-Aldrich; A8806) at a 1:6 molar ratio. .. Primary antibodies diluted in phosphate-buffered saline (PBS) with 1% BSA (for immunofluorescence) or 5% skim milk (for immunoblotting) were mouse anti-lysobisphosphatidic acid (anti-BMP) clone 6C4 1:1000 (EMD Millipore; catalog no. MABT837), rat monoclonal anti-mouse LAMP2 1:500/1:1000 (Developmental Studies Hybridoma Bank; catalog no. GL2A7), mouse anti-Flotillin-1 1:1000 (BD Biosciences; catalog no. 610821), rabbit anti-phospho-Rab10 1:1000 (Abcam; catalog no. ab230261), mouse anti-α-Tubulin 1:10,000 (Sigma-Aldrich; catalog no. T5168), rabbit anti-CLN5 1:000 (Abcam; catalog no. ab170899), rabbit anti-phosphoLRRK2 1:000 (Abcam; catalog no. ab133450), rabbit anti-LAMP1 XP D2D11 1:1000 (Cell Signalling; catalog no. 9091), rabbit anti-CD63 [EPR22458-280] 1:500/1:1000 (Abcam; catalog no. AB252919 ), rabbit anti-LRRK2 1:500 (Abcam; catalog no. AB133474 ), mouse anti-calnexin 1:1000 (BD Transduction; 610523), and rabbit anti-GFP 1:500 (Abcam; catalog no. AB290). ..

    other:

    Article Title: Mitochondrial protein import stress causes lysosomal damage and progressive tissue atrophy.
    Article Snippet: Briefly, sections were dehydrated gradually until 70% ethanol, followed by treatment with filtered Sudan Black B (#199664, Sigma-Aldrich) for 4 min.

    Article Title: GRASP55 maintains lysosome function by controlling sorting of lysosomal enzymes at the Golgi.
    Article Snippet: The H4B4 antibody against LAMP2 was obtained from the Developmental Studies Hybridoma Bank, created by the NICHD of the NIH and maintained at The University of Iowa, Department of Biology.

    Bioprocessing:

    Article Title: Lysosomal storage, mitochondrial pathology, and autophagy in knockout of tripeptidyl peptidase 1 in human neuroblastoma cells in vitro.
    Article Snippet: Deficiency of tripeptidyl-peptidase 1 (TPP1; EC 3.4.14.9), a lysosomal enzyme encoded by the CLN2 gene, is associated with the lysosomal storage disorder classic late infantile neuronal ceroid lipofuscinosis (CLN2 disease).. The classic form of CLN2 disease leads to the accumulation of autofluorescent lysosomal storage and a massive loss of neurons with gliosis in the brain.. The major component of the storage is subunit c of mitochondrial ATP synthase, a highly hydrophobic, 75–aminoacid polypeptide.

    Recombinant:

    Article Title: Lysosomal storage, mitochondrial pathology, and autophagy in knockout of tripeptidyl peptidase 1 in human neuroblastoma cells in vitro.
    Article Snippet: Deficiency of tripeptidyl-peptidase 1 (TPP1; EC 3.4.14.9), a lysosomal enzyme encoded by the CLN2 gene, is associated with the lysosomal storage disorder classic late infantile neuronal ceroid lipofuscinosis (CLN2 disease).. The classic form of CLN2 disease leads to the accumulation of autofluorescent lysosomal storage and a massive loss of neurons with gliosis in the brain.. The major component of the storage is subunit c of mitochondrial ATP synthase, a highly hydrophobic, 75–aminoacid polypeptide.

    Purification:

    Article Title: Lysosomal storage, mitochondrial pathology, and autophagy in knockout of tripeptidyl peptidase 1 in human neuroblastoma cells in vitro.
    Article Snippet: Deficiency of tripeptidyl-peptidase 1 (TPP1; EC 3.4.14.9), a lysosomal enzyme encoded by the CLN2 gene, is associated with the lysosomal storage disorder classic late infantile neuronal ceroid lipofuscinosis (CLN2 disease).. The classic form of CLN2 disease leads to the accumulation of autofluorescent lysosomal storage and a massive loss of neurons with gliosis in the brain.. The major component of the storage is subunit c of mitochondrial ATP synthase, a highly hydrophobic, 75–aminoacid polypeptide.

    Membrane:

    Article Title: Lysosomal storage, mitochondrial pathology, and autophagy in knockout of tripeptidyl peptidase 1 in human neuroblastoma cells in vitro.
    Article Snippet: Deficiency of tripeptidyl-peptidase 1 (TPP1; EC 3.4.14.9), a lysosomal enzyme encoded by the CLN2 gene, is associated with the lysosomal storage disorder classic late infantile neuronal ceroid lipofuscinosis (CLN2 disease).. The classic form of CLN2 disease leads to the accumulation of autofluorescent lysosomal storage and a massive loss of neurons with gliosis in the brain.. The major component of the storage is subunit c of mitochondrial ATP synthase, a highly hydrophobic, 75–aminoacid polypeptide.

    Marker:

    Article Title: Lysosomal storage, mitochondrial pathology, and autophagy in knockout of tripeptidyl peptidase 1 in human neuroblastoma cells in vitro.
    Article Snippet: Deficiency of tripeptidyl-peptidase 1 (TPP1; EC 3.4.14.9), a lysosomal enzyme encoded by the CLN2 gene, is associated with the lysosomal storage disorder classic late infantile neuronal ceroid lipofuscinosis (CLN2 disease).. The classic form of CLN2 disease leads to the accumulation of autofluorescent lysosomal storage and a massive loss of neurons with gliosis in the brain.. The major component of the storage is subunit c of mitochondrial ATP synthase, a highly hydrophobic, 75–aminoacid polypeptide.



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    Developmental Studies Hybridoma Bank hybridoma product h4b4
    ATG10S promotes complete autophagic flux and inhibits pro-inflammatory cytokine genes transcription. (A, B) in S protein- or LPS-induced pro-inflammatory cell models, autophagic flux in co-cultured MDMs and BEAS-2B cells was evaluated using the tandem fluorescent sensor RFP-GFP-LC3B. Control groups were not treated with S protein, LPS, or ATG10S. A representative image from one of eight randomly selected fields (20 cells per field) is shown for each group. Scale bar: 15 μm. (C, D) in S protein- or LPS-induced pro-inflammatory zebrafish and cell models, lysates from larvae and from co-cultured MDMs and BEAS-2B cells were immunoprecipitated with an anti-LC3B antibody to assess interactions between LC3B and <t>LAMP2,</t> ATG5–ATG12, ATG7, or SQSTM1. A representative blot from five independent experiments is shown. (E, F) in S protein- or LPS-induced pro-inflammatory cell models, luciferase assays were performed to evaluate the effect of ATG10S on the transcriptional activity of pro-inflammatory cytokine gene promoters ( IFNA , IFNG , IL1B , IL6 , TNF , IL8 , and CCL2 ) in co-cultured MDMs. *** p < 0.001. Data were presented as mean ± sd ( n = 3) (e). DNA IP assays were performed to assess the binding of ATG10S to pro-inflammatory cytokine gene promoters. lysates from co-cultured MDMs were immunoprecipitated using an anti-His antibody (specific to His-tagged ATG10S), and promoter enrichment was quantified by qRT-PCR. Data are presented as mean ± sd ( n = 3) (f).
    Hybridoma Product H4b4, supplied by Developmental Studies Hybridoma Bank, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/lamp+2/anti-LAMP-2/pm41991615-201-4-3
    Average 94 stars, based on 1 article reviews
    hybridoma product h4b4 - by Bioz Stars, 2026-11
    94/100 stars
      Buy from Supplier

    94
    Developmental Studies Hybridoma Bank mabs h4b4
    ATG10S promotes complete autophagic flux and inhibits pro-inflammatory cytokine genes transcription. (A, B) in S protein- or LPS-induced pro-inflammatory cell models, autophagic flux in co-cultured MDMs and BEAS-2B cells was evaluated using the tandem fluorescent sensor RFP-GFP-LC3B. Control groups were not treated with S protein, LPS, or ATG10S. A representative image from one of eight randomly selected fields (20 cells per field) is shown for each group. Scale bar: 15 μm. (C, D) in S protein- or LPS-induced pro-inflammatory zebrafish and cell models, lysates from larvae and from co-cultured MDMs and BEAS-2B cells were immunoprecipitated with an anti-LC3B antibody to assess interactions between LC3B and <t>LAMP2,</t> ATG5–ATG12, ATG7, or SQSTM1. A representative blot from five independent experiments is shown. (E, F) in S protein- or LPS-induced pro-inflammatory cell models, luciferase assays were performed to evaluate the effect of ATG10S on the transcriptional activity of pro-inflammatory cytokine gene promoters ( IFNA , IFNG , IL1B , IL6 , TNF , IL8 , and CCL2 ) in co-cultured MDMs. *** p < 0.001. Data were presented as mean ± sd ( n = 3) (e). DNA IP assays were performed to assess the binding of ATG10S to pro-inflammatory cytokine gene promoters. lysates from co-cultured MDMs were immunoprecipitated using an anti-His antibody (specific to His-tagged ATG10S), and promoter enrichment was quantified by qRT-PCR. Data are presented as mean ± sd ( n = 3) (f).
    Mabs H4b4, supplied by Developmental Studies Hybridoma Bank, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/lamp+2/anti-LAMP-2/pm42102651-70-31-42
    Average 94 stars, based on 1 article reviews
    mabs h4b4 - by Bioz Stars, 2026-11
    94/100 stars
      Buy from Supplier

    Image Search Results


    ATG10S promotes complete autophagic flux and inhibits pro-inflammatory cytokine genes transcription. (A, B) in S protein- or LPS-induced pro-inflammatory cell models, autophagic flux in co-cultured MDMs and BEAS-2B cells was evaluated using the tandem fluorescent sensor RFP-GFP-LC3B. Control groups were not treated with S protein, LPS, or ATG10S. A representative image from one of eight randomly selected fields (20 cells per field) is shown for each group. Scale bar: 15 μm. (C, D) in S protein- or LPS-induced pro-inflammatory zebrafish and cell models, lysates from larvae and from co-cultured MDMs and BEAS-2B cells were immunoprecipitated with an anti-LC3B antibody to assess interactions between LC3B and LAMP2, ATG5–ATG12, ATG7, or SQSTM1. A representative blot from five independent experiments is shown. (E, F) in S protein- or LPS-induced pro-inflammatory cell models, luciferase assays were performed to evaluate the effect of ATG10S on the transcriptional activity of pro-inflammatory cytokine gene promoters ( IFNA , IFNG , IL1B , IL6 , TNF , IL8 , and CCL2 ) in co-cultured MDMs. *** p < 0.001. Data were presented as mean ± sd ( n = 3) (e). DNA IP assays were performed to assess the binding of ATG10S to pro-inflammatory cytokine gene promoters. lysates from co-cultured MDMs were immunoprecipitated using an anti-His antibody (specific to His-tagged ATG10S), and promoter enrichment was quantified by qRT-PCR. Data are presented as mean ± sd ( n = 3) (f).

    Journal: Autophagy

    Article Title: Dual mechanism of human ATG10S in suppressing MEF2A-Driven pro-inflammatory responses

    doi: 10.1080/15548627.2026.2676074

    Figure Lengend Snippet: ATG10S promotes complete autophagic flux and inhibits pro-inflammatory cytokine genes transcription. (A, B) in S protein- or LPS-induced pro-inflammatory cell models, autophagic flux in co-cultured MDMs and BEAS-2B cells was evaluated using the tandem fluorescent sensor RFP-GFP-LC3B. Control groups were not treated with S protein, LPS, or ATG10S. A representative image from one of eight randomly selected fields (20 cells per field) is shown for each group. Scale bar: 15 μm. (C, D) in S protein- or LPS-induced pro-inflammatory zebrafish and cell models, lysates from larvae and from co-cultured MDMs and BEAS-2B cells were immunoprecipitated with an anti-LC3B antibody to assess interactions between LC3B and LAMP2, ATG5–ATG12, ATG7, or SQSTM1. A representative blot from five independent experiments is shown. (E, F) in S protein- or LPS-induced pro-inflammatory cell models, luciferase assays were performed to evaluate the effect of ATG10S on the transcriptional activity of pro-inflammatory cytokine gene promoters ( IFNA , IFNG , IL1B , IL6 , TNF , IL8 , and CCL2 ) in co-cultured MDMs. *** p < 0.001. Data were presented as mean ± sd ( n = 3) (e). DNA IP assays were performed to assess the binding of ATG10S to pro-inflammatory cytokine gene promoters. lysates from co-cultured MDMs were immunoprecipitated using an anti-His antibody (specific to His-tagged ATG10S), and promoter enrichment was quantified by qRT-PCR. Data are presented as mean ± sd ( n = 3) (f).

    Article Snippet: Antibody against LAMP2 (sc-18822) was obtained from Santa Cruz Biotechnology.

    Techniques: Cell Culture, Control, Immunoprecipitation, Luciferase, Activity Assay, Binding Assay, Quantitative RT-PCR

    ATG10S promotes autolysosome formation to facilitate MEF2A degradation. (A) in S protein- or LPS-induced pro-inflammatory zebrafish and cell models, MDMs and zebrafish lysates were subjected to co-IP with an anti-LC3B antibody to examine the effect of ATG10S on the interaction between LC3B, LAMP2, and MEF2A. Representative blots from five independent experiments are shown. (B) in S protein- or LPS-induced pro-inflammatory cell models, immunofluorescence was performed to assess the subcellular colocalization of MEF2A and LC3B after ATG10S treatment in MDMs. Control groups were untreated with S protein, LPS, or ATG10S. A representative image from one of eight observed fields (20 cells per field) is shown for each group. Scale bar: 15 μm. (C, D) in S protein- or LPS-induced pro-inflammatory cell models, co-IP (C) using an anti-HA antibody was performed to assess the interaction between LC3B and either wild-type MEF2A or the MEF2A∆LIR mutant in MDMs. A representative blot from five independent experiments is shown. Immunofluorescence (d) with anti-HA and anti-LC3B antibodies was used to visualize subcellular colocalization between LC3B and either MEF2A or MEF2A∆LIR in MDMs. A representative image from one of eight observed fields (20 cells per field) is shown for each group. Scale bar: 15 μm. (E, F) in S protein- or LPS-induced pro-inflammatory cell models, western blotting was used to examine MEF2A protein levels in MDMs treated with 2.5 μM ATG10S, 10 μM CQ, or 10 μM MG132. A representative blot from five independent experiments is shown, and statistical analysis was performed. *** p < 0.001. Data are presented as mean ± sd ( n = 5) (e). Luciferase assays were performed to assess the effect of ATG10S on the transcriptional activity of pro-inflammatory cytokine gene promoters in MDMs treated with 10 μM CQ, which inhibits autolysosomal degradation. Data are presented as mean ± sd ( n = 3) (f).

    Journal: Autophagy

    Article Title: Dual mechanism of human ATG10S in suppressing MEF2A-Driven pro-inflammatory responses

    doi: 10.1080/15548627.2026.2676074

    Figure Lengend Snippet: ATG10S promotes autolysosome formation to facilitate MEF2A degradation. (A) in S protein- or LPS-induced pro-inflammatory zebrafish and cell models, MDMs and zebrafish lysates were subjected to co-IP with an anti-LC3B antibody to examine the effect of ATG10S on the interaction between LC3B, LAMP2, and MEF2A. Representative blots from five independent experiments are shown. (B) in S protein- or LPS-induced pro-inflammatory cell models, immunofluorescence was performed to assess the subcellular colocalization of MEF2A and LC3B after ATG10S treatment in MDMs. Control groups were untreated with S protein, LPS, or ATG10S. A representative image from one of eight observed fields (20 cells per field) is shown for each group. Scale bar: 15 μm. (C, D) in S protein- or LPS-induced pro-inflammatory cell models, co-IP (C) using an anti-HA antibody was performed to assess the interaction between LC3B and either wild-type MEF2A or the MEF2A∆LIR mutant in MDMs. A representative blot from five independent experiments is shown. Immunofluorescence (d) with anti-HA and anti-LC3B antibodies was used to visualize subcellular colocalization between LC3B and either MEF2A or MEF2A∆LIR in MDMs. A representative image from one of eight observed fields (20 cells per field) is shown for each group. Scale bar: 15 μm. (E, F) in S protein- or LPS-induced pro-inflammatory cell models, western blotting was used to examine MEF2A protein levels in MDMs treated with 2.5 μM ATG10S, 10 μM CQ, or 10 μM MG132. A representative blot from five independent experiments is shown, and statistical analysis was performed. *** p < 0.001. Data are presented as mean ± sd ( n = 5) (e). Luciferase assays were performed to assess the effect of ATG10S on the transcriptional activity of pro-inflammatory cytokine gene promoters in MDMs treated with 10 μM CQ, which inhibits autolysosomal degradation. Data are presented as mean ± sd ( n = 3) (f).

    Article Snippet: Antibody against LAMP2 (sc-18822) was obtained from Santa Cruz Biotechnology.

    Techniques: Co-Immunoprecipitation Assay, Immunofluorescence, Control, Mutagenesis, Western Blot, Analysis, Luciferase, Activity Assay

    The MEF2 domain of MEF2A mediates its direct interaction with ATG10S. (A) in S protein- or LPS-induced pro-inflammatory cell models, endogenous ATG10S was knocked down in MDMs. Co-IP with an anti-LC3B antibody was performed to assess the effect of ATG10S on the interaction between LC3B, LAMP2, and MEF2A. A representative blot from five independent experiments is shown. (B) in S protein- or LPS-induced pro-inflammatory zebrafish and cell models, co-IP was performed using an anti-His antibody to detect interactions between ATG10S (with His tag) and MEF2A, LAMP2, and LC3B in MDMs and zebrafish. A representative blot from five independent experiments is shown. (C, D) in S protein- or LPS-induced pro-inflammatory cell models, subcellular colocalization of MEF2A and ATG10S in MDMs was assessed using immunofluorescence. Cells were stained with anti-MEF2A (green) and anti-His (red) antibodies. A representative image from eight observed fields (20 cells per field) is shown for each group. Scale bars: 15 μm (C). MDMs were subjected to nucleus/cytoplasm fractionation followed by western blotting to analyze MEF2A distribution. Co-IP with an anti-His antibody was conducted to detect the interaction between ATG10S and MEF2A in nuclear and cytoplasmic fractions. A representative blot from five independent experiments is shown. HSP90 and LMNB1 were used as cytoplasmic and nuclear markers, respectively (d). (E) a representative SPR sensorgram showing the binding of ATG10S (at 133, 266, 531, 1062, and 2125 nM) to MEF2A immobilized on the chip (27 μg/mL), confirming a concentration-dependent direct interaction. (F) Schematic representation of the functional domains of full-length MEF2A and its deletion mutant (∆MEF2A). (G) in S protein-induced pro-inflammatory cell models, co-IP with an anti-His antibody was conducted to evaluate the interaction between ATG10S and either full-length MEF2A or ∆MEF2A in MDMs. (H, I) in S protein- or LPS-induced pro-inflammatory cell models, DNA IP assays were performed to assess the binding of HA-MEF2A or HA-∆MEF2A to the promoters of IFNA , IFNG , IL1B , IL6 , TNF , IL8 , and CCL2 genes, and to evaluate the effect of ATG10S on this binding. MDMs lysates were immunoprecipitated with an anti-HA antibody, and promoter sequences were detected by qRT-PCR (H). Luciferase assays were performed to evaluate the transcriptional activity of MEF2A or ∆MEF2A on pro-inflammatory gene promoters, and to determine the effect of ATG10S on this activity. *** p < 0.001, ### p < 0.001. Data are presented as mean ± sd ( n = 3) (i).

    Journal: Autophagy

    Article Title: Dual mechanism of human ATG10S in suppressing MEF2A-Driven pro-inflammatory responses

    doi: 10.1080/15548627.2026.2676074

    Figure Lengend Snippet: The MEF2 domain of MEF2A mediates its direct interaction with ATG10S. (A) in S protein- or LPS-induced pro-inflammatory cell models, endogenous ATG10S was knocked down in MDMs. Co-IP with an anti-LC3B antibody was performed to assess the effect of ATG10S on the interaction between LC3B, LAMP2, and MEF2A. A representative blot from five independent experiments is shown. (B) in S protein- or LPS-induced pro-inflammatory zebrafish and cell models, co-IP was performed using an anti-His antibody to detect interactions between ATG10S (with His tag) and MEF2A, LAMP2, and LC3B in MDMs and zebrafish. A representative blot from five independent experiments is shown. (C, D) in S protein- or LPS-induced pro-inflammatory cell models, subcellular colocalization of MEF2A and ATG10S in MDMs was assessed using immunofluorescence. Cells were stained with anti-MEF2A (green) and anti-His (red) antibodies. A representative image from eight observed fields (20 cells per field) is shown for each group. Scale bars: 15 μm (C). MDMs were subjected to nucleus/cytoplasm fractionation followed by western blotting to analyze MEF2A distribution. Co-IP with an anti-His antibody was conducted to detect the interaction between ATG10S and MEF2A in nuclear and cytoplasmic fractions. A representative blot from five independent experiments is shown. HSP90 and LMNB1 were used as cytoplasmic and nuclear markers, respectively (d). (E) a representative SPR sensorgram showing the binding of ATG10S (at 133, 266, 531, 1062, and 2125 nM) to MEF2A immobilized on the chip (27 μg/mL), confirming a concentration-dependent direct interaction. (F) Schematic representation of the functional domains of full-length MEF2A and its deletion mutant (∆MEF2A). (G) in S protein-induced pro-inflammatory cell models, co-IP with an anti-His antibody was conducted to evaluate the interaction between ATG10S and either full-length MEF2A or ∆MEF2A in MDMs. (H, I) in S protein- or LPS-induced pro-inflammatory cell models, DNA IP assays were performed to assess the binding of HA-MEF2A or HA-∆MEF2A to the promoters of IFNA , IFNG , IL1B , IL6 , TNF , IL8 , and CCL2 genes, and to evaluate the effect of ATG10S on this binding. MDMs lysates were immunoprecipitated with an anti-HA antibody, and promoter sequences were detected by qRT-PCR (H). Luciferase assays were performed to evaluate the transcriptional activity of MEF2A or ∆MEF2A on pro-inflammatory gene promoters, and to determine the effect of ATG10S on this activity. *** p < 0.001, ### p < 0.001. Data are presented as mean ± sd ( n = 3) (i).

    Article Snippet: Antibody against LAMP2 (sc-18822) was obtained from Santa Cruz Biotechnology.

    Techniques: Co-Immunoprecipitation Assay, Immunofluorescence, Staining, Fractionation, Western Blot, Sensorgram, Binding Assay, Concentration Assay, Functional Assay, Mutagenesis, Immunoprecipitation, Quantitative RT-PCR, Luciferase, Activity Assay