Review




Structured Review

ABclonal Biotechnology primary antibody against lamp2
Structure and expression changes caused by mutant <t>LAMP2</t> . (A) in-silico structural modeling of wild-type LAMP2. The orange part shows the part that is truncated in the mutant LAMP2. The blue segment indicates the lumenal part of LAMP2. The white segment indicates the transmembrane part of LAMP2. The orange segment indicates the cytoplasmic part of LAMP2. (B) In-silico structural modeling of mutant LAMP2. The red segment indicates the mistranslated segment caused by the insertion mutation. The transmembrane helical domain is missing. (C) Immunohistochemical analyses for LAMP2. (D) Relative expression of LAMP2 in patient's and healthy controls' peripheral blood measured via proteomic analysis.
Primary Antibody Against Lamp2, supplied by ABclonal Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/primary antibody against lamp2/product/ABclonal Biotechnology
Average 90 stars, based on 1 article reviews
primary antibody against lamp2 - by Bioz Stars, 2026-03
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Images

1) Product Images from "De novo LAMP2 insertion mutation causes cardiac-only Danon disease: A case report"

Article Title: De novo LAMP2 insertion mutation causes cardiac-only Danon disease: A case report

Journal: Frontiers in Cardiovascular Medicine

doi: 10.3389/fcvm.2022.899283

Structure and expression changes caused by mutant LAMP2 . (A) in-silico structural modeling of wild-type LAMP2. The orange part shows the part that is truncated in the mutant LAMP2. The blue segment indicates the lumenal part of LAMP2. The white segment indicates the transmembrane part of LAMP2. The orange segment indicates the cytoplasmic part of LAMP2. (B) In-silico structural modeling of mutant LAMP2. The red segment indicates the mistranslated segment caused by the insertion mutation. The transmembrane helical domain is missing. (C) Immunohistochemical analyses for LAMP2. (D) Relative expression of LAMP2 in patient's and healthy controls' peripheral blood measured via proteomic analysis.
Figure Legend Snippet: Structure and expression changes caused by mutant LAMP2 . (A) in-silico structural modeling of wild-type LAMP2. The orange part shows the part that is truncated in the mutant LAMP2. The blue segment indicates the lumenal part of LAMP2. The white segment indicates the transmembrane part of LAMP2. The orange segment indicates the cytoplasmic part of LAMP2. (B) In-silico structural modeling of mutant LAMP2. The red segment indicates the mistranslated segment caused by the insertion mutation. The transmembrane helical domain is missing. (C) Immunohistochemical analyses for LAMP2. (D) Relative expression of LAMP2 in patient's and healthy controls' peripheral blood measured via proteomic analysis.

Techniques Used: Expressing, Mutagenesis, In Silico, Immunohistochemical staining



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Dimethyl malonate inhibits ferritinophagy and the accumulation of Fe 2+ in lysosomes. HT22 cells were subjected to oxygen-glucose deprivation (OGD) for 6 h. (A) Confocal microscopy images of the colocalization of FTH1 (red) with <t>LAMP2</t> (green). Scale bar = 100 μm (n = 5). (B) FTH1 and LAMP2 colocalization quantified with a Pearson correlation (n = 5). (C) Fluorescence quantification of FTH1 (n = 5). (D) Fluorescence quantification of LAMP2 (n = 5). (E) Representative immunofluorescence images of FerroOrange (red) and LysoTracker Green (green) used to examine the subcellular localization of Fe 2+ in cells. Scale bar = 50 μm (n = 5). (F) FerroOrange and LysoTracker colocalization quantified with a Pearson correlation (n = 5). (G) Fluorescence quantification of LysoTracker (n = 5). The data are expressed as mean ± SD. Statistical comparisons were conducted using a one-way ANOVA with a Tukey post hoc test for multiple comparisons. ∗ P ≤ 0.05, ∗∗ P ≤ 0.01.
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Dimethyl malonate inhibits ferritinophagy and the accumulation of Fe 2+ in lysosomes. HT22 cells were subjected to oxygen-glucose deprivation (OGD) for 6 h. (A) Confocal microscopy images of the colocalization of FTH1 (red) with <t>LAMP2</t> (green). Scale bar = 100 μm (n = 5). (B) FTH1 and LAMP2 colocalization quantified with a Pearson correlation (n = 5). (C) Fluorescence quantification of FTH1 (n = 5). (D) Fluorescence quantification of LAMP2 (n = 5). (E) Representative immunofluorescence images of FerroOrange (red) and LysoTracker Green (green) used to examine the subcellular localization of Fe 2+ in cells. Scale bar = 50 μm (n = 5). (F) FerroOrange and LysoTracker colocalization quantified with a Pearson correlation (n = 5). (G) Fluorescence quantification of LysoTracker (n = 5). The data are expressed as mean ± SD. Statistical comparisons were conducted using a one-way ANOVA with a Tukey post hoc test for multiple comparisons. ∗ P ≤ 0.05, ∗∗ P ≤ 0.01.
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Dimethyl malonate inhibits ferritinophagy and the accumulation of Fe 2+ in lysosomes. HT22 cells were subjected to oxygen-glucose deprivation (OGD) for 6 h. (A) Confocal microscopy images of the colocalization of FTH1 (red) with <t>LAMP2</t> (green). Scale bar = 100 μm (n = 5). (B) FTH1 and LAMP2 colocalization quantified with a Pearson correlation (n = 5). (C) Fluorescence quantification of FTH1 (n = 5). (D) Fluorescence quantification of LAMP2 (n = 5). (E) Representative immunofluorescence images of FerroOrange (red) and LysoTracker Green (green) used to examine the subcellular localization of Fe 2+ in cells. Scale bar = 50 μm (n = 5). (F) FerroOrange and LysoTracker colocalization quantified with a Pearson correlation (n = 5). (G) Fluorescence quantification of LysoTracker (n = 5). The data are expressed as mean ± SD. Statistical comparisons were conducted using a one-way ANOVA with a Tukey post hoc test for multiple comparisons. ∗ P ≤ 0.05, ∗∗ P ≤ 0.01.
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Dimethyl malonate inhibits ferritinophagy and the accumulation of Fe 2+ in lysosomes. HT22 cells were subjected to oxygen-glucose deprivation (OGD) for 6 h. (A) Confocal microscopy images of the colocalization of FTH1 (red) with <t>LAMP2</t> (green). Scale bar = 100 μm (n = 5). (B) FTH1 and LAMP2 colocalization quantified with a Pearson correlation (n = 5). (C) Fluorescence quantification of FTH1 (n = 5). (D) Fluorescence quantification of LAMP2 (n = 5). (E) Representative immunofluorescence images of FerroOrange (red) and LysoTracker Green (green) used to examine the subcellular localization of Fe 2+ in cells. Scale bar = 50 μm (n = 5). (F) FerroOrange and LysoTracker colocalization quantified with a Pearson correlation (n = 5). (G) Fluorescence quantification of LysoTracker (n = 5). The data are expressed as mean ± SD. Statistical comparisons were conducted using a one-way ANOVA with a Tukey post hoc test for multiple comparisons. ∗ P ≤ 0.05, ∗∗ P ≤ 0.01.
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Dimethyl malonate inhibits ferritinophagy and the accumulation of Fe 2+ in lysosomes. HT22 cells were subjected to oxygen-glucose deprivation (OGD) for 6 h. (A) Confocal microscopy images of the colocalization of FTH1 (red) with <t>LAMP2</t> (green). Scale bar = 100 μm (n = 5). (B) FTH1 and LAMP2 colocalization quantified with a Pearson correlation (n = 5). (C) Fluorescence quantification of FTH1 (n = 5). (D) Fluorescence quantification of LAMP2 (n = 5). (E) Representative immunofluorescence images of FerroOrange (red) and LysoTracker Green (green) used to examine the subcellular localization of Fe 2+ in cells. Scale bar = 50 μm (n = 5). (F) FerroOrange and LysoTracker colocalization quantified with a Pearson correlation (n = 5). (G) Fluorescence quantification of LysoTracker (n = 5). The data are expressed as mean ± SD. Statistical comparisons were conducted using a one-way ANOVA with a Tukey post hoc test for multiple comparisons. ∗ P ≤ 0.05, ∗∗ P ≤ 0.01.
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Dimethyl malonate inhibits ferritinophagy and the accumulation of Fe 2+ in lysosomes. HT22 cells were subjected to oxygen-glucose deprivation (OGD) for 6 h. (A) Confocal microscopy images of the colocalization of FTH1 (red) with <t>LAMP2</t> (green). Scale bar = 100 μm (n = 5). (B) FTH1 and LAMP2 colocalization quantified with a Pearson correlation (n = 5). (C) Fluorescence quantification of FTH1 (n = 5). (D) Fluorescence quantification of LAMP2 (n = 5). (E) Representative immunofluorescence images of FerroOrange (red) and LysoTracker Green (green) used to examine the subcellular localization of Fe 2+ in cells. Scale bar = 50 μm (n = 5). (F) FerroOrange and LysoTracker colocalization quantified with a Pearson correlation (n = 5). (G) Fluorescence quantification of LysoTracker (n = 5). The data are expressed as mean ± SD. Statistical comparisons were conducted using a one-way ANOVA with a Tukey post hoc test for multiple comparisons. ∗ P ≤ 0.05, ∗∗ P ≤ 0.01.
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Dimethyl malonate inhibits ferritinophagy and the accumulation of Fe 2+ in lysosomes. HT22 cells were subjected to oxygen-glucose deprivation (OGD) for 6 h. (A) Confocal microscopy images of the colocalization of FTH1 (red) with <t>LAMP2</t> (green). Scale bar = 100 μm (n = 5). (B) FTH1 and LAMP2 colocalization quantified with a Pearson correlation (n = 5). (C) Fluorescence quantification of FTH1 (n = 5). (D) Fluorescence quantification of LAMP2 (n = 5). (E) Representative immunofluorescence images of FerroOrange (red) and LysoTracker Green (green) used to examine the subcellular localization of Fe 2+ in cells. Scale bar = 50 μm (n = 5). (F) FerroOrange and LysoTracker colocalization quantified with a Pearson correlation (n = 5). (G) Fluorescence quantification of LysoTracker (n = 5). The data are expressed as mean ± SD. Statistical comparisons were conducted using a one-way ANOVA with a Tukey post hoc test for multiple comparisons. ∗ P ≤ 0.05, ∗∗ P ≤ 0.01.
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Dimethyl malonate inhibits ferritinophagy and the accumulation of Fe 2+ in lysosomes. HT22 cells were subjected to oxygen-glucose deprivation (OGD) for 6 h. (A) Confocal microscopy images of the colocalization of FTH1 (red) with <t>LAMP2</t> (green). Scale bar = 100 μm (n = 5). (B) FTH1 and LAMP2 colocalization quantified with a Pearson correlation (n = 5). (C) Fluorescence quantification of FTH1 (n = 5). (D) Fluorescence quantification of LAMP2 (n = 5). (E) Representative immunofluorescence images of FerroOrange (red) and LysoTracker Green (green) used to examine the subcellular localization of Fe 2+ in cells. Scale bar = 50 μm (n = 5). (F) FerroOrange and LysoTracker colocalization quantified with a Pearson correlation (n = 5). (G) Fluorescence quantification of LysoTracker (n = 5). The data are expressed as mean ± SD. Statistical comparisons were conducted using a one-way ANOVA with a Tukey post hoc test for multiple comparisons. ∗ P ≤ 0.05, ∗∗ P ≤ 0.01.
Primary Antibodies Against Tfeb, Gfp, Lamp2, Ndrg1, Smpd1, And Actin, supplied by Proteintech, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Structure and expression changes caused by mutant <t>LAMP2</t> . (A) in-silico structural modeling of wild-type LAMP2. The orange part shows the part that is truncated in the mutant LAMP2. The blue segment indicates the lumenal part of LAMP2. The white segment indicates the transmembrane part of LAMP2. The orange segment indicates the cytoplasmic part of LAMP2. (B) In-silico structural modeling of mutant LAMP2. The red segment indicates the mistranslated segment caused by the insertion mutation. The transmembrane helical domain is missing. (C) Immunohistochemical analyses for LAMP2. (D) Relative expression of LAMP2 in patient's and healthy controls' peripheral blood measured via proteomic analysis.
Primary Antibody Against Lamp2, supplied by ABclonal Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/result/primary antibody against lamp2/product/ABclonal Biotechnology
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QLX exerts anti‐inflammatory effects in CGN‐induced CNP via NF‐κB. A, The prostate index was determined by the weight of prostate relative to the rat bodyweight. B, Representative HE staining of prostate tissue is shown. C, Representative IF staining photographs of <t>Ly6G</t> in prostate tissue are shown. SN50 was injected as described in the methods description, and CGN and QLX addition was done as described in Figure . # P < .05, ## P < .01 (control vs CGN‐treated rats); ** P < .01 (QLX‐treated vs CGN‐treated rats); $ P < .05 (SN50‐treated in CGN rat models vs only CGN‐treated rats)
Primary Antibody Against Lamp2 And Ly6g, supplied by Santa Cruz Biotechnology, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Image Search Results


Dimethyl malonate inhibits ferritinophagy and the accumulation of Fe 2+ in lysosomes. HT22 cells were subjected to oxygen-glucose deprivation (OGD) for 6 h. (A) Confocal microscopy images of the colocalization of FTH1 (red) with LAMP2 (green). Scale bar = 100 μm (n = 5). (B) FTH1 and LAMP2 colocalization quantified with a Pearson correlation (n = 5). (C) Fluorescence quantification of FTH1 (n = 5). (D) Fluorescence quantification of LAMP2 (n = 5). (E) Representative immunofluorescence images of FerroOrange (red) and LysoTracker Green (green) used to examine the subcellular localization of Fe 2+ in cells. Scale bar = 50 μm (n = 5). (F) FerroOrange and LysoTracker colocalization quantified with a Pearson correlation (n = 5). (G) Fluorescence quantification of LysoTracker (n = 5). The data are expressed as mean ± SD. Statistical comparisons were conducted using a one-way ANOVA with a Tukey post hoc test for multiple comparisons. ∗ P ≤ 0.05, ∗∗ P ≤ 0.01.

Journal: Redox Biology

Article Title: Dimethyl malonate preserves brain and neurobehavioral phenotype following neonatal hypoxia–ischemia by inhibiting FTH1-mediated ferritinophagy

doi: 10.1016/j.redox.2025.103792

Figure Lengend Snippet: Dimethyl malonate inhibits ferritinophagy and the accumulation of Fe 2+ in lysosomes. HT22 cells were subjected to oxygen-glucose deprivation (OGD) for 6 h. (A) Confocal microscopy images of the colocalization of FTH1 (red) with LAMP2 (green). Scale bar = 100 μm (n = 5). (B) FTH1 and LAMP2 colocalization quantified with a Pearson correlation (n = 5). (C) Fluorescence quantification of FTH1 (n = 5). (D) Fluorescence quantification of LAMP2 (n = 5). (E) Representative immunofluorescence images of FerroOrange (red) and LysoTracker Green (green) used to examine the subcellular localization of Fe 2+ in cells. Scale bar = 50 μm (n = 5). (F) FerroOrange and LysoTracker colocalization quantified with a Pearson correlation (n = 5). (G) Fluorescence quantification of LysoTracker (n = 5). The data are expressed as mean ± SD. Statistical comparisons were conducted using a one-way ANOVA with a Tukey post hoc test for multiple comparisons. ∗ P ≤ 0.05, ∗∗ P ≤ 0.01.

Article Snippet: Primary antibodies against LAMP2 (mouse anti-LAMP2, 66301-1-lg, Proteintech; 1:200) and FTH1 (rabbit anti-FTH1, 83428-1-RR, Proteintech; 1:200) were applied and maintained at 4 °C overnight [ ].

Techniques: Confocal Microscopy, Fluorescence, Immunofluorescence

Structure and expression changes caused by mutant LAMP2 . (A) in-silico structural modeling of wild-type LAMP2. The orange part shows the part that is truncated in the mutant LAMP2. The blue segment indicates the lumenal part of LAMP2. The white segment indicates the transmembrane part of LAMP2. The orange segment indicates the cytoplasmic part of LAMP2. (B) In-silico structural modeling of mutant LAMP2. The red segment indicates the mistranslated segment caused by the insertion mutation. The transmembrane helical domain is missing. (C) Immunohistochemical analyses for LAMP2. (D) Relative expression of LAMP2 in patient's and healthy controls' peripheral blood measured via proteomic analysis.

Journal: Frontiers in Cardiovascular Medicine

Article Title: De novo LAMP2 insertion mutation causes cardiac-only Danon disease: A case report

doi: 10.3389/fcvm.2022.899283

Figure Lengend Snippet: Structure and expression changes caused by mutant LAMP2 . (A) in-silico structural modeling of wild-type LAMP2. The orange part shows the part that is truncated in the mutant LAMP2. The blue segment indicates the lumenal part of LAMP2. The white segment indicates the transmembrane part of LAMP2. The orange segment indicates the cytoplasmic part of LAMP2. (B) In-silico structural modeling of mutant LAMP2. The red segment indicates the mistranslated segment caused by the insertion mutation. The transmembrane helical domain is missing. (C) Immunohistochemical analyses for LAMP2. (D) Relative expression of LAMP2 in patient's and healthy controls' peripheral blood measured via proteomic analysis.

Article Snippet: For immunohistochemistry, a primary antibody against LAMP2 (1:100 dilution) was obtained from Abclonal (China, A14017) and a secondary antibody (goat anti-rabbit, 1:2000 dilution) was obtained from Abcam (England, ab205718).

Techniques: Expressing, Mutagenesis, In Silico, Immunohistochemical staining

QLX exerts anti‐inflammatory effects in CGN‐induced CNP via NF‐κB. A, The prostate index was determined by the weight of prostate relative to the rat bodyweight. B, Representative HE staining of prostate tissue is shown. C, Representative IF staining photographs of Ly6G in prostate tissue are shown. SN50 was injected as described in the methods description, and CGN and QLX addition was done as described in Figure . # P < .05, ## P < .01 (control vs CGN‐treated rats); ** P < .01 (QLX‐treated vs CGN‐treated rats); $ P < .05 (SN50‐treated in CGN rat models vs only CGN‐treated rats)

Journal: Journal of Cellular and Molecular Medicine

Article Title: Qianliexin capsule exerts anti‐inflammatory activity in chronic non‐bacterial prostatitis and benign prostatic hyperplasia via NF‐κB and inflammasome

doi: 10.1111/jcmm.16599

Figure Lengend Snippet: QLX exerts anti‐inflammatory effects in CGN‐induced CNP via NF‐κB. A, The prostate index was determined by the weight of prostate relative to the rat bodyweight. B, Representative HE staining of prostate tissue is shown. C, Representative IF staining photographs of Ly6G in prostate tissue are shown. SN50 was injected as described in the methods description, and CGN and QLX addition was done as described in Figure . # P < .05, ## P < .01 (control vs CGN‐treated rats); ** P < .01 (QLX‐treated vs CGN‐treated rats); $ P < .05 (SN50‐treated in CGN rat models vs only CGN‐treated rats)

Article Snippet: Primary antibody against LAMP2 and Ly6G (SCBT) was incubated overnight at 4°C.

Techniques: Staining, Injection, Control