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anti atg5  (Bioss)


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    Bioss anti atg5
    Anti Atg5, supplied by Bioss, used in various techniques. Bioz Stars score: 90/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti atg5/product/Bioss
    Average 90 stars, based on 3 article reviews
    anti atg5 - by Bioz Stars, 2026-02
    90/100 stars

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    CGA inhibits Aβ 25-35 -induced autophagy in SH-SY5Y cells. Notes: ( A ) The viability of cells treated with various concentrations of CGA for 24 and 48 h was determined with MTT assay. ( B ) Representative MDC-stained autophagy vesicles in SH-SY5Y cells (right panel, ×200), and analysis of mean fluorescence intensity (left panel). ( C ) Representative Western blot imagines of LC3B-II/LC3B-I (16/18 KDa) and p62/SQSTM (75 KDa) in SH-SY5Y cells (left panel); β-actin (43 KDa) was used as a control for protein loading. The right panel shows the relative optical density values of LC3B-II/LC3B-I and p62/SQSTM between the experimental groups. ( D ) Representative Western blot imagines of beclin1 (50 KDa) and <t>Atg5</t> (32 KDa) in SH-SY5Y cells (left panel); GAPDH (37 KDa) was used as a control for protein loading. The right panel shows the relative optical density values of beclin1 and Atg5 between the experimental groups. ( E ) SH-SY5Y cells expressing mCherry-GFP-LC3 stably were treated in the presence or absence of CGA. Autophagosomes (yellow foci) and autophagic flux (red-only foci) were measured with confocal fluorescence microscopy (FV1200; Olympus, Tokyo, Japan). Three independent experiments were performed, and the date are expressed the mean ± s.e.m for five samples per treatment group. **P<0.01 compared with the no Aβ 25-35 treatment group; # P<0.05, ## P<0.05, ### P<0.001 compared with the Aβ 25-35 treatment group.
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    Figure 2. MARCH5 regulates SMAD2 and <t>ATG5</t> mRNA and protein levels. (A and B) MARCH5 mRNA and protein levels were downregulated by infection with LV3–1 and LV3–2. (C) Ovarian cancer SKOV3 cells were infected with LV3-NC and LV3–1. SMAD2 and ATG5 mRNA and protein levels were downregulated by infection with LV3–1 and LV3–2. (D) Ovarian cancer SKOV3 cells were transfected with MARCH5 30 UTR. SMAD2 and ATG5 mRNA and protein levels were upregulated. (E) Putative binding sites targeted by MIR30A were predicted to be located in the 30 UTR of MARCH5, ATG5, and SMAD2 mRNA. (F) SKOV3 cells were cotransfected with MIR30A mimics or control RNA (NC) with luciferase reporter plasmids containing either wild-type (pMIR-MARCH5–3UTR, pMIR-ATG5–3UTR, and pMIR-SMAD2–3UTR) or mutant 30 UTR (pMIR- MARCH5–3UTRm, pMIR-ATG5–3UTRm, and pMIR-SMAD2–3UTRm) of MARCH5, ATG5, and SMAD2 genes. Luciferase expression was measured. The fold changes of the rel- ative luciferase activity in MIR30A mimics with the indicated plasmids transfected cells were normalized to NC with the corresponding indicated plasmid-transfected cells. (G) Ovarian cancer SKOV3 cells were transfected with MIR30 mimics or control RNA (NC). (H) Ovarian cancer SKOV3 cells were transfected with MIR30 inhibitor or control RNA (NC). (I) Ovarian cancer SKOV3 cells were infected with LV3-NC and LV3–1. One group was infected with LV3–1-transfected MIR30A inhibitors. Error bars represent standard error. The symbols and indicate p < 0.05 and 0.01, respectively.
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    CGA inhibits Aβ 25-35 -induced autophagy in SH-SY5Y cells. Notes: ( A ) The viability of cells treated with various concentrations of CGA for 24 and 48 h was determined with MTT assay. ( B ) Representative MDC-stained autophagy vesicles in SH-SY5Y cells (right panel, ×200), and analysis of mean fluorescence intensity (left panel). ( C ) Representative Western blot imagines of LC3B-II/LC3B-I (16/18 KDa) and p62/SQSTM (75 KDa) in SH-SY5Y cells (left panel); β-actin (43 KDa) was used as a control for protein loading. The right panel shows the relative optical density values of LC3B-II/LC3B-I and p62/SQSTM between the experimental groups. ( D ) Representative Western blot imagines of beclin1 (50 KDa) and Atg5 (32 KDa) in SH-SY5Y cells (left panel); GAPDH (37 KDa) was used as a control for protein loading. The right panel shows the relative optical density values of beclin1 and Atg5 between the experimental groups. ( E ) SH-SY5Y cells expressing mCherry-GFP-LC3 stably were treated in the presence or absence of CGA. Autophagosomes (yellow foci) and autophagic flux (red-only foci) were measured with confocal fluorescence microscopy (FV1200; Olympus, Tokyo, Japan). Three independent experiments were performed, and the date are expressed the mean ± s.e.m for five samples per treatment group. **P<0.01 compared with the no Aβ 25-35 treatment group; # P<0.05, ## P<0.05, ### P<0.001 compared with the Aβ 25-35 treatment group.

    Journal: Drug Design, Development and Therapy

    Article Title: Chlorogenic Acid Alleviates Aβ 25-35 -Induced Autophagy and Cognitive Impairment via the mTOR/TFEB Signaling Pathway

    doi: 10.2147/DDDT.S235969

    Figure Lengend Snippet: CGA inhibits Aβ 25-35 -induced autophagy in SH-SY5Y cells. Notes: ( A ) The viability of cells treated with various concentrations of CGA for 24 and 48 h was determined with MTT assay. ( B ) Representative MDC-stained autophagy vesicles in SH-SY5Y cells (right panel, ×200), and analysis of mean fluorescence intensity (left panel). ( C ) Representative Western blot imagines of LC3B-II/LC3B-I (16/18 KDa) and p62/SQSTM (75 KDa) in SH-SY5Y cells (left panel); β-actin (43 KDa) was used as a control for protein loading. The right panel shows the relative optical density values of LC3B-II/LC3B-I and p62/SQSTM between the experimental groups. ( D ) Representative Western blot imagines of beclin1 (50 KDa) and Atg5 (32 KDa) in SH-SY5Y cells (left panel); GAPDH (37 KDa) was used as a control for protein loading. The right panel shows the relative optical density values of beclin1 and Atg5 between the experimental groups. ( E ) SH-SY5Y cells expressing mCherry-GFP-LC3 stably were treated in the presence or absence of CGA. Autophagosomes (yellow foci) and autophagic flux (red-only foci) were measured with confocal fluorescence microscopy (FV1200; Olympus, Tokyo, Japan). Three independent experiments were performed, and the date are expressed the mean ± s.e.m for five samples per treatment group. **P<0.01 compared with the no Aβ 25-35 treatment group; # P<0.05, ## P<0.05, ### P<0.001 compared with the Aβ 25-35 treatment group.

    Article Snippet: Anti-Beclin1 (no. AH11208656) and anti-ATG5/APG5L (no. AB04011456,) were purchased from Bioss (Woburn, MA, USA).

    Techniques: MTT Assay, Staining, Western Blot, Expressing, Stable Transfection, Fluorescence, Microscopy

    Figure 2. MARCH5 regulates SMAD2 and ATG5 mRNA and protein levels. (A and B) MARCH5 mRNA and protein levels were downregulated by infection with LV3–1 and LV3–2. (C) Ovarian cancer SKOV3 cells were infected with LV3-NC and LV3–1. SMAD2 and ATG5 mRNA and protein levels were downregulated by infection with LV3–1 and LV3–2. (D) Ovarian cancer SKOV3 cells were transfected with MARCH5 30 UTR. SMAD2 and ATG5 mRNA and protein levels were upregulated. (E) Putative binding sites targeted by MIR30A were predicted to be located in the 30 UTR of MARCH5, ATG5, and SMAD2 mRNA. (F) SKOV3 cells were cotransfected with MIR30A mimics or control RNA (NC) with luciferase reporter plasmids containing either wild-type (pMIR-MARCH5–3UTR, pMIR-ATG5–3UTR, and pMIR-SMAD2–3UTR) or mutant 30 UTR (pMIR- MARCH5–3UTRm, pMIR-ATG5–3UTRm, and pMIR-SMAD2–3UTRm) of MARCH5, ATG5, and SMAD2 genes. Luciferase expression was measured. The fold changes of the rel- ative luciferase activity in MIR30A mimics with the indicated plasmids transfected cells were normalized to NC with the corresponding indicated plasmid-transfected cells. (G) Ovarian cancer SKOV3 cells were transfected with MIR30 mimics or control RNA (NC). (H) Ovarian cancer SKOV3 cells were transfected with MIR30 inhibitor or control RNA (NC). (I) Ovarian cancer SKOV3 cells were infected with LV3-NC and LV3–1. One group was infected with LV3–1-transfected MIR30A inhibitors. Error bars represent standard error. The symbols and indicate p < 0.05 and 0.01, respectively.

    Journal: Autophagy

    Article Title: MARCH5 RNA promotes autophagy, migration, and invasion of ovarian cancer cells.

    doi: 10.1080/15548627.2016.1256520

    Figure Lengend Snippet: Figure 2. MARCH5 regulates SMAD2 and ATG5 mRNA and protein levels. (A and B) MARCH5 mRNA and protein levels were downregulated by infection with LV3–1 and LV3–2. (C) Ovarian cancer SKOV3 cells were infected with LV3-NC and LV3–1. SMAD2 and ATG5 mRNA and protein levels were downregulated by infection with LV3–1 and LV3–2. (D) Ovarian cancer SKOV3 cells were transfected with MARCH5 30 UTR. SMAD2 and ATG5 mRNA and protein levels were upregulated. (E) Putative binding sites targeted by MIR30A were predicted to be located in the 30 UTR of MARCH5, ATG5, and SMAD2 mRNA. (F) SKOV3 cells were cotransfected with MIR30A mimics or control RNA (NC) with luciferase reporter plasmids containing either wild-type (pMIR-MARCH5–3UTR, pMIR-ATG5–3UTR, and pMIR-SMAD2–3UTR) or mutant 30 UTR (pMIR- MARCH5–3UTRm, pMIR-ATG5–3UTRm, and pMIR-SMAD2–3UTRm) of MARCH5, ATG5, and SMAD2 genes. Luciferase expression was measured. The fold changes of the rel- ative luciferase activity in MIR30A mimics with the indicated plasmids transfected cells were normalized to NC with the corresponding indicated plasmid-transfected cells. (G) Ovarian cancer SKOV3 cells were transfected with MIR30 mimics or control RNA (NC). (H) Ovarian cancer SKOV3 cells were transfected with MIR30 inhibitor or control RNA (NC). (I) Ovarian cancer SKOV3 cells were infected with LV3-NC and LV3–1. One group was infected with LV3–1-transfected MIR30A inhibitors. Error bars represent standard error. The symbols and indicate p < 0.05 and 0.01, respectively.

    Article Snippet: Detection of protein expression by western blotting The expressions of SMAD2, p-SMAD2, ATG5, MARCH5, and GAPDH proteins were analyzed by western blot.23 The primary antibodies used include polyclonal rabbit anti-MARCH5 (Bioss Biotechnology Company, bs-9339R); rabbit monoclonal to SMAD2 (Abcam, ab40855); rabbit monoclonal to p-SMAD2 (Abcam, ab188334); and polyclonal rabbit anti-GAPDH (Santa Cruz Biotechnology, AB10016).

    Techniques: Infection, Transfection, Binding Assay, Control, Luciferase, Mutagenesis, Expressing, Activity Assay, Plasmid Preparation

    Figure 3. ATG5 and SMAD2 modulation of MARCH5 levels are MIR30A dependent. (A) Ovarian cancer SKOV3 cells were transfected with control RNA (NC), ATG5 siRNA, and ATG5 siRNA C MIR30A inhibitor. (B) Ovarian cancer SKOV3 cells were transfected with control RNA (NC), SMAD2 siRNA, and SMAD2 siRNAC MIR30A inhibitor. (C) Ovarian cancer SKOV3 cells were transfected with control RNA (NC), ATG5 siRNA, and ATG5 siRNA C MIR30A inhibitor. (D) Ovarian cancer SKOV3 cells were transfected with control RNA (NC), SMAD2 siRNA, and SMAD2 siRNA C MIR30A inhibitor. Error bars represent standard error. The symbols and indicate p < 0.05 and 0.01, respectively.

    Journal: Autophagy

    Article Title: MARCH5 RNA promotes autophagy, migration, and invasion of ovarian cancer cells.

    doi: 10.1080/15548627.2016.1256520

    Figure Lengend Snippet: Figure 3. ATG5 and SMAD2 modulation of MARCH5 levels are MIR30A dependent. (A) Ovarian cancer SKOV3 cells were transfected with control RNA (NC), ATG5 siRNA, and ATG5 siRNA C MIR30A inhibitor. (B) Ovarian cancer SKOV3 cells were transfected with control RNA (NC), SMAD2 siRNA, and SMAD2 siRNAC MIR30A inhibitor. (C) Ovarian cancer SKOV3 cells were transfected with control RNA (NC), ATG5 siRNA, and ATG5 siRNA C MIR30A inhibitor. (D) Ovarian cancer SKOV3 cells were transfected with control RNA (NC), SMAD2 siRNA, and SMAD2 siRNA C MIR30A inhibitor. Error bars represent standard error. The symbols and indicate p < 0.05 and 0.01, respectively.

    Article Snippet: Detection of protein expression by western blotting The expressions of SMAD2, p-SMAD2, ATG5, MARCH5, and GAPDH proteins were analyzed by western blot.23 The primary antibodies used include polyclonal rabbit anti-MARCH5 (Bioss Biotechnology Company, bs-9339R); rabbit monoclonal to SMAD2 (Abcam, ab40855); rabbit monoclonal to p-SMAD2 (Abcam, ab188334); and polyclonal rabbit anti-GAPDH (Santa Cruz Biotechnology, AB10016).

    Techniques: Transfection, Control

    Figure 5. Silencing MARCH5 inhibited pelvic peritoneal metastasis in a nude mice model. (A) Mean tumor weight on d 35 after tumor cell injection. LV3–1- and LV3-NC- infected SKOV3 cells were implanted by IP injection. The arrow indicates the lesion in the abdominal cavity. (B) Immunohistochemical analysis of MARCH5, ATG5, SMAD2, and p-SMAD2 expression was performed on tumor xenografts. Representative images are shown (original magnification £200). Error bars represent standard error. The symbols and indicate p < 0.05 and 0.01, respectively. Scale bar: 100 mm.

    Journal: Autophagy

    Article Title: MARCH5 RNA promotes autophagy, migration, and invasion of ovarian cancer cells.

    doi: 10.1080/15548627.2016.1256520

    Figure Lengend Snippet: Figure 5. Silencing MARCH5 inhibited pelvic peritoneal metastasis in a nude mice model. (A) Mean tumor weight on d 35 after tumor cell injection. LV3–1- and LV3-NC- infected SKOV3 cells were implanted by IP injection. The arrow indicates the lesion in the abdominal cavity. (B) Immunohistochemical analysis of MARCH5, ATG5, SMAD2, and p-SMAD2 expression was performed on tumor xenografts. Representative images are shown (original magnification £200). Error bars represent standard error. The symbols and indicate p < 0.05 and 0.01, respectively. Scale bar: 100 mm.

    Article Snippet: Detection of protein expression by western blotting The expressions of SMAD2, p-SMAD2, ATG5, MARCH5, and GAPDH proteins were analyzed by western blot.23 The primary antibodies used include polyclonal rabbit anti-MARCH5 (Bioss Biotechnology Company, bs-9339R); rabbit monoclonal to SMAD2 (Abcam, ab40855); rabbit monoclonal to p-SMAD2 (Abcam, ab188334); and polyclonal rabbit anti-GAPDH (Santa Cruz Biotechnology, AB10016).

    Techniques: Injection, Infection, Immunohistochemical staining, Expressing

    Figure 6. MARCH5 promotion of SKOV3 cell autophagy, migration, and invasion involves ATG5, SMAD2 and the TGFB1-SMAD2/3 pathway. (A) A2780 cells infected with LV5-GFP and LV5-MARCH5. After 48 h, puromycin was added at a concentration of 2.5 mg/ml. The cells were transfected with ATG5 siRNA, SMAD2 siRNA or LY2109761 was added (10 mM) for 48 h. The migration and invasion assays were performed in the presence of TGFB1 (10 ng/ml). (B) SKOV3 cells transfected with a plasmid encoding mRFP-GFP-LC3 and pCMV5 empty vector, pCMV5-MARCH5, pCMV5-MARCH5 C siATG5, pCMV5-MARCH5 C siSMAD2, and pCMV5-MARCH5 C LY2109761. After 48 h, TGFB1 was added at a concentration of 10 ng/ml. mRFP-GF-LC3 distribution in SKOV3 was analyzed by confocal microscopy after TGFB1 treatment for 24 h. The LC3 dots were quantified using image pro-plus 6.0 software. All experiments were repeated 3 times and the representative results are shown. The right panel indicates the quanti- fication of LC3 puncta numbers. Error bars represented standard error. The symbols and indicate p < 0.05 and 0.01, respectively. Scale bar: 100 mm.

    Journal: Autophagy

    Article Title: MARCH5 RNA promotes autophagy, migration, and invasion of ovarian cancer cells.

    doi: 10.1080/15548627.2016.1256520

    Figure Lengend Snippet: Figure 6. MARCH5 promotion of SKOV3 cell autophagy, migration, and invasion involves ATG5, SMAD2 and the TGFB1-SMAD2/3 pathway. (A) A2780 cells infected with LV5-GFP and LV5-MARCH5. After 48 h, puromycin was added at a concentration of 2.5 mg/ml. The cells were transfected with ATG5 siRNA, SMAD2 siRNA or LY2109761 was added (10 mM) for 48 h. The migration and invasion assays were performed in the presence of TGFB1 (10 ng/ml). (B) SKOV3 cells transfected with a plasmid encoding mRFP-GFP-LC3 and pCMV5 empty vector, pCMV5-MARCH5, pCMV5-MARCH5 C siATG5, pCMV5-MARCH5 C siSMAD2, and pCMV5-MARCH5 C LY2109761. After 48 h, TGFB1 was added at a concentration of 10 ng/ml. mRFP-GF-LC3 distribution in SKOV3 was analyzed by confocal microscopy after TGFB1 treatment for 24 h. The LC3 dots were quantified using image pro-plus 6.0 software. All experiments were repeated 3 times and the representative results are shown. The right panel indicates the quanti- fication of LC3 puncta numbers. Error bars represented standard error. The symbols and indicate p < 0.05 and 0.01, respectively. Scale bar: 100 mm.

    Article Snippet: Detection of protein expression by western blotting The expressions of SMAD2, p-SMAD2, ATG5, MARCH5, and GAPDH proteins were analyzed by western blot.23 The primary antibodies used include polyclonal rabbit anti-MARCH5 (Bioss Biotechnology Company, bs-9339R); rabbit monoclonal to SMAD2 (Abcam, ab40855); rabbit monoclonal to p-SMAD2 (Abcam, ab188334); and polyclonal rabbit anti-GAPDH (Santa Cruz Biotechnology, AB10016).

    Techniques: Migration, Infection, Concentration Assay, Transfection, Plasmid Preparation, Confocal Microscopy, Software

    Figure 8. The TGFB1-SMAD2/3 pathway regulates MARCH5, ATG5, and SMAD2 through MIR30A. (A) The TGFB1–SMAD2/3 signal pathway luciferase reporter activity was detected in ectopically expressing MARCH5 ovarian cancer A2780 cells infected with LV5-MARCH5. (B) The TGFB1–SMAD2/3 signal pathway luciferase reporter activity was detected in LV3–1-, LV3–2-, and LV3-NC-infected SKOV3 cells. (C) Ovarian cancer SKOV3 cells were transfected with LV5-GFP, LV5-MARCH5, LV5-MARCH5 C ATG5 siRNA, or LV5-MARCH5 C SMAD2 siRNA. The protein expression of p-SAMD2 was detected by western blot. (Di) The expression of MARCH5, ATG5, and SMAD2 mRNA in SKOV3 cells was regulated by TGFB1 and MIR30A mimics. (Dii) The expression of MIR30A in SKOV3 cells was regulated by TGFB1. (Diii) The expression of MARCH5, ATG5, and SMAD2 mRNA in SKOV3 cells was regulated by LY2109761 and MIR30A inhibitor. (Div) The expression of MIR30A in SKOV3 cells was regulated by LY2109761. (E) The putative binding sites between MIR30A and SMAD2/3. (F) A graphic abstract for the significance of the MARCH5 pathway (MIR30A, SMAD2/3, MARCH5, ATG5, and SMAD2). Data are expressed as mean § SD from 3 independent experiments. p < 0.05, and p < 0.01.

    Journal: Autophagy

    Article Title: MARCH5 RNA promotes autophagy, migration, and invasion of ovarian cancer cells.

    doi: 10.1080/15548627.2016.1256520

    Figure Lengend Snippet: Figure 8. The TGFB1-SMAD2/3 pathway regulates MARCH5, ATG5, and SMAD2 through MIR30A. (A) The TGFB1–SMAD2/3 signal pathway luciferase reporter activity was detected in ectopically expressing MARCH5 ovarian cancer A2780 cells infected with LV5-MARCH5. (B) The TGFB1–SMAD2/3 signal pathway luciferase reporter activity was detected in LV3–1-, LV3–2-, and LV3-NC-infected SKOV3 cells. (C) Ovarian cancer SKOV3 cells were transfected with LV5-GFP, LV5-MARCH5, LV5-MARCH5 C ATG5 siRNA, or LV5-MARCH5 C SMAD2 siRNA. The protein expression of p-SAMD2 was detected by western blot. (Di) The expression of MARCH5, ATG5, and SMAD2 mRNA in SKOV3 cells was regulated by TGFB1 and MIR30A mimics. (Dii) The expression of MIR30A in SKOV3 cells was regulated by TGFB1. (Diii) The expression of MARCH5, ATG5, and SMAD2 mRNA in SKOV3 cells was regulated by LY2109761 and MIR30A inhibitor. (Div) The expression of MIR30A in SKOV3 cells was regulated by LY2109761. (E) The putative binding sites between MIR30A and SMAD2/3. (F) A graphic abstract for the significance of the MARCH5 pathway (MIR30A, SMAD2/3, MARCH5, ATG5, and SMAD2). Data are expressed as mean § SD from 3 independent experiments. p < 0.05, and p < 0.01.

    Article Snippet: Detection of protein expression by western blotting The expressions of SMAD2, p-SMAD2, ATG5, MARCH5, and GAPDH proteins were analyzed by western blot.23 The primary antibodies used include polyclonal rabbit anti-MARCH5 (Bioss Biotechnology Company, bs-9339R); rabbit monoclonal to SMAD2 (Abcam, ab40855); rabbit monoclonal to p-SMAD2 (Abcam, ab188334); and polyclonal rabbit anti-GAPDH (Santa Cruz Biotechnology, AB10016).

    Techniques: Luciferase, Activity Assay, Expressing, Infection, Transfection, Western Blot, Binding Assay