Anti bcl 2

Manufactured by Abcam

Sourced in United States, United Kingdom, China, Japan

Anti-Bcl-2 is a laboratory reagent used in research applications. It is an antibody that specifically binds to the Bcl-2 protein, which is involved in the regulation of apoptosis (programmed cell death). The core function of Anti-Bcl-2 is to enable the detection and study of Bcl-2 expression in experimental systems.

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Lab products found in correlation

Anti bax, by Abcam (232 mentions) Anti caspase 3, by Abcam (81 mentions) Anti gapdh, by Abcam (69 mentions) Anti cleaved caspase 3, by Abcam (57 mentions) Anti β actin, by Abcam (46 mentions) Pvdf membrane, by Merck Group (39 mentions) Anti akt, by Abcam (22 mentions) Anti cyclin d1, by Abcam (22 mentions) Ripa lysis buffer, by Beyotime (21 mentions) Anti e cadherin, by Abcam (17 mentions) Anti cleaved caspase 3, by Cell Signaling Technology (17 mentions) Anti p akt, by Abcam (17 mentions) Anti akt, by Cell Signaling Technology (16 mentions) Anti bax, by Cell Signaling Technology (15 mentions) Anti gapdh, by Cell Signaling Technology (15 mentions) Anti p62, by Abcam (15 mentions) Bca protein assay kit, by Beyotime (15 mentions) Anti n cadherin, by Abcam (14 mentions) Anti ki67, by Abcam (14 mentions) Anti bcl xl, by Abcam (14 mentions)

Spelling variants of this product

Bcl-2 (961 citations) Rabbit anti-Bcl-2 (34 citations) Mouse anti-Bcl-2 (12 citations) Rabbit anti-Bcl-2 antibody (8 citations) Anti-Bcl-2 (#ab196495) (4 citations) Anti-B-cell lymphoma-2 (Bcl-2) (3 citations) Monoclonal rabbit anti-Bcl-2 (3 citations) Rabbit monoclonal Anti-Bcl-2 antibody (3 citations) Rabbit Anti-mouse Bcl-2 (2 citations) Anti-Bcl-2 Ab (2 citations)

397 protocols using anti bcl 2

Protein Extraction and Western Blot Analysis

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Protein extraction and western blot analysis were performed as previously described [39 (link)].
Cells were harvested for protein extraction 48h after transfection. Lysates from transfected cells were collected using RIPA buffer (Sigma R0278, St Louis, MO, USA). Protein lysates were separated on SDS-polyacrylamide gels, electroblotted onto polyvinylidene difluoride membrane and immunoblotted with primary antibodies, then with peroxidase-conjugated secondary antibodies. After three additional washes, the immune complex was detected by ECL detection (Thermo 34077; Rockford, IL, USA). The following antibodies were used: anti-Cyclin A2 (1540-1, Epitomics, Burlingame, CA, USA), anti-Cyclin B1(1495-1, Epitomics), anti-Cyclin D1(1677-1, Epitomics), anti-Cyclin E(4129;Cell Signaling Technology, Beverly, MA, USA), anti-Bcl-2 (1017-1, Epitomics), anti-PUMA(1652-1, Epitomics), anti-mdm2 (556353, BD PharMingen, San Diego, CA, USA), anti-Caspase-3 (1087-1, Epitomics), anti-p21(2990-1, Epitomics), anti-PARP-1 (1072-1, Epitomics), anti-Bax (1063-1, Epitomics), anti-β-actin (60008-1-Ig, Protein Tech, Chicago, IL, USA), goat anti-mouse IgG-HRP (sc-2005, Santa Cruz Biotechnology, Dallas, Texas) and goat anti-rabbit IgG-HRP (sc-2004, Santa Cruz Biotechnology).

He X., Liao J., Liu F., Yan J., Yan J., Shang H., Dou Q., Chang Y., Lin J, & Song Y. (2014). Functional repair of p53 mutation in colorectal cancer cells using trans-splicing. Oncotarget, 6(4), 2034-2045.

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Molecular Mechanisms of Pancreatic Cancer Progression

Cited 1 time

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Whole Pancreatic cancer cells were lysed on ice in a lysis buffer (RIPA, Beyotime, Shanghai, China) with a protease inhibitor mixture cocktail (Roche, Switzerland) after culturing in MRC-5-CM for 14 days. Western-blot analysis was performed by established protocols 43 (link). Anti-CTNNA1 and CTNNB1, anti-E-cadherin, anti-N-cadherin, anti-ZEB-1, ZEB-2, Snail, Slug and anti-vimentin primary antibodies were purchased from (Abcam); anti-MMP-2, 3, 13 and 21, anti-WNT-2, anti-WNT16, anti-TGFB1, anti-Src, P-Src-Y418 and P-Src-Y529 primary antibodies were purchased from (Epitomics); anti-Bcl-2, Bcl-xl, Bad, Bax, Bim, Bid, Caspase-3 and anti-β-actin were from ( Cell Signaling Technology).

Ding S.M., Lu A.L., Zhang W., Zhou L., Xie H.Y., Zheng S.S, & Li Q.Y. (2018). The role of cancer-associated fibroblast MRC-5 in pancreatic cancer. Journal of Cancer, 9(3), 614-628.

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Protein Expression Analysis in Paclitaxel-Treated Cells

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Cells were harvested at various times after paclitaxel treatment and disrupted in lysis buffer (1% Triton X-100, 1 mM ethyleneglycol-bis(2-aminoethyl ether)-N,N,N′,N′tetraacetic acid (EGTA), 1 mM EDTA, 10 mM Tris-HCl, pH 7.4, and protease inhibitors). Cell debris was removed by centrifugation at 10,000g for 10 min at 4°C. The resulting supernatants were resolved using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and transferred onto nitrocellulose membranes. The membranes were blocked with 5% non-fat dried milk at room temperature for 30 min and incubated with anti-TWIST (Bio Matrix Research, Japan), anti-phospho Akt (Cell Signaling Technology, Inc.), anti-Bcl-2 (Epitomics, USA), and anti-GAPDH. The membranes were then washed and incubated with horseradish peroxidase-conjugated secondary antibody. Signals were visualized using enhanced chemiluminescence (Amersham, UK). All western blot densitometry data were normalized for the loading control GAPDH by CS Analyzer.

Kwon C.H., Park H.J., Choi Y., Won Y.J., Lee S.J, & Park D.Y. (2017). TWIST mediates resistance to paclitaxel by regulating Akt and Bcl-2 expression in gastric cancer cells. Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine, 39(10).

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Extracellular Vesicle Protein Profiling

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eEV and eEV-IL-3 were lysed in lysis buffer (RIPA buffer with proteinase inhibitors). Starting from the same EV particle number, protein samples were quantified by the Bradford method before performing Western blot (50 µg proteins/each sample were loaded). Anti-CD63, anti-CD81, antiHSP90, anti-GM130, anti-Bcl-2 (Abcam, Milan, Italy), anti-MEK1/2, (Cell Signaling, Danvers, MA, USA), anti-CD29, anti-caveolin-1, anti-p-eNOS-ser1177 (Invitrogen, Carlsbad, CA, USA), and anti-vinculin (Millipore, Milan, Italy) antibodies were used as primary antibodies. Appropriate HRP-conjugated secondary antibodies (BioRad, Milan, Italy) were used, and proteins were detected with Clarity Western ECL substrate (BioRad, Milan, Italy). Image Lab Software (BioRad Milan, Italy) instrument was used for densitometric analysis. Data are expressed as arbitrary unit. Ponceaus-staining has been used as input (EV protein content normalization).

Penna C., Femminò S., Tapparo M., Lopatina T., Fladmark K.E., Ravera F., Comità S., Alloatti G., Giusti I., Dolo V., Camussi G., Pagliaro P, & Brizzi M.F. (2020). The Inflammatory Cytokine IL-3 Hampers Cardioprotection Mediated by Endothelial Cell-Derived Extracellular Vesicles Possibly via Their Protein Cargo. Cells, 10(1), 13.

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Western Blot Analysis of Apoptosis Markers

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Protein samples were separated on 10% sodium dodecyl sulphate–polyacrylamide gel electrophoresis (SDS-PAGE) and then transferred to polyvinylidene fluoride membranes (PVDF) (Millipore, Billerica, MA) for protein bands detection. The membranes were blocked in 5% nonfat milk. Primary antibodies including anti-GAPDH (1:2000, Abmart, Shanghai, CHN), anti-BCL2 (1:500, Abcam, Cambridge, UK), anti-Caspase 9 (1:1000, Cell Signaling Techonolgy, MA, USA), anti-cleaved-Caspase 9 (1:500, Cell Signaling Techonolgy, MA, USA), anti-Caspase 3 (1:1000, Abcam, Cambridge, UK), and anti-cleaved-Caspase 3 (1:1000, Abcam, Cambridge, UK) were used for incubation overnight at 4 °C. The membranes were incubated with HRP-conjugated secondary antibody (1:3000, Jackson Immuno Research, PA, USA) at room temperature for 1 h and the protein bands were detected by Pierce Fast Western Blot Kit (Thermo Fisher Scientific, MA, USA).

Tian J., Cui P., Li Y., Yao X., Wu X., Wang Z, & Li C. (2020). LINC02418 promotes colon cancer progression by suppressing apoptosis via interaction with miR-34b-5p/BCL2 axis. Cancer Cell International, 20, 460.

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Protein Expression Analysis via Western Blot

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Cells were disrupted by lysis buffer and protein content was determined using the BCA Protein Assay Kit. The quantified protein samples were then separated by SDS-PAGE and transferred to PVDF membranes, followed by sealing with 5% skim milk for 1 hour at room temperature. The PVDF membranes carrying the samples were incubated with primary antibodies overnight at 4°C, and then with secondary antibody for 2 h at room temperature. The signal was displayed with an enhanced chemiluminescence (ECL) kit (Thermo Fisher Scientific, Inc.). And, the protein expression levels were semi-quantified using Image-Pro Plus version 6.0 (Media Cybernetics, Inc.) software. The antibodies used in this study were purchased from Abcam and were used at the following concentrations: anti-Bcl-2 (1:1000), anti-Bax (1:1000), anti-cleaved caspase3 (1:100), anti-caspase3 (1:500), anti-PDE3B (1:2000), anti-p-AMPK (1:1000), anti-AMPK (1:1000), anti-p-mTOR (1:1000), anti-mTOR (1:10,000), anti-GAPDH (1:2500), and goat anti-rabbit IgG H&L (HRP) (1:2000).

Ma L., Zhang C., Wu L., Qin L, & Liu T. (2022). Diosgenin reduces phosphodiesterase 3B (PDE3B) through AMP-activated protein kinase/ mechanistic target of rapamycin (AMPK/mTOR) signaling pathway to ameliorate streptozotocin-induced pancreatic β-cell apoptosis and dysfunction. Bioengineered, 13(2), 2217-2225.

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Apoptosis Protein Expression Analysis

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The proteins were extracted from the cells using RIPA lysis buffer (Thermo Fisher Scientific, Inc.) and their concentration levels were quantified using a bicinchoninic acid protein assay kit (Beyotime Institute of Biotechnology). The proteins (40 µg per lane) were separated by SDS-PAGE on 10% gels, and were transferred onto 0.45 µm PVDF membranes (Thermo Fisher Scientific, Inc.). Following blocking with 5% non-fat milk at room temperature for 1 h, the membranes were incubated with primary antibodies overnight at 4°C. The following primary antibodies were used: Anti-Bax (Abcam; cat. no. ab32503; 1:1,000), anti-Bcl-2 (Abcam; cat. no. ab32124; 1:1,000), anti-cleaved caspase 3 (Abcam; cat. no. ab2302; 1:1,000), anti-cytochrome c (Cyto C; Abcam; cat. no. ab13575; 1:1,000), anti-apoptotic protease activating factor-1 (Apaf 1; Abcam; cat. no. ab2001; 1:1,000), anti-cleaved caspase 9 (Abcam; cat. no. ab2324; 1:1,000) and anti-β-actin (Abcam; cat. no. ab8227; 1:1,000). Subsequently, the membranes were incubated with horseradish peroxidase-conjugated secondary antibody (Abcam; cat. no. ab150077; 1:200) for 1 h at room temperature. Finally, an image of the protein band was detected using ECL reagent (Santa Cruz Biotechnology, Inc.). Image-Pro Plus software (version 7, Media Cybernetics, Inc.) was used for the targets that were normalized to β-actin.

Wang W., Wang J., Zhang J., Taq W, & Zhang Z. (2019). miR-222 induces apoptosis in human intervertebral disc nucleus pulposus cells by targeting Bcl-2. Molecular Medicine Reports, 20(6), 4875-4882.

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Western Blot Analysis of PDGFRA, BCL-2, and Caspase-3

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Cells were collected 48 h after transfection and prepared for lysis in radioimmunoprecipitation assay buffer (BioVision, Inc.). Protein concentration was determined via a bicinchoninic acid assay. Protein (50 µg/lane) was separated via 8% SDS-PAGE. Separated proteins were transferred to polyvinylidene fluoride membranes (EMD Millipore). The membranes were blocked with 5% fat-free milk powder for 2 h at room temperature, and then incubated with primary antibodies against PDGFRA (1:1,000; Santa Cruz Biotechnology, Inc., cat. no. sc-338), anti-BCL-2 (1:1,000; Abcam, cat. no. ab59348), anti-Caspase-3 (1:500; Abcam, cat. no. ab13847) and β-actin antibody (1:1,000; Santa Cruz Biotechnology, Inc., cat. no. sc-47778) at 4°C overnight. Subsequently, the membranes were incubated with horseradish peroxidase-conjugated antimouse IgG (H+L) (1:10,000; Invitrogen; Thermo Fisher Scientific, Inc., cat. no. 62-6520) or anti-rabbit IgG (1:5,000; Invitrogen; Thermo Fisher Scientific, Inc., cat. no. 65-6122) antibody for 1 h at room temperature. The membranes were developed utilizing an ECL kit (Pierce; Thermo Fisher Scientific, Inc.) and visualized with X-ray film. Protein expression levels were standardized to those of β-actin. Data was analyzed by Quantity One version 4.62 software (Bio-Rad Laboratories, Inc.).

Yang X, & Guo F. (2019). miR-342-3p suppresses cell migration and invasion in preeclampsia by targeting platelet-derived growth factor receptor α. Molecular Medicine Reports, 20(2), 1772-1780.

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Comprehensive Protein Expression Profiling of Extracellular Vesicles

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Protein extracts were boiled in RIPA buffer (Beyotime) and separated by sodium dodecyl sulfate–polyacrylamide electrophoresis gel electrophoresis (SDS‐PAGE). The proteins were then transferred to polyvinylidene fluoride membranes (Millipore) and probed with anti‐CD9, anti‐CD63, anti‐ALIX, anti‐TSG101, anti‐EGFR, anti‐FXR1, anti‐TLR‐4, anti‐MMP2, anti‐TGF‐β1, anti‐phospho‐STAT5, anti‐STAT5, anti‐phospho‐ERK1/2, anti‐ERK1/2, anti‐phospho‐AKT, anti‐AKT, anti‐Ki‐67, anti‐PTEN (Abcam), anti‐Bcl‐2, anti‐Bax, anti‐E‐Cadherin, anti‐Vimentin, and anti‐GAPDH antibodies (Cell Signaling Technology). Electrochemiluminescence (Millipore) was applied to determine protein expression levels.

Li F., Zhao X., Sun R., Ou J., Huang J., Yang N., Xu T., Li J., He X., Li C., Yang M, & Zhang Q. (2020). EGFR‐rich extracellular vesicles derived from highly metastatic nasopharyngeal carcinoma cells accelerate tumour metastasis through PI3K/AKT pathway‐suppressed ROS. Journal of Extracellular Vesicles, 10(1), e12003.

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Apoptotic Effects of AEE Crystal

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AEE transparent crystal with the purity of 99.5% by RE-HPLC was prepared in Lanzhou Institute of Husbandry and Pharmaceutical Sciences of CAAS. H₂O₂ solution (cat number: 323381), dimethyl sulfoxide (DMSO), reactive oxygen species assay kit, and trypsin-EDTA were supplied by Sigma (St. Louis, MO). Cell Counting Kit-8 (CCK-8) was from MedChemExpress (NJ, USA), DMEM/F12 (1 : 1), and fetal bovine serum was from Gibco (NY, USA). LysoTracker Red probe, Hoechst 33342 staining solution, cellular glutathione peroxidase assay kit, Cu/Zn-SOD and Mn-SOD assay kit, and mitochondrial membrane potential assay kit were purchased from Beyotime (Shanghai, China). MitoTracker Red CMXRos probe was from Thermo Scientific (MA, USA). Anti-Bid cleavage site, Anti-Bax, Anti-Bcl2, Anti-Bcl-XL, anti-Caspase3 (Cas3), anti-cytochrome C, and anti-Cathepsin D (CTSD) were purchased from Abcam (MA, USA) and the CTSD activity assay kit was from BioVision (CA, USA). An Annexin V/FITC apoptosis detection kit was from BD Biosciences (NY, USA). A Caspase-3 activity assay kit was from Cell Signaling Technology (MA, USA).

Huang M.Z., Yang Y.J., Liu X.W., Qin Z, & Li J.Y. (2019). Aspirin Eugenol Ester Reduces H2O2-Induced Oxidative Stress of HUVECs via Mitochondria-Lysosome Axis. Oxidative Medicine and Cellular Longevity, 2019, 8098135.

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