p62/SQSTM1 Antibody (2C11)

Immunocytochemistry/Immunofluorescence: p62/SQSTM1 Antibody (2C11) [H00008878-M01] - Analysis of p62 in SH-SY5Y cells using anti-p62/SQSTM1 antibody. Red - p62 puncta; Blue - nuclear DAPI; Green - Cytoskeleton. Image from verified customer review.

Western Blot: p62/SQSTM1 Antibody (2C11) [H00008878-M01] - Disruption of the VANGL2-p62/SQSTM1 interaction in breast cancer cells. Soft agar colony formation of T47D cells overexpressing GFP, GFP-VANGL2 and GFP-p62/SQSTM1 (right). Protein expression was revealed with anti-p62/SQSTM1, anti-VANGL2 and anti-GFP antibodies by western blot analysis (right). In anti-GFP blot, the arrowhead indicates position of co-migrating GFP-VANGL2 and GFP-p62/SQSTM1 and the asterisk pinpoints GFP alone. Error bars represent mean+/-s.d. (n=3). Image collected and cropped by CiteAb from the following publication (https://www.nature.com/doifinder/10.1038/ncomms10318), licensed under a CC-BY license.

Immunocytochemistry/Immunofluorescence: p62/SQSTM1 Antibody (2C11) [H00008878-M01] - Analysis of p62/SQSTM1 antibody on HeLa cells. Image from verified customer review.

Western Blot: p62/SQSTM1 Antibody (2C11) [H00008878-M01] - Confirmation of loss of hepatic ATG7 protein and a phenotype of hepatic autophagy inactivation. Fourth ug of liver protein were loaded on 4-20% gradient Tris-Glycine gels and subsequently immunoblotted with antibodies against ATG7, p62 and LC3. Blots were visualized with G:BOX Chemi XRQ (SynGene). Representative immunoblots are shown for WT and KO mice. Full-length immunoblots are presented in Supplementary Figure S1. ATG7: autophagy-related protein 7; p62: sequestosome 1; LC3: microtubule-associated protein 1 light chain 3; WT: Mx1-Cre-Atg7F/F mouse; KO: Mx1-Cre+Atg7F/F mouse. Image collected and cropped by CiteAb from the following publication (https://www.nature.com/articles/s41598-017-14405-w), licensed under a CC-BY license.

ELISA: p62/SQSTM1 Antibody (2C11) [H00008878-M01] - Detection limit for recombinant GST tagged SQSTM1 is approximately 0.03ng/ml as a capture antibody.

Western Blot: p62/SQSTM1 Antibody (2C11) [H00008878-M01] -

Confirmation of loss of hepatic ATG7 protein and a phenotype of hepatic autophagy inactivation. Fourty ug of liver protein were loaded on 4-20% gradient Tris-Glycine gels and subsequently immunoblotted with antibodies against ATG7, p62 and LC3. Blots were visualised with G:BOX Chemi XRQ (SynGene). Representative immunoblots are shown for WT and KO mice. Full-length immunoblots are presented in Supplementary Figure S1. ATG7: autophagy-related protein 7; p62: sequestosome 1; LC3: microtubule-associated protein 1 light chain 3; WT: Mx1-Cre-Atg7F/F mouse; KO: Mx1-Cre+Atg7F/F mouse. Image collected and cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/29074879), licensed under a CC-BY licence.

Western Blot: p62/SQSTM1 Antibody (2C11) [H00008878-M01] -

miR-29a downregulates TFEB and ATG9A to inhibit autophagy. D). 5ug of total protein cell lysates from Panc-1 cells were transfected with CTRL, miR-29a mimics, siCTRL, siTFEB, or siATG9A. 24 hours post-transfection, total protein was harvested and subjected to western blot analysis for p62 and LC3B, and GAPDH was used as loading control. Quantification of band intensities normalized to GAPDH and relative to control are shown below respective blots. All experiments were repeated 3 times and representative data is presented. Image collected and cropped by CiteAb from the following publication (https://www.oncotarget.com/lookup/doi/10.18632/oncotarget.11928), licensed under a CC-BY licence.

Simple Western: p62/SQSTM1 Antibody (2C11) [H00008878-M01] -

Time-dependent effects of subacute administration of effective dose of escitalopram (5 mg/kg/day) for 3 and 7 days on expression of 5-HT7R in the thalamic plasma membrane fraction (Panel (A)). Ordinate: mean ± SD (n = 6) of the relative protein level of 5-HT7R in the thalamic plasma membrane fraction. Panel (B) indicates the pseudo-gel images using capillary immunoblotting. ** p 0.01 vs. control by one-way analysis of variance with Tukey’s post-hoc test. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/33572981), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunoprecipitation: p62/SQSTM1 Antibody (2C11) [H00008878-M01] -

TAZ stimulates exercise-induced mitochondrial biogenesis and increases respiratory metabolism and activity.a Wild-type (WT) and muscle-specific TAZ knockout (mKO) mice were subjected to endurance exercise training. The gastrocnemius muscle obtained from these mice was isolated and embedded in paraffin. The sectioned tissues were immunostained with an anti-COX4 antibody to visualise the mitochondria. Scale bar = 50 μm. b Genomic DNA was isolated from the gastrocnemius muscle of mice described in (a). Relative mitochondrial DNA copy number was determined via quantitative PCR using primers for mitochondrial-encoded Cox2 and nuclear-encoded beta-globin. The Ct values of mitochondrial Cox2 were normalized to those of nuclear beta-globin; n = 6 for each genotype (WT untrained vs. mKO untrained; *p = 0.0188, WT untrained vs. WT trained; **p = 0.0069, WT trained vs. mKO trained; ***p = 0.0002). c Protein from the gastrocnemius muscle of mice described in (a) was assessed via immunoblotting to observe the indicated proteins. GAPDH was used as the loading control. d RNA was isolated from the gastrocnemius muscle of mice described in (a). Mitochondrial-encoded marker gene expression was analysed via quantitative reverse transcription (qRT)-PCR, n = 6 for each genotype (mt-Atp6; **p = 0.0035 for WT untrained vs. mKO untrained, **p = 0.0071 for WT untrained vs. WT trained, ****p  0.0001 for WT trained vs. mKO trained, mt-Co2; *p = 0.0174 for WT untrained vs. mKO untrained, ****p  0.0001 for WT untrained vs. WT trained, ****p  0.0001 for WT trained vs. mKO trained, mt-Cytb; *p = 0.0214 for WT untrained vs. mKO untrained, *p = 0.0124 for WT untrained vs. WT trained, ****p  0.0001 for WT trained vs. mKO trained, mt-Nd5; *p = 0.0186 for WT untrained vs. mKO untrained, **p = 0.0059 for WT untrained vs. WT trained, ****p  0.0001 for WT trained vs. mKO trained). e Nuclear-encoded mitochondrial gene expression in the gastrocnemius muscle of mice in (a) was analysed via qRT-PCR, n = 6 for each genotype (Atp5a1; *p = 0.0137 for WT untrained vs. WT trained, **p = 0.0048 for eKO untrained vs. eKO trained, Idh3g; **p = 0.0089 for WT untrained vs. WT trained, Ndufa10; *p = 0.0205 for WT untrained vs. WT trained, Uqcrc1; ****p  0.0001 for WT untrained vs. WT trained, **p = 0.0011 for mKO untrained vs. mKO trained). f The respiratory metabolism of mice described in (a) was analysed using the Oxylet system. Data are shown as the average values observed under light and dark conditions; n = 6 for each condition (VO2-light; **p = 0.0033 for WT untrained vs. mKO untrained, **p = 0.0098 for WT trained vs. mKO trained, VO2-dark; *p = 0.0146 for WT untrained vs. mKO untrained, ***p  0.0007 for WT untrained vs. WT trained, ****p  0.0001 for WT trained vs. mKO trained, VCO2-dark; ****p  0.0001 for WT untrained vs. WT trained, ****p  0.0001 for WT trained vs. mKO trained, Energy expenditure-light; *p = 0.0234 for mKO untrained vs. mKO trained, Energy expenditure-dark; *p = 0.021 for WT untrained vs. mKO untrained, ***p = 0.0001 for WT untrained vs. WT trained, ****p  0.0001 for WT trained vs. mKO trained). Ten to twelve-week-old mice were used for all panels. Data are presented as mean ± SEM for (b, d–f). Statistical significance was analysed via two-way ANOVA with Sidak’s multiple comparison test. Representative data was shown and experiments were performed at least twice with similar results for (a, c). Source data are provided as a Source data file. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/35115527), licensed under a CC-BY license. Not internally tested by Novus Biologicals.

Immunohistochemistry: p62/SQSTM1 Antibody (2C11) [H00008878-M01] -

Immunocytochemistry analysis of histone induced activations of caspase 1, caspase 3, and NLRP3 (400×). BMECs were cultured briefly on cover glasses (pre-treated with poly-L –lysine, 0.1 mg/mL, Sigma-Aldrich) and incubated with histone (50 and 100 μg/mL) for 16 h. The samples were visualized with DAB, counterstained with hematoxylin and observed by inverted microscope. Three independent experiments were carried out by light microscope analyses. Image collected and cropped by CiteAb from the following open publication (https://pubmed.ncbi.nlm.nih.gov/31156617), licensed under a CC-BY license. Not internally tested by Novus Biologicals.