LC3 Antibody Search Results


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    Cell Signaling Technology Inc lc3
    FOXO mediate hypoxia‐induced autophagy in human nucleus pulposus cells. (a,b) Gene expression analysis in human primary nucleus pulposus (NP) cells cultured under normoxia (20% oxygen) or hypoxia (1% oxygen) for 24 hr showing hypoxia‐induced activation of FOXO3 and HIF1A signaling (a) and autophagic genes (b). (c) Western blot analysis of <t>LC3‐I,</t> LC3‐II, and p62 protein levels in human NP cells cultured in normoxia or hypoxia for 24 hr in the presence or absence of 25 µM chloroquine (CQ). Panel on the right shows densitometric quantification of LC3‐II and β‐tubulin. Values shown are mean ± SD of three different experiments. (d) Human NP cells were transfected with siRNA specific for FOXO1 (siFOXO1), FOXO3 (siFOXO3), or a combination of both (siFOXO1 + 3) and cultured in hypoxia for 24 hr. Upper panel shows Western blot analysis of FOXO1 and FOXO3 proteins confirming FOXO knockdown. Lower panel shows gene expression analysis of antioxidant and autophagic genes upon FOXO knockdown. (e) Western blot analysis of LC3 protein levels in human NP cells transfected with the indicated siRNA and cultured in normoxia or hypoxia for 24 hr in the presence of 25 µM CQ. Lower panel shows densitometric quantification of LC3‐II and β‐tubulin. (f) Gene expression analysis in human immortalized NP cells transfected with plasmids encoding for GFP, FOXO1‐ER, or FOXO3‐ER and treated with 1 µM 4OHT for 24 hr. (g) Western blot analysis of FOXO1, FOXO3, and LC3 protein levels in human NP cells transfected with plasmids encoding for GFP, FOXO1‐ER, or FOXO3‐ER and treated with 1 µM 4‐hydroxytamoxifen (4OHT) for 24 hr in the presence or absence of 25 µM CQ. Values shown are mean ± SD . Statistical comparisons were assessed by an unpaired, two‐tailed t ‐test after testing for equal variance using an F ‐test. * p
    Lc3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lc3/product/Cell Signaling Technology Inc
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    lc3 - by Bioz Stars, 2021-05
    99/100 stars
      Buy from Supplier

    99
    Cell Signaling Technology Inc anti lc3
    Down-regulation of OGT promotes the formation of autolysosome induced by cisplatin. (A) OGT-deficient A2780 and SKOV3 cells were cultured in different concentrations of cisplatin with 3-MA (3 mM) or Baf (200 nM) for 48 h. Cell viability was measured by CCK-8. (B) OGT-deficient A2780 and SKOV3 cells were treated with 3-MA (3 mM) or Baf (200 nM) in the presence of cisplatin (5 µg/mL) for 24 h. Apoptotic cells were identified by ANXA5 and PI staining. (C-D) Control and OGT-deficient A2780 (C) and SKOV3 (D) cells were transfected with <t>mRFP-GFP-LC3</t> vector for 24 h and then treated with cisplatin (5 µg/mL) for 24 h. Representative images of fluorescent LC3 puncta are shown. The mean number of yellow puncta representing autophagosomes and the mean number of red puncta representing autolysosomes are plotted. * P
    Anti Lc3, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti lc3/product/Cell Signaling Technology Inc
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti lc3 - by Bioz Stars, 2021-05
    99/100 stars
      Buy from Supplier

    99
    Novus Biologicals lc3b antibody
    Down-regulation of OGT promotes the formation of autolysosome induced by cisplatin. (A) OGT-deficient A2780 and SKOV3 cells were cultured in different concentrations of cisplatin with 3-MA (3 mM) or Baf (200 nM) for 48 h. Cell viability was measured by CCK-8. (B) OGT-deficient A2780 and SKOV3 cells were treated with 3-MA (3 mM) or Baf (200 nM) in the presence of cisplatin (5 µg/mL) for 24 h. Apoptotic cells were identified by ANXA5 and PI staining. (C-D) Control and OGT-deficient A2780 (C) and SKOV3 (D) cells were transfected with <t>mRFP-GFP-LC3</t> vector for 24 h and then treated with cisplatin (5 µg/mL) for 24 h. Representative images of fluorescent LC3 puncta are shown. The mean number of yellow puncta representing autophagosomes and the mean number of red puncta representing autolysosomes are plotted. * P
    Lc3b Antibody, supplied by Novus Biologicals, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/lc3b antibody/product/Novus Biologicals
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    lc3b antibody - by Bioz Stars, 2021-05
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    99
    Millipore anti lc3b antibody
    Down-regulation of OGT promotes the formation of autolysosome induced by cisplatin. (A) OGT-deficient A2780 and SKOV3 cells were cultured in different concentrations of cisplatin with 3-MA (3 mM) or Baf (200 nM) for 48 h. Cell viability was measured by CCK-8. (B) OGT-deficient A2780 and SKOV3 cells were treated with 3-MA (3 mM) or Baf (200 nM) in the presence of cisplatin (5 µg/mL) for 24 h. Apoptotic cells were identified by ANXA5 and PI staining. (C-D) Control and OGT-deficient A2780 (C) and SKOV3 (D) cells were transfected with <t>mRFP-GFP-LC3</t> vector for 24 h and then treated with cisplatin (5 µg/mL) for 24 h. Representative images of fluorescent LC3 puncta are shown. The mean number of yellow puncta representing autophagosomes and the mean number of red puncta representing autolysosomes are plotted. * P
    Anti Lc3b Antibody, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/anti lc3b antibody/product/Millipore
    Average 99 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    anti lc3b antibody - by Bioz Stars, 2021-05
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    N/A
    LC3 Antibody is a Rabbit Polyclonal antibody against LC3 The product of this gene is a subunit of neuronal microtubule associated MAP1A and MAP1B proteins which are involved in microtubule
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    N/A
    Probably involved in formation of autophagosomal vacuoles autophagosomes
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    N/A
    The LC3 Antibody Pack from Novus Biologicals is a set of antibodies to LC3 These antibodies react with human mouse The LC3 Antibody Pack has been validated for the following
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    Image Search Results


    FOXO mediate hypoxia‐induced autophagy in human nucleus pulposus cells. (a,b) Gene expression analysis in human primary nucleus pulposus (NP) cells cultured under normoxia (20% oxygen) or hypoxia (1% oxygen) for 24 hr showing hypoxia‐induced activation of FOXO3 and HIF1A signaling (a) and autophagic genes (b). (c) Western blot analysis of LC3‐I, LC3‐II, and p62 protein levels in human NP cells cultured in normoxia or hypoxia for 24 hr in the presence or absence of 25 µM chloroquine (CQ). Panel on the right shows densitometric quantification of LC3‐II and β‐tubulin. Values shown are mean ± SD of three different experiments. (d) Human NP cells were transfected with siRNA specific for FOXO1 (siFOXO1), FOXO3 (siFOXO3), or a combination of both (siFOXO1 + 3) and cultured in hypoxia for 24 hr. Upper panel shows Western blot analysis of FOXO1 and FOXO3 proteins confirming FOXO knockdown. Lower panel shows gene expression analysis of antioxidant and autophagic genes upon FOXO knockdown. (e) Western blot analysis of LC3 protein levels in human NP cells transfected with the indicated siRNA and cultured in normoxia or hypoxia for 24 hr in the presence of 25 µM CQ. Lower panel shows densitometric quantification of LC3‐II and β‐tubulin. (f) Gene expression analysis in human immortalized NP cells transfected with plasmids encoding for GFP, FOXO1‐ER, or FOXO3‐ER and treated with 1 µM 4OHT for 24 hr. (g) Western blot analysis of FOXO1, FOXO3, and LC3 protein levels in human NP cells transfected with plasmids encoding for GFP, FOXO1‐ER, or FOXO3‐ER and treated with 1 µM 4‐hydroxytamoxifen (4OHT) for 24 hr in the presence or absence of 25 µM CQ. Values shown are mean ± SD . Statistical comparisons were assessed by an unpaired, two‐tailed t ‐test after testing for equal variance using an F ‐test. * p

    Journal: Aging Cell

    Article Title: FOXO are required for intervertebral disk homeostasis during aging and their deficiency promotes disk degeneration, et al. FOXO are required for intervertebral disk homeostasis during aging and their deficiency promotes disk degeneration

    doi: 10.1111/acel.12800

    Figure Lengend Snippet: FOXO mediate hypoxia‐induced autophagy in human nucleus pulposus cells. (a,b) Gene expression analysis in human primary nucleus pulposus (NP) cells cultured under normoxia (20% oxygen) or hypoxia (1% oxygen) for 24 hr showing hypoxia‐induced activation of FOXO3 and HIF1A signaling (a) and autophagic genes (b). (c) Western blot analysis of LC3‐I, LC3‐II, and p62 protein levels in human NP cells cultured in normoxia or hypoxia for 24 hr in the presence or absence of 25 µM chloroquine (CQ). Panel on the right shows densitometric quantification of LC3‐II and β‐tubulin. Values shown are mean ± SD of three different experiments. (d) Human NP cells were transfected with siRNA specific for FOXO1 (siFOXO1), FOXO3 (siFOXO3), or a combination of both (siFOXO1 + 3) and cultured in hypoxia for 24 hr. Upper panel shows Western blot analysis of FOXO1 and FOXO3 proteins confirming FOXO knockdown. Lower panel shows gene expression analysis of antioxidant and autophagic genes upon FOXO knockdown. (e) Western blot analysis of LC3 protein levels in human NP cells transfected with the indicated siRNA and cultured in normoxia or hypoxia for 24 hr in the presence of 25 µM CQ. Lower panel shows densitometric quantification of LC3‐II and β‐tubulin. (f) Gene expression analysis in human immortalized NP cells transfected with plasmids encoding for GFP, FOXO1‐ER, or FOXO3‐ER and treated with 1 µM 4OHT for 24 hr. (g) Western blot analysis of FOXO1, FOXO3, and LC3 protein levels in human NP cells transfected with plasmids encoding for GFP, FOXO1‐ER, or FOXO3‐ER and treated with 1 µM 4‐hydroxytamoxifen (4OHT) for 24 hr in the presence or absence of 25 µM CQ. Values shown are mean ± SD . Statistical comparisons were assessed by an unpaired, two‐tailed t ‐test after testing for equal variance using an F ‐test. * p

    Article Snippet: Specific antibodies used were FOXO1 (1:1,000; 2,880 T; Cell Signaling Technology, Danvers, MA, USA), FOXO3 (1:1,000; 2497S; Cell Signaling Technology), LC3 (1:1,000; 12,741 T; Cell Signaling Technology), p62 (SQSTM1, 8025S; 1:1,000; Cell Signaling Technology), HIF1A (1:1,000; 20960‐1‐AP; Proteintech) β‐tubulin (1:2,000; 66240‐1‐Ig; Proteintech), and GAPDH (1:5,000; AM4300; Thermo Fisher Scientific).

    Techniques: Expressing, Cell Culture, Activation Assay, Western Blot, Transfection, Two Tailed Test

    Reduced nucleus pulposus cell viability and impaired autophagy in FOXO‐deficient intervertebral disks. (a) Terminal deoxynucleotidyl transferase (TdT) dUTP Nick‐End Labeling (TUNEL) staining in lumbar intervertebral disks (IVD) isolated from Col2a1Cre −/− and Col2a1Cre‐FOXO KO mice at 4 and 6 months of age ( n = 5 mice per group). Lower panels show quantification of TUNEL‐positive cells in the NP and EP. No positive cells were observed in the AF. NP: nucleus pulposus; AF: annulus fibrosus; EP: endplate. Magnification bar = 100 µm. (b) TUNEL staining in lumbar IVD from AcanCreER −/− and AcanCreER‐FOXO KO mice at 12 months of age ( n = 5 mice per group). Lower panels show quantification of TUNEL‐positive cells in the NP and EP. (c) Gene expression analysis of homeostatic genes in NP from Col2a1Cre −/− and Col2a1Cre‐FOXO KO mice at 2 months of age ( n = 4 mice per group). (d) Immunofluorescence staining for LC3 in the NP of lumbar IVD isolated from Col2a1Cre −/− and Col2a1Cre‐FOXO KO mice at 4 months of age ( n = 5 mice per group) shows a decrease in immunostained cells in FOXO‐deficient NP cells. Right panel shows quantification of LC3 puncta per cell. Values shown are mean ± SD . Statistical comparisons were assessed by an unpaired, two‐tailed t ‐test after testing for equal variance using an F ‐test. Values are mean ± SD . * p

    Journal: Aging Cell

    Article Title: FOXO are required for intervertebral disk homeostasis during aging and their deficiency promotes disk degeneration, et al. FOXO are required for intervertebral disk homeostasis during aging and their deficiency promotes disk degeneration

    doi: 10.1111/acel.12800

    Figure Lengend Snippet: Reduced nucleus pulposus cell viability and impaired autophagy in FOXO‐deficient intervertebral disks. (a) Terminal deoxynucleotidyl transferase (TdT) dUTP Nick‐End Labeling (TUNEL) staining in lumbar intervertebral disks (IVD) isolated from Col2a1Cre −/− and Col2a1Cre‐FOXO KO mice at 4 and 6 months of age ( n = 5 mice per group). Lower panels show quantification of TUNEL‐positive cells in the NP and EP. No positive cells were observed in the AF. NP: nucleus pulposus; AF: annulus fibrosus; EP: endplate. Magnification bar = 100 µm. (b) TUNEL staining in lumbar IVD from AcanCreER −/− and AcanCreER‐FOXO KO mice at 12 months of age ( n = 5 mice per group). Lower panels show quantification of TUNEL‐positive cells in the NP and EP. (c) Gene expression analysis of homeostatic genes in NP from Col2a1Cre −/− and Col2a1Cre‐FOXO KO mice at 2 months of age ( n = 4 mice per group). (d) Immunofluorescence staining for LC3 in the NP of lumbar IVD isolated from Col2a1Cre −/− and Col2a1Cre‐FOXO KO mice at 4 months of age ( n = 5 mice per group) shows a decrease in immunostained cells in FOXO‐deficient NP cells. Right panel shows quantification of LC3 puncta per cell. Values shown are mean ± SD . Statistical comparisons were assessed by an unpaired, two‐tailed t ‐test after testing for equal variance using an F ‐test. Values are mean ± SD . * p

    Article Snippet: Specific antibodies used were FOXO1 (1:1,000; 2,880 T; Cell Signaling Technology, Danvers, MA, USA), FOXO3 (1:1,000; 2497S; Cell Signaling Technology), LC3 (1:1,000; 12,741 T; Cell Signaling Technology), p62 (SQSTM1, 8025S; 1:1,000; Cell Signaling Technology), HIF1A (1:1,000; 20960‐1‐AP; Proteintech) β‐tubulin (1:2,000; 66240‐1‐Ig; Proteintech), and GAPDH (1:5,000; AM4300; Thermo Fisher Scientific).

    Techniques: End Labeling, TUNEL Assay, Staining, Isolation, Mouse Assay, Expressing, Immunofluorescence, Two Tailed Test

    Down-regulation of OGT promotes the formation of autolysosome induced by cisplatin. (A) OGT-deficient A2780 and SKOV3 cells were cultured in different concentrations of cisplatin with 3-MA (3 mM) or Baf (200 nM) for 48 h. Cell viability was measured by CCK-8. (B) OGT-deficient A2780 and SKOV3 cells were treated with 3-MA (3 mM) or Baf (200 nM) in the presence of cisplatin (5 µg/mL) for 24 h. Apoptotic cells were identified by ANXA5 and PI staining. (C-D) Control and OGT-deficient A2780 (C) and SKOV3 (D) cells were transfected with mRFP-GFP-LC3 vector for 24 h and then treated with cisplatin (5 µg/mL) for 24 h. Representative images of fluorescent LC3 puncta are shown. The mean number of yellow puncta representing autophagosomes and the mean number of red puncta representing autolysosomes are plotted. * P

    Journal: Theranostics

    Article Title: Down-regulation of OGT promotes cisplatin resistance by inducing autophagy in ovarian cancer

    doi: 10.7150/thno.27806

    Figure Lengend Snippet: Down-regulation of OGT promotes the formation of autolysosome induced by cisplatin. (A) OGT-deficient A2780 and SKOV3 cells were cultured in different concentrations of cisplatin with 3-MA (3 mM) or Baf (200 nM) for 48 h. Cell viability was measured by CCK-8. (B) OGT-deficient A2780 and SKOV3 cells were treated with 3-MA (3 mM) or Baf (200 nM) in the presence of cisplatin (5 µg/mL) for 24 h. Apoptotic cells were identified by ANXA5 and PI staining. (C-D) Control and OGT-deficient A2780 (C) and SKOV3 (D) cells were transfected with mRFP-GFP-LC3 vector for 24 h and then treated with cisplatin (5 µg/mL) for 24 h. Representative images of fluorescent LC3 puncta are shown. The mean number of yellow puncta representing autophagosomes and the mean number of red puncta representing autolysosomes are plotted. * P

    Article Snippet: Cells were blocked with 0.1% BSA for 1 h at room temperature and subsequently incubated with anti-LC3 (1:100, CST, 2775s) and Lamp1 (1:200, Abcam, ab25630) at 4 °C overnight.

    Techniques: Cell Culture, CCK-8 Assay, Staining, Transfection, Plasmid Preparation

    O -GlcNAcylation of SNAP-29 regulates the interaction of SNAP-29 with Stx17 and VAMP8. (A) SKOV3 cells were transfected with SNAP-29 and SNAP-29 (Mut) vectors and then treated with cisplatin (5 µg/mL) for 24 h. The O -GlcNAcylation levels of SNAP-29 were tested by co-immunoprecipitation. (B) SKOV3 cells were transfected with SNAP-29-GFP, SNAP-29 (Mut)-GFP and RFP-LC3 vectors and then treated with cisplatin (5 µg/mL) for 24 h. Colocalization of SNAP-29 and LC3 was determined by confocal fluorescence microscopy. Scale bar represent 10 μm. (C) SKOV3 cells were transfected with control, SNAP-29 or SNAP-29 (Mut) vectors and then treated with cisplatin (5 µg/mL) for 24 h. The expressions of LC3 and p62 were measured by western blotting. (D) The expressions of LC3 and p62 in SKOV3 cells that were transfected with si Stx17 or si VAMP8 and treated with cisplatin (5 µg/mL) for 24 h. (E) SKOV3 cell were transfected with SNAP-29 or SNAP-29 (Mut) vectors and then treated with cisplatin (5 µg/mL) for 24 h. Then, cell extracts were immunoprecipitated with anti-SNAP-29 and the resulting precipitants were immunoblotted against Stx17 and VAMP8. Whole-cell lysates were tested for SNAP-29 and actin. The values are presented as mean ± SD (n = 3). ** P

    Journal: Theranostics

    Article Title: Down-regulation of OGT promotes cisplatin resistance by inducing autophagy in ovarian cancer

    doi: 10.7150/thno.27806

    Figure Lengend Snippet: O -GlcNAcylation of SNAP-29 regulates the interaction of SNAP-29 with Stx17 and VAMP8. (A) SKOV3 cells were transfected with SNAP-29 and SNAP-29 (Mut) vectors and then treated with cisplatin (5 µg/mL) for 24 h. The O -GlcNAcylation levels of SNAP-29 were tested by co-immunoprecipitation. (B) SKOV3 cells were transfected with SNAP-29-GFP, SNAP-29 (Mut)-GFP and RFP-LC3 vectors and then treated with cisplatin (5 µg/mL) for 24 h. Colocalization of SNAP-29 and LC3 was determined by confocal fluorescence microscopy. Scale bar represent 10 μm. (C) SKOV3 cells were transfected with control, SNAP-29 or SNAP-29 (Mut) vectors and then treated with cisplatin (5 µg/mL) for 24 h. The expressions of LC3 and p62 were measured by western blotting. (D) The expressions of LC3 and p62 in SKOV3 cells that were transfected with si Stx17 or si VAMP8 and treated with cisplatin (5 µg/mL) for 24 h. (E) SKOV3 cell were transfected with SNAP-29 or SNAP-29 (Mut) vectors and then treated with cisplatin (5 µg/mL) for 24 h. Then, cell extracts were immunoprecipitated with anti-SNAP-29 and the resulting precipitants were immunoblotted against Stx17 and VAMP8. Whole-cell lysates were tested for SNAP-29 and actin. The values are presented as mean ± SD (n = 3). ** P

    Article Snippet: Cells were blocked with 0.1% BSA for 1 h at room temperature and subsequently incubated with anti-LC3 (1:100, CST, 2775s) and Lamp1 (1:200, Abcam, ab25630) at 4 °C overnight.

    Techniques: Transfection, Immunoprecipitation, Fluorescence, Microscopy, Western Blot

    Down-regulation of OGT enhances autophagy induced by cisplatin in ovarian cancer cells. (A-B) A2780 and SKOV3 cells were treated with or without cisplatin (5 µg/mL) for 24 h. The expression levels of LC3 and p62 were tested by western blotting. (C-D) Control and OGT-deficient ovarian cancer cells were treated with cisplatin (5 µg/mL) for 24 h. LC3 and p62 expression levels were determined by western blotting. (E) Control and OGT-deficient ovarian cancer cells were cultured with cisplatin (5 µg/mL) for 24 h. LC3 puncta were detected by anti-LC3 by fluorescence microscopy. Scale bar represent 50 μm. The values are presented as mean ± SD (n = 3). ** P

    Journal: Theranostics

    Article Title: Down-regulation of OGT promotes cisplatin resistance by inducing autophagy in ovarian cancer

    doi: 10.7150/thno.27806

    Figure Lengend Snippet: Down-regulation of OGT enhances autophagy induced by cisplatin in ovarian cancer cells. (A-B) A2780 and SKOV3 cells were treated with or without cisplatin (5 µg/mL) for 24 h. The expression levels of LC3 and p62 were tested by western blotting. (C-D) Control and OGT-deficient ovarian cancer cells were treated with cisplatin (5 µg/mL) for 24 h. LC3 and p62 expression levels were determined by western blotting. (E) Control and OGT-deficient ovarian cancer cells were cultured with cisplatin (5 µg/mL) for 24 h. LC3 puncta were detected by anti-LC3 by fluorescence microscopy. Scale bar represent 50 μm. The values are presented as mean ± SD (n = 3). ** P

    Article Snippet: Cells were blocked with 0.1% BSA for 1 h at room temperature and subsequently incubated with anti-LC3 (1:100, CST, 2775s) and Lamp1 (1:200, Abcam, ab25630) at 4 °C overnight.

    Techniques: Expressing, Western Blot, Cell Culture, Fluorescence, Microscopy

    The O -GlcNAcylation level of SNAP-29 is associated with autophagy activity induced by cisplatin. (A) Control and OGT-deficient SKOV3 cells were transfected with NC siRNA or SNAP-29 siRNA and then treated with cisplatin (5 µg/mL) for 24 h. The expression levels of LC3 and p62 were examined by western blotting. (B) OGT-deficient SKOV3 cells were transfected with mRFP-GFP-LC3 vector for 24 h and then transfected with NC siRNA or SNAP-29 siRNA. After culturing in cisplatin (5 µg/mL) for 24 h, cells were imaged with a confocal microscope. Representative images of fluorescent LC3 puncta are shown. * P

    Journal: Theranostics

    Article Title: Down-regulation of OGT promotes cisplatin resistance by inducing autophagy in ovarian cancer

    doi: 10.7150/thno.27806

    Figure Lengend Snippet: The O -GlcNAcylation level of SNAP-29 is associated with autophagy activity induced by cisplatin. (A) Control and OGT-deficient SKOV3 cells were transfected with NC siRNA or SNAP-29 siRNA and then treated with cisplatin (5 µg/mL) for 24 h. The expression levels of LC3 and p62 were examined by western blotting. (B) OGT-deficient SKOV3 cells were transfected with mRFP-GFP-LC3 vector for 24 h and then transfected with NC siRNA or SNAP-29 siRNA. After culturing in cisplatin (5 µg/mL) for 24 h, cells were imaged with a confocal microscope. Representative images of fluorescent LC3 puncta are shown. * P

    Article Snippet: Cells were blocked with 0.1% BSA for 1 h at room temperature and subsequently incubated with anti-LC3 (1:100, CST, 2775s) and Lamp1 (1:200, Abcam, ab25630) at 4 °C overnight.

    Techniques: Activity Assay, Transfection, Expressing, Western Blot, Plasmid Preparation, Microscopy