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Santa Cruz Biotechnology antibody against lamp2

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).

Antibody Against Lamp2, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 96/100, based on 969 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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1) Product Images from "Dual mechanism of human ATG10S in suppressing MEF2A-Driven pro-inflammatory responses"

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

Journal: Autophagy

doi: 10.1080/15548627.2026.2676074

Figure Legend 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).

Techniques Used: 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).

Figure Legend 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).

Techniques Used: 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).$
Figure Legend 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).

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

Ubiquitin Proteomics:

Article Title: FBXO2-mediated KPTN ubiquitination promotes amino acid-dependent mTORC1 signaling and tumor growth.
Article Snippet: Antibodies against mTOR (2983S), NPRL2 (37344S), and pS6K1-Thr389 375 (9234L) were purchased from Cell Signaling Technology. .. Antibodies against 376 ubiquitin (sc-8017), LAMP2 (sc-18822), and S6K1 (sc-8418) were purchased from 377 Santa Cruz Biotechnology. .. Antibodies against KPTN (16094-1-AP), FBXO2 378 (14590-1-AP), and Flag (20543-1-AP, for immunofluorescence assays) were 379 purchased from Proteintech.

other:

Article Title: The lysosomal LAMTOR-Rag complex functions as a checkpoint for antiviral interferon production
Article Snippet: LAMP2 (IF 1:400) , Santa Cruz Biotechnology , sc-18822.

Image Search Results

Targeting and delivery capabilities of the nanocarrier Pt@WM-PASP. (a) Bone affinity of Pt@WM-FA/R, Pt@WM-PASP, and H 2 O 2 -treated Pt@WM-PASP evaluated by (i) digital imaging, confocal laser scanning microscopy (CLSM), and SEM, and (ii) quantification of fluorescence intensity. MFI: mean fluorescence intensity; (b) ROS-responsive thioketal (TK) cleavage in Pt@WM-PASP evaluated by the ninhydrin reaction; (c) Uptake of Pt@WM-MAL, Pt@WM-PASP, and H 2 O 2 -treated Pt@WM-PASP by M1-polarized RAW264.7 macrophages, assessed by CLSM. NP: nanoparticle; (d) Uptake of Pt@WM-MAL, Pt@WM-PASP, and H 2 O 2 -treated Pt@WM-PASP by M1-polarized RAW264.7 macrophages, assessed by (i) flow cytometry and (ii) corresponding quantification. * P < 0.05 versus Pt@WM-MAL and # P < 0.05 versus Pt@WM-PASP; (e) Intracellular ROS-scavenging ability of Pt@WM-PASP and WM-PASP evaluated using the 2′,7′-dichlorofluorescein (DCF) probe, shown as (i) representative flow cytometry histograms and (ii) corresponding quantification; (f) Endosomal escape ability of siP@WM evaluated by (i) CLSM and (ii) corresponding quantification using Manders' coefficient. BF: bright field. Data are presented as mean ± SD (n = 3 independent experiments). Statistical significance was determined by two-tailed unpaired Student's t -test or one-way ANOVA followed by Tukey's multiple-comparisons test. * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001; ns, not significant.

Journal: Bioactive Materials

Article Title: Osteoporosis treatment via programmed delivery of IRF5 siRNA to macrophages in bone tissue combined with ROS scavenging

doi: 10.1016/j.bioactmat.2026.10.015

Figure Lengend Snippet: Targeting and delivery capabilities of the nanocarrier Pt@WM-PASP. (a) Bone affinity of Pt@WM-FA/R, Pt@WM-PASP, and H 2 O 2 -treated Pt@WM-PASP evaluated by (i) digital imaging, confocal laser scanning microscopy (CLSM), and SEM, and (ii) quantification of fluorescence intensity. MFI: mean fluorescence intensity; (b) ROS-responsive thioketal (TK) cleavage in Pt@WM-PASP evaluated by the ninhydrin reaction; (c) Uptake of Pt@WM-MAL, Pt@WM-PASP, and H 2 O 2 -treated Pt@WM-PASP by M1-polarized RAW264.7 macrophages, assessed by CLSM. NP: nanoparticle; (d) Uptake of Pt@WM-MAL, Pt@WM-PASP, and H 2 O 2 -treated Pt@WM-PASP by M1-polarized RAW264.7 macrophages, assessed by (i) flow cytometry and (ii) corresponding quantification. * P < 0.05 versus Pt@WM-MAL and # P < 0.05 versus Pt@WM-PASP; (e) Intracellular ROS-scavenging ability of Pt@WM-PASP and WM-PASP evaluated using the 2′,7′-dichlorofluorescein (DCF) probe, shown as (i) representative flow cytometry histograms and (ii) corresponding quantification; (f) Endosomal escape ability of siP@WM evaluated by (i) CLSM and (ii) corresponding quantification using Manders' coefficient. BF: bright field. Data are presented as mean ± SD (n = 3 independent experiments). Statistical significance was determined by two-tailed unpaired Student's t -test or one-way ANOVA followed by Tukey's multiple-comparisons test. * P < 0.05, ** P < 0.01, *** P < 0.001, and **** P < 0.0001; ns, not significant.

Article Snippet: Lysosomes were stained with anti-lysosomal-associated membrane protein 2 primary antibody (LAMP2, Proteintech) at 4 °C overnight, followed by incubation with secondary antibody at room temperature for 1 h. Coverslips were mounted with Fluoroshield with DAPI (Sigma) and observed using CLSM.

Techniques: Imaging, Confocal, Laser-Scanning Microscopy, Fluorescence, Flow Cytometry, Two Tailed Test, Confocal Laser Scanning Microscopy

Astrocytes showed activated phagocytic ability in LC following acute TBI. (A and D) The location of LC in control group and TBI group. The irregular dashed line outlining the range of DBH represents the LC. Scale bar: 100 μm. (B and C) Co-labeling of astrocytes and Lamp2 in LC of control group. Co-labeling of GFAP and Lamp2 in LC of control group were shown by the head of white arrows in (C), with the inset in the upper right corner showing an enlarged view of the indicated area. (E and F) Co-labeling of astrocytes and Lamp2 in LC of TBI group. Co-labeling of GFAP and Lamp2 in LC of TBI group were shown by the head of white arrows in (F), with the inset in the upper right corner showing an enlarged view of the indicated area. (B and E) Scale bar: 100 μm. (C and F)Scale bar: 20 μm. (G) Co-labeling of Lamp2 and GFAP in LC is enhanced following TBI, which indicates an increased phagocytic capacity of astrocytes. (each group, n = 5). t-tests employed for (G). (Contol group vs. TBI group, *** p < 0.001). IV:Fourth ventricle.

Journal: Annals of Medicine

Article Title: MERTK-related engulfment of norepinephrinergic neuronal presynaptic membrane by astrocytes following acute TBI and potentiation effect of peripheral nerve modulation

doi: 10.1080/07853890.2026.2735720

Figure Lengend Snippet: Astrocytes showed activated phagocytic ability in LC following acute TBI. (A and D) The location of LC in control group and TBI group. The irregular dashed line outlining the range of DBH represents the LC. Scale bar: 100 μm. (B and C) Co-labeling of astrocytes and Lamp2 in LC of control group. Co-labeling of GFAP and Lamp2 in LC of control group were shown by the head of white arrows in (C), with the inset in the upper right corner showing an enlarged view of the indicated area. (E and F) Co-labeling of astrocytes and Lamp2 in LC of TBI group. Co-labeling of GFAP and Lamp2 in LC of TBI group were shown by the head of white arrows in (F), with the inset in the upper right corner showing an enlarged view of the indicated area. (B and E) Scale bar: 100 μm. (C and F)Scale bar: 20 μm. (G) Co-labeling of Lamp2 and GFAP in LC is enhanced following TBI, which indicates an increased phagocytic capacity of astrocytes. (each group, n = 5). t-tests employed for (G). (Contol group vs. TBI group, *** p < 0.001). IV:Fourth ventricle.

Article Snippet: The primary antibodies used in this study were: Rabbit anti-Dopamine beta Hydroxylase (DBH) (ab209487, 1:500, Abcam), Rabbit anti-cFos (2250 T, 1:1000, Cell signaling Technology), Rabbit anti-Caspase-3 p12 (A5357, 1:500, Selleck), Mouse anti-Glial Fibrillary Acidic Protein (GFAP) (ab279290, 1:500, Abcam), Rabbit anti-Norepinephrine transporter (NET) (ab254361, 1:100, Abcam), Rabbit anti-Lysosome-associated membrane protein 2 (Lamp2) (bs-2739R, 1:200, Bioss), Rabbit anti-MERTK (ab184086, 1:500, Abcam).

Techniques: Control, Labeling

Journal: Autophagy

Article Title: CHCHD2 and CHCHD10 promoted autophagic clearance of protein aggregates via GABARAPs

doi: 10.1080/15548627.2026.2678427

Figure Lengend Snippet: Plasmids.

Article Snippet: MYC-LAMP2A , Origene TM Technologies , RC221216.

Techniques: Plasmid Preparation

Agrimol B blocks autophagic flux in PDAC cells. (A, B) Western blot analysis of P62 and CTSD in PANC-1 and AsPC-1 cells treated with Agrimol B for 24 h. (C, E, F) Immunofluorescence analysis of RFP-GFP-LC3 after PANC-1 and AsPC-1 cells were transfected with RFP-GFP-LC3 for 48 h, followed by treatment with or without Agrimol B for another 24 h. Scale bars, 10 μm. (D, G-L) Immunofluorescence analysis of the colocalization of endogenous LC3 with LAMP2 after treatment with Agrimol B or rapamycin for 24 h in PANC-1 and AsPC-1 cells. Scale bars, 10 μm. (M-O) Immunofluorescence analysis of LC3 in PDAC cells treated with or without Agrimol B in the presence or absence of HCQ. Scale bars, 10 μm.

Journal: Precision Clinical Medicine

Article Title: Agrimol B inhibits pancreatic ductal adenocarcinoma by induction of lethal mitophagy through decreasing mitochondrial transcription termination factor 3

doi: 10.1093/pcmedi/pbag009

Figure Lengend Snippet: Agrimol B blocks autophagic flux in PDAC cells. (A, B) Western blot analysis of P62 and CTSD in PANC-1 and AsPC-1 cells treated with Agrimol B for 24 h. (C, E, F) Immunofluorescence analysis of RFP-GFP-LC3 after PANC-1 and AsPC-1 cells were transfected with RFP-GFP-LC3 for 48 h, followed by treatment with or without Agrimol B for another 24 h. Scale bars, 10 μm. (D, G-L) Immunofluorescence analysis of the colocalization of endogenous LC3 with LAMP2 after treatment with Agrimol B or rapamycin for 24 h in PANC-1 and AsPC-1 cells. Scale bars, 10 μm. (M-O) Immunofluorescence analysis of LC3 in PDAC cells treated with or without Agrimol B in the presence or absence of HCQ. Scale bars, 10 μm.

Article Snippet: An anti-microtubule-associated protein light chain 3 (LC3) antibody (NB100-2220) was purchased from Novus, while anti-MTERF3 (EM1701-29) and lysosomal associated membrane protein 2 (LAMP2) (M1603-5) antibodies were purchased from HuaBio.

Techniques: Western Blot, Immunofluorescence, Transfection

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

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

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

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antibody against lamp2 (Santa Cruz Biotechnology)

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