P62 ab56416

Manufactured by Abcam

Sourced in United States

p62 (ab56416) is a protein that plays a role in the autophagy pathway. It serves as a cargo receptor, recognizing and binding to ubiquitinated proteins targeted for degradation. This product is suitable for use in various research applications involving the study of autophagy and cellular degradation processes.

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Lab products found in correlation

Close spelling variants of this product

Ab56416 (204 citations) Anti-p62 (ab56416) (4 citations) Mouse anti-p62 (ab56416) (2 citations) Anti-SQSTM1/p62 (ab56416, (2 citations)

6 protocols using p62 ab56416

Autophagy-Related Protein Detection

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The following antibodies were purchased from Abcam: p62 (ab56416), LAMP2A (ab18528), SNAP29 (ab138500), VAMP8 (ab75021). The STX17 antibody was purchased from Proteintech (17815-1-AP). The antibody against LC3B (for western blots and immunofluorescence (IF) with p62) was purchased from Novus Biologics (NB100-2220). The secondary goat anti-rabbit IgG antibody was purchased from R&D systems (HAF008). The Alexa Fluor^® 488 secondary goat anti-mouse IgG antibody was purchased from Invitrogen (A11001). The following were purchased from Sigma-Aldrich: Chloroquine diphosphate salt (C6628), and anti-β-actin (A5441). The following antibody was purchased from Cell Signaling: anti-NBR1 (#9891). The following were purchased from Jackson ImmunoResearch: Rhodamine Red^TM goat anti-mouse IgG secondary antibody for TRITC (115-295-146), Alexa Fluor^® 488 goat anti-rabbit IgG secondary antibody for FITC (111-545-144), HRP goat anti-mouse secondary antibody (115-036-003). The Lysotraker Red DND-99 reagent was purchased from Invitrogen (L752). Cathepsin B activity fluorometric assay kit was purchased from Biovision (#K-140).

Aivazidis S., Jain A., Rauniyar A.K., Anderson C.C., Marentette J.O., Orlicky D.J., Fritz K.S., Harris P.S., Siegel D., Maclean K.N, & Roede J.R. (2019). SNARE proteins rescue impaired autophagic flux in Down syndrome. PLoS ONE, 14(11), e0223254.

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Baicalin-Mediated Apoptosis and Autophagy

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Baicalin (purity > 98%) (Shanghai Yuanye Biotechnology, Shanghai, China) was dissolved in DMSO. DMSO (<0.5%) was added to the control group as a vehicle control. N-Acetyl-L-cysteine (NAC) was obtained from Beyotime Institute of Biotechnology. 3-Methyladenine (3-MA) was obtained from Solarbio Biotechnology (Beijing, China). Antibodies against Bcl-2(D55G8), Bax (D2E11), cleaved PARP (Asp214), cleaved caspase-3 (Asp175), p-ERK1/2 (D13.14.4E), p-AKT (D25E6), β-catenin (D10A8), AKT (C67E7), p-mTOR (D9C2), mTOR (7C10), GAPDH (D16H11), c-Myc (E5Q6W), Cdk2 (E8J9T), cyclinE1 (D7T3U), cyclinA2 (E6D1J) and the secondary antibodies (goat anti-rabbit IgG and anti-mouse IgG) were purchased from Cell Signaling Technology (Beverly, MA, USA). Caspase-3 (ab13847), LC3 (ab48394) and p62 (ab56416) antibodies were obtained from Abcam Biotechnology. Antibodies against ERK1/2 (C-9) were obtained from Santa Cruz Biotechnology.

Pang H., Wu T., Peng Z., Tan Q., Peng X., Zhan Z., Song L, & Wei B. (2022). Baicalin induces apoptosis and autophagy in human osteosarcoma cells by increasing ROS to inhibit PI3K/Akt/mTOR, ERK1/2 and β-catenin signaling pathways. Journal of Bone Oncology, 33, 100415.

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Analyzing GJA8 Expression in HLE Cells

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HLE cells were adhered overnight in 6-well plates to grow to 80% cell density, then transfection with or without 1.0 or 2.0 μg/well peGFP-C1-GJA8 plasmid for 24 h, and washed with PBS for twice, replaced with no fetal calf serum media for 2 h or 4 h (Sta2h/Sta4h group) or complete medium (NC group) for 2 h. Then the cells were lysed in lysis buffer (Shenggong, Shanghai, China) and blocked in 5% BSA (Shenggong, Shanghai, China) in TBST (0.1% Tween-20 in TBS). Immunocomplexes were separated by 10% SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) and then subjected to immunoprecipitation with the primary antibody [P62 (ab56416) 1:1000, α-Tubulin (ab4074) 1:1000 from Abcam], and the HPR-conjugated second antibody.

Yu X., Ping X., Zhang X., Cui Y., Yang H., Tang X., Tang Y, & Shentu X. (2018). The impact of GJA8 SNPs on susceptibility to age-related cataract. Human Genetics, 137(11), 897-904.

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Exploring Cellular Stress Response Pathways

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Ubiquitin (#3933), UBA1 (#4891), p21 (#2947), Cyclin D1 (#2922), CDC2 (#9116), c-Jun (#9165), cleaved PARP (#9532), LC3B (#3868), PERK (#5683), p-PERK (#3179), CHOP (#2895), ATF4 (#11815), IRE1α (#3294), eIF2α (#5324), p-eIF2α (#9721), XBP1s (#27901), GRP78 (#3177), cleaved caspase-3 (#9661), p-JNK (#9251), and β-actin (#9562) primary antibodies were purchased from Cell Signaling Technology (CST, MA, USA). Antibody against Ki-67 (RM-9106) was purchased from Thermo Fisher (Waltham, MA, USA). ATF6 (sc-166659 and JNK1 (sc-1648) antibodies were obtained from Santa Cruz Biotechnology (Santa Cruz, CA, USA). p-IRE1α (ab243665) and p62 (ab56416) were purchased from Abcam (Burlingame, CA, USA). UBA1 inhibitor TAK-243 was obtained from CSNpharm (CSNpharm, Chicago, IL, USA). TAK-243 was dissolved in DMSO to create a 10 mmol/L solution, which was diluted to different concentrations in DMEM medium before use.

Liu G., Yu J., Wu R., Shi L., Zhang X., Zhang W., Zhong X., Wang Y., Li H., Shen Y., Wu C., Yu R., Niu M, & Liu X. (2021). GRP78 determines glioblastoma sensitivity to UBA1 inhibition-induced UPR signaling and cell death. Cell Death & Disease, 12(8), 733.

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Quantifying Diaphragm Protein Dynamics

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Diaphragm protein extracts were assayed as previously described [29 (link)]. Briefly, diaphragm tissues were homogenized 1:10 (wt/vol) in 5 mM Tris (pH 7.5) and 5 mM EDTA (pH 8.0) with a protease inhibitor cocktail (Sigma-Aldrich, St. Louis, MO) and centrifuged at 1500 g for 10 min at 4°C. Supernatant was collected and protein content was assessed by the Bradford method (Sigma-Aldrich). Proteins were separated via polyacrylamide gel electrophoresis. Membranes were probed for Beclin 1 (#3495), Atg12 (#4180), LC3B (#2775) (Cell Signaling Technology, Danvers, MA), Atg7 (NBP2-24682) (Novus Biologicals, Minneapolis, MN), p62 (ab56416), catalase (ab16731), PMP70 (ab3421) (Abcam, Cambridge, UK) and cathepsin L (sc-6498), spectrin (sc-48382). α-tubulin (sc-58667) (Santa Cruz Biotechnology, Dallas, TX) was also probed for as a loading control. In addition, mitochondrial protein extracts were also assayed via western blot. Membranes were probed for 4-HNE (ab46545), Parkin (ab15954), PINK1 (ab23707), Mul1 (ab84067), p62 (ab56416) (Abcam), OPA1 (612606), DLP1 (611112) (BD Biosciences, San Jose, CA), Mfn2 (M6444) (Sigma-Aldrich) and Fis1 (alx-210-907) (Enzo Life Sciences, Farmingdale, NY). VDAC (sc-8829) (Santa Cruz) was also probed as a loading control for all mitochondrial proteins.

Smuder A.J., Sollanek K.J., Nelson W.B., Min K., Talbert E.E., Kavazis A.N., Hudson M.B., Sandri M., Szeto H.H, & Powers S.K. (2017). Crosstalk between autophagy and oxidative stress regulates proteolysis in the diaphragm during mechanical ventilation. Free radical biology & medicine, 115, 179-190.

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Western Blot Analysis of Autophagy and ER Stress Markers

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Sample preparation and western blotting were performed as previously described [51 (link)]. Anti-Atg5-Atg12 complex (#4180), -Atg16L1 (#8089), -Bak (#12105), -Beclin1 (#3495), -Bim (#2933), -Calnexin (#2679), -CHOP (#2895), -cleaved PARP (#9541), -cytochrome c (#4280), -Ero1-Lα (#3264), -ERp44 (#3798), -ERp72 (#5033), -GRP94 (#2104), -LC3A/B-I/II (#12741), -Mcl-1 (#5453), -PDI (#3501) and -VDAC (#4661) antibodies were from Cell Signaling Technology (Beverly, MA, USA). Anti-β-actin (ab8226), -Bcl-2 (ab692), -cleaved caspase-3 (ab2302), -GAPDH (ab9485), -GRP78 (ab21685) and -p62 (ab56416) antibodies were from Abcam (Cambridge, MA, USA). Anti-XBP1s (sc-7160) antibody was from Santa Cruz Biotechnology (Santa Cruz, CA, USA). Anti-cleaved ATF6 (NBP1-40256) antibody was from Novus Biologicals (Littleton, CO). Horseradish peroxidase-conjugated goat anti-mouse and anti-rabbit immunoglobulin G secondary antibodies were from GenDEPOT (Barker, TX, USA). The blots were developed using a chemiluminescent detection kit (Ab Frontier, Seoul, Republic of Korea). Densitometric quantification of western blot bands was performed using Image J software, version 1.49 (http://rsb.info.nih.gov/ij/index.html).

Lee S., Kim S., Hwang S., Cherrington N.J, & Ryu D.Y. (2017). Dysregulated expression of proteins associated with ER stress, autophagy and apoptosis in tissues from nonalcoholic fatty liver disease. Oncotarget, 8(38), 63370-63381.

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