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> Chemicals & Drugs > Amino Acid > Cyclin B1

Cyclin B1

Cyclin B1: A key regulator of cell division, essential for progression through the G2/M phase of the cell cycle.
Cyclin B1 forms a complex with the serine/threonine-protein kinase CDK1, activating it and driving the cell into mitosis.
Understanding the mechanisms and dynamics of Cyclin B1 is crucial for research into cell cycle control, cancer, and regenerative medicine.
Optimize your Cyclin B1 protocols and enhance reproducibility with PubCompare.ai's AI-powered platform, which helps you find the most effective methods and products from the literature, preprints, and patents.

Most cited protocols related to «Cyclin B1»

1
Quantifying Cell Cycle Protein Levels
Cells were grown on Histogrip (Invitrogen) coated glass coverslips and fixed using ice-cold 100% methanol (β-tubulin) or with 3.7% formaldehyde diluted in PBS with 0.5% Triton X-100 for 10 min (Mad2, pSerCdk, Lamin A/C, Plk1, cyclin B1, and securin). All cells were washed and then blocked (3% BSA, 0,1% Tween 20 in PBS) for 30 min. Cells were incubated with primary antibodies were incubated for 2 h at room temperature in blocking solution. DNA was stained with DAPI. For Lamin A/C staining a Leica DM6000 SP8 confocal with a 63× lens was used. All other images were captured using Leica DM5500 microscope coupled with a Coolsnap HQ2 camera, using a Leica 100× or 40× APO 1.4 lens, powered by Leica LAS AF v3 software. To quantify pSer-CDK, cyclin B and secruin levels in cells, a single in-focus plane was acquired. Using ImageJ (v1.48, NIH), an outline was drawn around each cell and circularity, area, mean fluorescence measured, along with several adjacent background readings. The total corrected cellular fluorescence (TCCF) = integrated density – (area of selected cell × mean fluorescence of background readings), was calculated. This TCCF was then equalized against the mean TCCF of neighboring interphase cells in the same field of view, with results presented as fold increase over interphase levels. Box plots and statistical analysis (2-sided unpaired Student t tests) were performed using GraphPad Prism 5. For all other images, 0.3 µm z-sections were taken, de-convolved, and displayed as 2D maximum projections using ImageJ. False coloring and overlays were performed using Adobe Photoshop CS5 software.
McCloy R.A., Rogers S., Caldon C.E., Lorca T., Castro A, & Burgess A. (2014). Partial inhibition of Cdk1 in G2 phase overrides the SAC and decouples mitotic events. Cell Cycle, 13(9), 1400-1412.
Publication 2014
Antibodies Cells Cold Temperature Cyclin B Cyclin B1 DAPI Fluorescence Formaldehyde Interphase Lens, Crystalline LMNA protein, human Methanol Microscopy PLK1 protein, human prisma PTTG1 protein, human Student Triton X-100 Tubulin Tween 20
2
Protein Expression Analysis of Tumor Subtypes

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Publication 2018
4-carboxyphenylglyoxal ASNS protein, human beta-Catenin Brain Neoplasm, Malignant Breast Cadherins Caspase-7 CCNE1 protein, human CDKN2A Gene Chronic Obstructive Airway Disease Claudins Cyclin B1 DPP4 protein, human Estrogen Receptor alpha FASN protein, human GAPDH protein, human Gastric Cancer IGFBP-2 protein, human Kidney Liver Malignant Neoplasms Mesenchyma Mitogen Activated Protein Kinase 1 Neoplasms Phenobarbital Phosphoproteins PRKCA protein, human Protein Arrays Proteins SERPINE1 protein, human TFRC protein, human Tubulin
3
Measuring Cyclin B1-GFP Degradation and Mitotic Markers
To measure the fluorescent cyclin B1-GFP degradation in living cells, time-lapse images were collected at 1-min intervals. The region was drawn around each cell to be measured, and the identical region was placed in an area without fluorescent objects to be used for background subtraction. The net average fluorescence intensity of a pixel in the region of interest was calculated for each time point. Because cells expressed different levels of fluorescent cyclin B, the net average intensity values were normalized to the initial (first time point) value that was designated as 1. Averages of normalized intensity values of at least five identically treated cells were calculated for each time point and plotted on a graph. For these experiments, all parameters during image acquisition were the same.
To measure fluorescence intensities of MPM2, pS-Cdk, and pNucleolin antibody labeling, 1-μm Z-stacks through cells of different stages of mitosis were acquired. A region was drawn around each cell to be measured, and the same size region was drawn in an area without fluorescent objects to be used for background subtraction. The net integrated intensity for each cell was measured at a single Z plane with highest integrated intensity values in the region of interest (this was usually the plane with the best focus). The weak signal from interphase cells was designated as 1, and the fluorescence intensity values at each mitotic stage were normalized and plotted relative to interphase. Each bar represents an average of 15–30 cells. The intensity of a signal from the control slide labeled with secondary antibodies alone was comparable to the intensity of the background in experimental samples.
Potapova T.A., Sivakumar S., Flynn J.N., Li R, & Gorbsky G.J. (2011). Mitotic progression becomes irreversible in prometaphase and collapses when Wee1 and Cdc25 are inhibited. Molecular Biology of the Cell, 22(8), 1191-1206.
Publication 2011
Antibodies Cells Cyclin B Cyclin B1 Debility Division Phase, Cell Fluorescence Immunoglobulins Interphase Signal Transduction
4
Western Blot Analysis of Cell Cycle Regulators

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Publication 2007
ABCB1 protein, human Actins Antibodies Apoptosis Caspase-7 Caspase 3 CDK1 protein, human CDK2 protein, human Cell Fractionation Cyclin A Cyclin B1 Cyclin D1 Cyclin E Densitometry Mus Peroxidase Proteins Rabbits Technique, Dilution
5
Quantitative Microscopy of Mitotic Regulators
Immunofluorescence, immunoblotting, and immunoprecipitations were all done as described previously (Taylor et al., 2001 (link)) using antibodies against the following: phosphohistone H3 (Upstate Biotechnology); cyclin B1 (Upstate Biotechnology); tubulin (TAT1); centromere/kinetochores (human ACA); BubR1 (SBR1.1); Bub1 (4B12); Aurora A (RAA.1); and Myc-tag (9E10). Aurora B was detected using either the anti-AIM-1 mouse mAb (Transduction Laboratories) or a sheep anti–human Aurora B pAb (unpublished data). For localization of Mad2 and Survivin, we used DLD-1 cell lines stably expressing Myc-tagged hMad2 or hSurvivin ORFs (unpublished data). For IP kinase assays, beads were equilibrated in kinase buffer (10 mM Tris, pH7.5, 5 mM KCl, 1 mM NaF, 0.24 mM DTT, and 2.5 mM MnCl) and were then incubated at RT for 1 h in kinase buffer supplemented with 2.5 μM ATP, 5 μCi γ[32P]ATP, and 3 μM biotinyl-Ahx-tetra (LRRWSLG) peptide substrate. Reactions were stopped with 20% phosphoric acid, and were then spotted onto P30 filtermat (Whatman). After five washes in 0.5% phosphoric acid, bound radiolabel was quantitated by scintillation counting. Deconvolution microscopy and pixel intensity quantitation were performed as described previously (Taylor et al., 2001 (link)). In brief, kinetochore fluorescence values were determined using softWoRx imaging software (Applied Precision). Background readings were subtracted, and the values were then normalized against the ACA signal to account for any variations in staining or image acquisition. SoftWoRx was used to measure interkinetochore distances using either ACA or Bub1 foci as indicated to determine kinetochore position.
Ditchfield C., Johnson V.L., Tighe A., Ellston R., Haworth C., Johnson T., Mortlock A., Keen N, & Taylor S.S. (2003). Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores. The Journal of Cell Biology, 161(2), 267-280.
Publication 2003
Antibodies AURKA protein, human AURKB protein, human Biological Assay BUB1 protein, human Buffers Cell Lines Centromere Cyclin B1 Domestic Sheep Fluorescence Homo sapiens Immunofluorescence Immunoprecipitation Kinetochores Microscopy Mus Open Reading Frames Peptides Phosphoric Acids Phosphotransferases Survivin Tetragonopterus Tromethamine Tubulin

Most recents protocols related to «Cyclin B1»

1
Western Blotting Analysis of ABC Transporters
Western Blotting analysis was performed as previously described (25 (link)) in both HGC27-S/R and KATOIII-S/R. Briefly, for each experimental condition the cells were lysed in ice-cold lysis buffer (50 mM Tris, 10 mM EDTA, 1% v/v Triton-X100), supplemented with the protease/phosphatase inhibitor cocktail set (Merck KGaA, Darmstadt, Germany), incubated on ice for 15 minutes and centrifuged at 13,000 × g for 15 min at 4°C. Separate cytoplasmic and nuclear protein fractions were obtained using the NE-PER Nuclear and Cytoplasmic Extraction Kit (Thermo Fisher Scientific Inc., MA USA) following the manufacturing procedures. Protein extracts were quantified by Micro BCA™ Protein Assay Kit (Thermo Fisher Scientific Inc., MA USA) and 40 μg of total protein extract or nuclear/cytoplasmic fraction were subjected to SDS-PAGE and immunoblotted with the following antibodies: P-gp (1:250, rabbit polyclonal, Santa Cruz Biotechnology Inc., Santa Cruz, CA), MRP1 (1:500, mouse clone MRPm5, Abcam, Cambridge, UK), BCRP (1:500, mouse clone BXP-21, Santa Cruz Biotechnology Inc.), Phospho-βcatenin (Ser675) and βcatenin (1:1000 Cell Signaling, Beverly, MA, USA), NFkB (1:1000, Santa Cruz Biotechnology Inc.), Phospho-cyclin B1 (Ser147) and cyclin B1 (1:1000 Cell Signaling, Beverly, MA, USA), Beta III Tubulin (TUBβIII 1:2000 Abcam, Cambridge, UK), Phospho-c-Myc (Ser62) and c-Myc (1:1000 Cell Signaling, Beverly, MA, USA), Phospho-SAPK/JNK (Thr183/Tyr185) and JNK2 (1:1000 Cell Signaling, Beverly, MA, USA), Phospho-c-Jun (Ser63) and c-Jun (1:1000 Cell Signaling, Beverly, MA, USA), caspase 3/7 (1:1000 Cell Signaling, Beverly, MA, USA), VEGF Receptor 2 (VEGFR2 1:500, Santa Cruz Biotechnology Inc., Santa Cruz, CA) VEGF receptor 3 (VEGFR3 1:200, Abcam, Cambridge, UK), Angiopoietin 2 (Ang 2 1:500, R&D Systems, Minneapolis, MN, USA), VEGFA (Abcam, Cambridge, UK), Fibronectin1 (FN1 1:400; Invitrogen), ALIX (1:1000; Abcam, Cambridge, UK), CD81 (1:500; Invitrogen) and GAPDH (1:1000 Abcam, Cambridge, UK). Subsequently, the membranes were incubated with the corresponding horseradish peroxidase (HRP)-conjugated secondary antibodies (Bio-Rad, Hercules, CA, USA). An enhanced chemiluminescence kit (Bio-Rad, Hercules, CA, USA) was used. A Chemidoc XRS+ and the Bio-rad software (Bio-Rad, Hercules, CA, USA) was used to observe and analyze the chemiluminescence signals from proteins. Nuclear protein extracts have been normalized using stain free technology, using Image Lab Software (Bio-Rad, Hercules, CA, USA). Total protein expression was quantified using the ImageJ software (http://rsb.info.nih.gov/ij/).
Schirizzi A., Contino M., Carrieri L., Riganti C., De Leonardis G., Scavo M.P., Perrone M.G., Miciaccia M., Kopecka J., Refolo M.G., Lotesoriere C., Depalo N., Rizzi F., Giannelli G., Messa C, & D’Alessandro R. (2023). The multiple combination of Paclitaxel, Ramucirumab and Elacridar reverses the paclitaxel-mediated resistance in gastric cancer cell lines. Frontiers in Oncology, 13, 1129832.
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Publication 2023
Angiopoietin-2 ANGPT1 protein, human Antibodies beta-Tubulin Biological Assay Buffers Caspase-7 CD9 protein, human Cells Chemiluminescence Clone Cells Cold Temperature Cyclin B1 Cytoplasm Edetic Acid GAPDH protein, human Horseradish Peroxidase jun Oncogenes Mus NF-kappa B Nuclear Protein Oncogenes, myc Phosphoric Monoester Hydrolases Protease Inhibitors Proteins Rabbits SDS-PAGE Stains Tissue, Membrane Training Programs Triton X-100 Tromethamine Vascular Endothelial Growth Factor Receptor-2 vegfr3 protein, human Western Blot
2
Western Blot Analysis of Cell Signaling
Western blot analysis was performed as previously described 20 (link). Antibodies against FoxM1, survivin, XIAP, Cyclin B1, phospho-Cdc25c, Bax, Bcl-2, cleaved PARP, and cleaved caspase 3 were purchased from Cell Signaling Technology (Danvers, MA, USA), and antibodies against Ki67 and GAPDH were purchased from Santa Cruz Biotechnology (Dallas, TX, USA). The antibody against phospho-histone H2AX, Ser139 (γ-H2AX) was purchased from EMD Millipore (MA, USA).
Qin Q., Chen H., Xu H., Zhang X., Chen J., Zhang C., Liu J., Xu L, & Sun X. (2023). FoxM1 knockdown enhanced radiosensitivity of esophageal cancer by inducing apoptosis. Journal of Cancer, 14(3), 454-463.
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Publication 2023
Antibodies BCL2 protein, human Caspase 3 CDC25C protein, human Cyclin B1 GAPDH protein, human H2AX protein, human Immunoglobulins Survivin Western Blot
3
Western Blot Analysis of Protein Signaling
Cells were seeded into 100 mm Petri dishes at 1 × 106 cells/plate. The samples were treated with 3a at 5 and 10 μM for 24 or 48 h. Cellular homogenate was obtained using RIPA lysis buffer with protease and phosphatase inhibitors (Sigma, #P8340). After centrifugation (10,000× g for 10 min at 4 °C), supernatants were collected, and quantification of total proteins was determined using BCA kit (Pierce Biotechnology Inc., Waltham, MA, USA). 50 μg of total protein was separated by SDS–PAGE (12%) and transferred (100 V, 250 mA for 2 h) onto a PVDF membrane (Amersham Bioscience, Amersham, UK). After membrane blocking (5% non-fat milk in Tris-buffered saline + 0.1% Tween20) (1 h at 4 °C), it was probed with primary antibodies: anti-phospho-ERK(Tyr 204) (Santa-Cruz, sc-7383, 1:200), anti-ERK 1/2 (Cell signaling, #4696, 1:1000), anti-Cyclin B1 (Santa Cruz, sc-245, 1:200), anti-AKT(Ser 473) (Cell signaling, #4060), and α-tubulin (Sigma–1:1000) overnight at 4 °C. After washing, the membrane was incubated with an appropriate secondary antibody—HRP conjugated for 2h at room temperature. Immunoreactive bands were revealed by ECL Western blotting Detection Kit (Amersham Bioscience), and quantified by ImageJ [73 (link)].
Pressete C.G., Viegas F.P., Campos T.G., Caixeta E.S., Hanemann J.A., Ferreira-Silva G.Á., Zavan B., Aissa A.F., Miyazawa M., Viegas-Jr C, & Ionta M. (2023). Piperine–Chlorogenic Acid Hybrid Inhibits the Proliferation of the SK-MEL-147 Melanoma Cells by Modulating Mitotic Kinases. Pharmaceuticals, 16(2), 145.
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Publication 2023
alpha-Tubulin Antibodies Buffers Cells Centrifugation Cyclin B1 Cyclins Hyperostosis, Diffuse Idiopathic Skeletal Immunoglobulins inhibitors iodine-131-tositumomab Milk, Cow's Mitogen Activated Protein Kinase 1 Peptide Hydrolases Phosphoric Monoester Hydrolases polyvinylidene fluoride Proteins Radioimmunoprecipitation Assay Saline Solution SDS-PAGE Tissue, Membrane Tween 20
4
Western Blot Analysis of Cell Signaling
Western blotting was performed as previously described [38 (link),39 (link)]. All cell lysates (50–80 µg) were prepared in an ice-cold lysis buffer. Protein samples were loaded onto 10–12% sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis membranes for electrophoretic separation and then transferred to PVDF membranes (Millipore) at 500 mA for 2 h. After blocking the buffer overnight with 5% non-fat dry milk in PBS containing Tween20 (PBST), the membranes were incubated with primary antibodies [Cyclin B1 (1:1000; Proteintech; 55004-1-AP), CDK1 (1:1000; Cell Signaling; E1Z6R), NRF2 (1:1000; Proteintech; 16396-1-AP), and β-actin (1:20,000; Sigma; A5441)] for 2 h at room temperature or overnight at 4 °C. Membranes were then washed once with PBST and twice with PBS, incubated with the secondary antibody Li-COR (Taipei, Taiwan) at a 1:20,000 dilution for 30–40 min, and washed again. Antigens were visualized using a near-infrared fluorescence imaging system (Odyssey LICOR, USA), and these data were interpreted using Odyssey2.1 software or a chemiluminescence detection kit (ECL; Amersham Corp., Arlington Heights, IL, USA). Densitometry analysis (including the integrated density of bands) was carried out using ImageJ (NIH), followed by normalization of the measured values to β-actin as a loading control.
Tsai T.H., Su Y.F., Tsai C.Y., Wu C.H., Lee K.T, & Hsu Y.C. (2023). RTA dh404 Induces Cell Cycle Arrest, Apoptosis, and Autophagy in Glioblastoma Cells. International Journal of Molecular Sciences, 24(4), 4006.
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Publication 2023
Actins Antibodies Antigens Buffers CDK1 protein, human Cells Chemiluminescence Cold Temperature Cyclin B1 Densitometry Electrophoresis Immunoglobulins Milk, Cow's NFE2L2 protein, human polyvinylidene fluoride Proteins SDS-PAGE Sulfate, Sodium Dodecyl Technique, Dilution Tissue, Membrane Tween 20
5
Western Blot Analysis of Apoptosis Markers
Briefly, AGS cells were extracted and protein concentrations were calculated. Equal amounts of the lysates separated by sodium dodecyl-polyacrylamide gel electrophoresis (SDS-PAGE) were transferred to a polyvinylidene difluoride (PVDF) membrane, and the membrane was then blocked at room temperature with 1× TBS containing 0.1% Tween 20 and 5% skim milk. After blocking, the matched primary antibodies (1:3000) were applied to the membranes, including the following primary antibodies at 4 °C overnight: anti-caspase-3, anti-survivin, anti-heat shock protein (HSP) 27, anti-HSP70, anti-HSP90, anti-caspase-8, anti-caspase-9, anti-p-extracellular signal-regulated kinase (ERK) (Thr202/Tyr204), anti-ERK, anti-p-Jun N-terminal kinase (JNK) (Thr183/Tyr185), anti-JNK, anti-p-p38 (Thr180/Tyr182), anti-p38 (Cell Signaling Technology), anti-β-actin, anti-Bcl-2, anti-Bcl-xL, anti-cyclin D1, anti-vascular endothelial growth factor (VEGF), anti-matrix metallopeptidase (MMP) 9, anti-MMP2, anti-Cyclin B1 (Santa Cruz Biotechnology, Inc.), anti-cleaved caspase (Genetex), anti-heat shock factor 1 (HSF1), and anti-pHSF1 (Abcam, Inc.). After washing three times, membranes were incubated for 1 h at room temperature with diluted anti-rabbit or anti-mouse IgG secondary antibodies (Santa Cruz Biotechnology, Inc., 1:1000). Between each step, the blots were thrice rinsed with 1 TBS-T buffer for 10 min. The membranes were detected using an enhanced chemiluminescence (ECL) kit (Millipore, Billerica, MA, USA).
Ahn C.R., Kim H.I., Kim J.E., Ha I.J., Ahn K.S., Park J., Kim Y.W, & Baek S.H. (2023). Ponciri Fructus Immatarus Sensitizes the Apoptotic Effect of Hyperthermia Treatment in AGS Gastric Cancer Cells through ROS-Dependent HSP Suppression. Biomedicines, 11(2), 405.
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Publication 2023
Actins anti-IgG Antibodies BCL2 protein, human Buffers Caspase Caspase-8 Caspase 3 Caspase 9 Cells Chemiluminescence Cyclin B1 Cyclin D1 Cyclins Extracellular Signal Regulated Kinases Fibrinogen Heat-Shock Proteins 70 Heat-Shock Response HSP90 Heat-Shock Proteins HSPB1 protein, human iodine-131-tositumomab JNK Mitogen-Activated Protein Kinases Matrix Metalloproteinases Milk, Cow's MMP2 protein, human Mus Polyacrylamide Gel Electrophoresis polyvinylidene fluoride Proteins Rabbits Sodium Survivin Tissue, Membrane Tween 20 Vascular Endothelial Growth Factors

Top products related to «Cyclin B1»

1
Cyclin b1 by Cell Signaling Technology
Sourced in United States, United Kingdom, China
Cyclin B1 is a protein that plays a crucial role in the regulation of the cell cycle. It is a key component of the M-phase promoting factor (MPF), which is responsible for driving cells from the G2 phase into the M phase of the cell cycle. Cyclin B1 is expressed during the late G2 and M phases of the cell cycle and is degraded at the end of mitosis.
2
Cyclin b1 by Santa Cruz Biotechnology
Sourced in United States, United Kingdom
Cyclin B1 is a protein involved in the regulation of the cell cycle. It plays a critical role in the transition from the G2 phase to the M phase of the cell cycle. Cyclin B1 forms a complex with the enzyme cyclin-dependent kinase 1 (CDK1), which is necessary for the initiation of mitosis.
3
β actin by Cell Signaling Technology
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β-actin is a cytoskeletal protein that is ubiquitously expressed in eukaryotic cells. It is an important component of the microfilament system and is involved in various cellular processes such as cell motility, structure, and integrity.
4
Cleaved caspase 3 by Cell Signaling Technology
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Cleaved caspase-3 is an antibody that detects the activated form of caspase-3 protein. Caspase-3 is a key enzyme involved in the execution phase of apoptosis, or programmed cell death. The cleaved caspase-3 antibody specifically recognizes the active, cleaved form of the enzyme and can be used to monitor and quantify apoptosis in experimental systems.
5
Anti cyclin b1 by Cell Signaling Technology
Sourced in United States, United Kingdom
Anti-cyclin B1 is a laboratory reagent used in research applications. It is an antibody that specifically binds to the cyclin B1 protein, which is a key regulator of the cell cycle. The core function of Anti-cyclin B1 is to enable the detection and analysis of cyclin B1 expression in cells and tissues.
6
Cyclin d1 by Cell Signaling Technology
Sourced in United States, China, United Kingdom, Germany, Japan
Cyclin D1 is a key regulatory protein involved in cell cycle progression. It plays a crucial role in the G1/S transition phase of the cell cycle. Cyclin D1 functions as a regulatory subunit of cyclin-dependent kinase 4 (CDK4) and cyclin-dependent kinase 6 (CDK6), promoting cell cycle advancement.
7
Caspase 3 by Cell Signaling Technology
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Caspase-3 is a key enzyme involved in the execution phase of cell apoptosis (programmed cell death). It plays a central role in the apoptotic pathway by cleaving various cellular substrates, leading to the characteristic morphological and biochemical changes associated with apoptosis.
8
β actin by Merck Group
Sourced in United States, United Kingdom, Germany, China, Canada, Japan, Macao, Italy, Sao Tome and Principe, Israel, Spain, Denmark, France, Finland, Australia, Morocco, Ireland, Czechia, Sweden, Uruguay, Switzerland, Netherlands, Senegal
β-actin is a protein that is found in all eukaryotic cells and is involved in the structure and function of the cytoskeleton. It is a key component of the actin filaments that make up the cytoskeleton and plays a critical role in cell motility, cell division, and other cellular processes.
9
Gapdh by Cell Signaling Technology
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GAPDH is a protein that functions as an enzyme involved in the glycolysis process, catalyzing the conversion of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate. It is a common reference or housekeeping protein used in various assays and analyses.
10
Bcl 2 by Cell Signaling Technology
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Bcl-2 is a protein that plays a key role in regulating apoptosis, or programmed cell death. It functions as an anti-apoptotic protein, helping to prevent cell death by inhibiting the activity of pro-apoptotic proteins.

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