Review

lamp2 (Proteintech)

Proteintech is a verified supplier

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

Proteintech lamp2
Lamp2, supplied by Proteintech, used in various techniques. Bioz Stars score: 96/100, based on 220 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/lamp2/LAMP2+Antibody/pm42865485-124-115-117
Average 96 stars, based on 220 article reviews

lamp2 - by Bioz Stars, 2026-10

96/100 stars

Images

Labeling:

Article Title: α-hederin decreases the glycolysis level in intestinal epithelial cells via SNX10-mediated DEPDC5 degradation
Article Snippet: Rapamycin (HY-10219), cycloheximide (HY-12320), chloroquine (HY-17589A), and Pronase E (HY-114158) were obtained from MedChemExpress (Monmouth Junction, NJ, USA). .. Antibodies against mTOR (ab2732), Raptor (ab40768), p70S6K (ab32529), 4EBP1 (ab32024), p-4EBP1 (ab278686), LAMP-2A (ab125068, ab18528), Alexa Fluor® 594 labeled Goat anti-rabbit IgG (H + L) (ab150080), Alexa Fluor® 647 labeled Goat anti-mouse IgG (H + L) (ab150115), Alexa Fluor® 488 labeled Goat anti-mouse IgG (H + L) (ab150113), and Alexa Fluor® 488 labeled Goat anti-rabbit IgG (H + L) (ab150077) were supplied by Abcam, and p-mTOR (5536S), GβL (3274S), c-Myc (5605T), LDHA (3582T), PKM2 (4053T), anti-mouse IgG (7076P2) and anti-rabbit IgG (7074P2) were obtained from CST (Danvers, MA, USA), SNX10 (sc-293380) was provided by Santa Cruz (Dallas, TX, USA), β-Tubulin ( M20005 ), DEPDC5 (TA7028), p-DEPDC5 (Ser1002) (TA8614) were purchased from Abmart (Shanghai, China), and mTOR (66888-1-Ig), HSC70 (ab51052), LAMP2 (66301-1-Ig) and Flag (66008-4-Ig) were obtain from Proteintech (Wuhan, China). .. Five human CRC cells DLD-1, Lovo, Caco-2, SW620, and HT29, and two normal human IECs, FHC and NCM460, and human embryonic kidney cell HEK-293T were obtained from American Type Culture Collection (ATCC, Rockville, Maryland, USA).

other:

Article Title: Targeting the HDAC4-NHE6-endosomal pH axis restores amyloid-β clearance and cognitive function in Alzheimer's disease mice.
Article Snippet: 108 2 Materials and Methods 109 Materials 110 The antibodies used are as follows: IBA1 (Oasis, OB-PGP049-01), Aβ (BioLegend, 111 800708), LRP1 (ZRB1311), GFAP (FujiFilm, MO389), β-amyloid-FITC (MCE, HY112 P3908), LAMP2 (Proteintech, 66301-1-Ig), S100A10 (Proteintech, 11250-1-AP).

Incubation:

Article Title: N-acetylglucosamine ameliorates the transition from acute kidney injury to chronic kidney disease by reducing the accumulation of lipid droplets.
Article Snippet: Acute kidney injury (AKI) can advance to chronic kidney disease (CKD) and ultimately to renal fibrosis.. Inadequate repair of renal tubular epithelial cells (TECs) after injury is a major driver of fibrosis.. N-acetylglucosamine (NAG), a natural bioactive monosaccharide involved in metabolism and glycoprotein synthesis, has antiinflammatory and antioxidant properties.

Western Blot:

Article Title: Architecture of the human KICSTOR complex and its role in mTORC1 regulation
Article Snippet: The Precision Plus Protein Dual Color Standards (Bio-Rad, 161–0394) were used as a pre-stained protein ladder during electrophoresis. .. The following primary antibodies were used for Western blotting: pS6K1 T389 (CST, 9234; 1:20,000), S6K1 (CST, 9202; 1:20,000), WDR59 (CST, 53385; 1:5,000), NPRL2 (CST, 37344; 1:2,000), KPTN (Proteintech, 16094-1-AP; 1:1,000), Calnexin (Proteintech, 66903-1-Ig; 1:5,000), LAMP2 (Proteintech, 27823-1-AP; 1:5,000), TOMM20 (ABclonal, A19403; 1:5,000), HA-HRP (ABclonal, AE025; 1:10,000), GFP (ABclonal, AE078; 1:5,000), MIOS (Bethyl, A304-699A; 1:5,000), GAPDH-HRP (MBL, M171-7; 1:20,000), and Flag-HRP (Sigma, A8592; 1:20,000). .. Anti-rabbit HRP (7074; 1:20,000) was purchased from Cell Signaling Technology; antimouse HRP (SA00001-1; 1:20,000) was purchased from Proteintech.

Hemagglutination Assay:

Image Search Results

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

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

Review

lamp2 (Proteintech)

Structured Review

Images

Related Articles

Labeling:

other:

Incubation:

Western Blot:

Hemagglutination Assay:

Similar Products

Image Search Results