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Mouse anti cyclin b1

Manufactured by Santa Cruz Biotechnology
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Sourced in United States, United Kingdom

Mouse anti-cyclin B1 is a laboratory reagent used for the detection and quantification of cyclin B1 protein in biological samples. Cyclin B1 is a key regulator of the cell cycle and plays a crucial role in the transition from G2 phase to mitosis. This product provides a specific and reliable tool for researchers studying cell cycle regulation and related biological processes.

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Lab products found in correlation

Mouse anti cyclin a, by Santa Cruz Biotechnology (2 mentions) Rabbit anti erk1 2, by Cell Signaling Technology (1 mentions) Mouse anti gapdh, by Santa Cruz Biotechnology (1 mentions) Bradford assay, by Thermo Fisher Scientific (1 mentions) Ripa buffer, by Santa Cruz Biotechnology (1 mentions) Mouse anti yap1, by Santa Cruz Biotechnology (1 mentions) Rabbit anti c myc, by Cell Signaling Technology (1 mentions) Rabbit anti src, by Cell Signaling Technology (1 mentions) Rabbit anti phospho histone h3 ser10, by Merck Group (1 mentions) Anti γh2ax, by Merck Group (1 mentions) Anti actin, by Santa Cruz Biotechnology (1 mentions) Mouse anti tubulin, by Merck Group (1 mentions) Mouse anti gfp antibody, by Roche (1 mentions) Rabbit anti mouse igg, by Jackson ImmunoResearch (1 mentions) Alexa fluor 546 conjugated secondary antibody, by Thermo Fisher Scientific (1 mentions) Lipofectamine, by Thermo Fisher Scientific (1 mentions) Nocodazole, by Merck Group (1 mentions) Ro 3306, by Enzo Life Sciences (1 mentions) Mouse anti β actin antibody, by Merck Group (1 mentions) Mouse anti t7 antibody, by Merck Group (1 mentions)

Spelling variants of this product

Cyclin B1 (162 citations) Anti-cyclin B1 (69 citations) Mouse monoclonal anti-cyclin B1 (3 citations)

8 protocols using mouse anti cyclin b1

1

Western Blot Analysis of Metabolic Enzymes

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Mouse tissues were homogenized and lysed by using RIPA buffer (Santa Cruz Biotechnology). Protein contents were measured by using the Bradford assay (Pierce Biotechnology). Detailed steps for western blot analysis were as previously described59 (link). The primary antibodies included goat anti-KYNU, rabbit anti-KMO, mouse anti-KAT1, mouse anti-Cyclin B1, mouse anti-GAPDH (all above antibodies from Santa Cruz Biotechnology); mouse anti-YAP1, mouse anti-phospho-YAP (ser 127), rabbit anti-Erk1/2 (Thr202/Tyr204), rabbit anti-Erk1/2, rabbit anti-c-Myc, rabbit anti-phospho-Src (Tyr527) and rabbit anti-Src (all seven antibodies from Cell Signaling). The relative protein levels were calculated by normalizing to GAPDH protein as a loading reference by using ImageJ.
Zhang D., Ning J., Ramprasath T., Yu C., Zheng X., Song P., Xie Z, & Zou M.H. (2022). Kynurenine promotes neonatal heart regeneration by stimulating cardiomyocyte proliferation and cardiac angiogenesis. Nature Communications, 13, 6371.
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2

Cdc5L Regulation of Cell Cycle

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Cdc5L insert was subcloned into pcDNA3.0-Flag vector. Site-directed mutagenesis was done by standard methods. Mouse anti-Cyclin B1 (1 : 1000) and anti-Actin (1 : 2000) were from Santa Cruz Biotechnology (Santa Cruz, CA, USA); rabbit polyclonal antibody against SPF27 (1 : 1000) and anti-Prp19 (1 : 1000) were from Abcam (Cambridge, UK); mouse anti-Tubulin (1:5,000), rabbit anti-Bub1were from Sigma (St. Louis, MA, USA); mouse anti-Cdc5L (1 : 1000) was from BD Biosciences (San Jose, CA, USA); rabbit anti-PARP, anti-cleaved-Caspase3 were from Cell Signaling Technology (Danvers, MA, USA); rabbit anti-PLRG1 (1 : 1000), rabbit anti-BubR1 were from Bethyl Laboratories Inc. (Montgomery, AL, USA); rabbit anti-phospho-histone H3 (Ser 10; 1 : 5000) and anti-γH2AX (1 : 100) were from Merck-Millipore (Boston, MA, USA); human anti-ACA (1 : 100) was from antibodies (Antibodies Inc., Davis, CA, USA); human anti-DYNC1H1 was from Proteintech (Chicago, IL, USA; 1 : 100).
Mu R., Wang Y.B., Wu M., Yang Y., Song W., Li T., Zhang W.N., Tan B., Li A.L., Wang N., Xia Q., Gong W.L., Wang C.G., Zhou T., Guo N., Sang Z.H, & Li H.Y. (2014). Depletion of pre-mRNA splicing factor Cdc5L inhibits mitotic progression and triggers mitotic catastrophe. Cell Death & Disease, 5(3), e1151-.
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3

Antibody Generation and Reagent Sourcing

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The rabbit polyclonal antibodies specific to ADD1 pS12 and pS355 were generated using synthesized peptides C-SRAAVVTpSP and C-KSRpSPGSPVGE, respectively, as antigens (GeneTex, Inc.). The rabbit anti-ADD1 (H-100), mouse anti–β-tubulin (D-10), mouse anti–cyclin B1, and mouse anti-Myo10 (C-1) antibodies were purchased from Santa Cruz Biotechnology, Inc. The mouse anti-FLAG (M2), rabbit anti-FLAG, mouse anti–α-tubulin (DM1A), mouse anti-GFP (B-2), mouse anti–β-actin antibodies, and nocodazole were purchased from Sigma-Aldrich. The mouse anti-T7 antibody was purchased from EMD Millipore. The mouse anti-GFP antibody and X-tremeGENE HP were purchased from Roche. The HRP-conjugated goat anti–rabbit or goat anti–mouse antibodies and rabbit anti–mouse IgG were purchased from Jackson ImmunoResearch Laboratories, Inc. Alexa Fluor 488– and Alexa Fluor 546–conjugated secondary antibodies and Lipofectamine were purchased from Invitrogen. The CDK1 inhibitor RO-3306 was purchased from Enzo Life Sciences. Purified CDK1/cyclin B1 was purchased from EMD Millipore.
Chan P.C., Hsu R.Y., Liu C.W., Lai C.C, & Chen H.C. (2014). Adducin-1 is essential for mitotic spindle assembly through its interaction with myosin-X. The Journal of Cell Biology, 204(1), 19-28.
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4

Immunoblotting Analysis of Cellular Proteins

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The proteins were separated with gel electrophoresis, using Novex Bis-Tris 4–12% gels, MES buffer, NuPAGE LDS loading buffer and NuPAGE reducing agent according to the manufacturer's recommendations (ThermoFisher). The proteins were then transferred to a PVDF membrane using a Trans-Blot Turbo system (1.3 A, 25 V for 7 min) and the RTA lf-PVDF kit (Bio-Rad) according to the manufacturer's instructions. Antibody incubations were performed with Super Signal West Femto Rabbit or Mouse kit (ThermoFisher) along with primary antibody incubations overnight: rabbit anti-Atox1 (1 μg/mL, Abcam), mouse anti-GADPH (2 μg/mL, Abcam), mouse anti-cyclin B1 (1 μg/mL, Santa Cruz) or mouse anti-cyclin A (1 μg/mL, Santa Cruz), and detected with ChemiDoc MP (Bio-Rad) using high sensitivity chemiluminescence detection.
Matson Dzebo M., Blockhuys S., Valenzuela S., Celauro E., Esbjörner E.K, & Wittung-Stafshede P. (2018). Copper Chaperone Atox1 Interacts with Cell Cycle Proteins. Computational and Structural Biotechnology Journal, 16, 443-449.
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5

Comprehensive Western Blot Antibody Panel

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Western blot detection was done as described previously [7 (link)]. The following antibodies were used: rabbit anti-RAE1 (Sigma, 1:2000), mouse anti-beta tubulin (Sigma, 1:2000), mouse anti-Flag horse radish peroxidase (HRP) conjugated antibody (Sigma, 1:5000), rabbit anti-SPRYD3 (Abcam, 1:2000), rabbit anti-CIT (CT295, 1:1000)[59 (link)] (kindly provided by Prof Kennedy of the California Institute of Technology), rabbit anti-PAM (Bethyl Laboratories A301-833A, 1:2000), rabbit anti-KCTD6 (Sigma), rabbit anti-USP11 [7 (link)] (1:2000), mouse anti-beta actin HRP (Abcam, 1:20000), mouse anti-hemagglutinin (HA) clone 16B12 (Covance, 1:2000), rabbit anti-HA (Sigma, 1:1000), mouse anti-securin (Novus Biologicals, 1:500), mouse anti-cyclin B1 (Santa Cruz Biotechnology, 1:2000), rabbit anti-APC3 (Cell Signalling Technologies, 1:1000), rabbit anti-NuMA (Cell Signalling Technologies, 1:1000), mouse anti-HDAC6 (Insight Biotechnology Ltd, 1:200), mouse anti-DYNEIN (Santa Cruz Biotechnology, 1:100), mouse anti-CENP-E (Insight Biotechnology Ltd, 1:200), rabbit anti-Plk1 (Bethyl Laboratories). Donkey anti-rabbit and sheep anti-mouse HRP conjugated antibodies (GE Healthcare) were used at a 1:2000 dilution. For the detection of NuMA and the ubiquitination of endogenous RAE1, Clarity Max ECL substrate was used, all other western blots were detected with Clarity ECL substrate (Bio-Rad).
Stockum A., Snijders A.P, & Maertens G.N. (2018). USP11 deubiquitinates RAE1 and plays a key role in bipolar spindle formation. PLoS ONE, 13(1), e0190513.
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6

Comprehensive Antibody Panel for Cell Cycle

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Antibodies against the following proteins were used: goat anti-actin (Santa Cruz sc-1616), mouse anti-α-Tubulin (Sigma T5168), ANA-Centromere CREST AutoAb Human (Fitzgerald 90C-CS1058), mouse anti-APC3 (BD Transduction #610455), rabbit anti-astrin (Bethyl Laboratories A301-512A), mouse anti-Cdk1 (BD Transduction 610038), rabbit anti-Cdk2 (Santa Cruz sc-163), rabbit anti-CENP-E (Sigma C7488), rabbit anti-cleaved PARP (Cell Signaling #5625S), mouse anti-cyclin B1 (Santa Cruz sc-245), rabbit anti-cyclin B2 (Santa Cruz sc-22776), rabbit anti-KIF4 (Bethyl Laboratories A301-074A), rabbit anti-Mad2 (Bethyl Laboratories A300-301A), goat anti-phospho-PRC1 Thr481 (Santa Cruz sc-11768), mouse anti-PRC1 (BioLegend 629002), rabbit anti-PRC1 (Santa Cruz sc-8356). Secondary peroxidase-conjugated antibodies were obtained from DAKO and ALEXA fluorescently-labelled secondary antibodies were purchased from Molecular Probes.
Voets E., Marsman J., Demmers J., Beijersbergen R, & Wolthuis R. (2015). The lethal response to Cdk1 inhibition depends on sister chromatid alignment errors generated by KIF4 and isoform 1 of PRC1. Scientific Reports, 5, 14798.
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7

Antibody Generation and Characterization

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Rabbit anti-human SUN1 (Atlas) and mouse monoclonal β-actin antibodies were obtained from Sigma. Mouse anti-Myc antibody was purchased from Zymed Laboratories Inc Mouse anti-cyclin B1, mouse anti-cyclin A and goat anti-lamin A/C (6215) antibodies were purchased from Santa Cruz Biotechnologies. Rabbit anti-GFP antibody was obtained from Abcam. Rabbit anti-emerin antibody was kindly provided by G. Morris (Center for Inherited Neuromuscular Disease, Oswestry, UK). Anti-human SUN1 2383 has been reported previously.27 (link)
SUN1 serine 48 (pS48) phospho-antibodies were generated by immunization of rabbits with a peptide corresponding to residues 42–55 of human SUN1, phosphorylated at serine 48. Immunizations and antibody purification, using peptide columns, were performed by Eurogentec.
Patel J.T., Bottrill A., Prosser S.L., Jayaraman S., Straatman K., Fry A.M, & Shackleton S. (2014). Mitotic phosphorylation of SUN1 loosens its connection with the nuclear lamina while the LINC complex remains intact. Nucleus, 5(5), 462-473.
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8

Western Blot Analysis of Cell Cycle Proteins

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The 30 μg of lysate was initially denatured in 4 × Loading Buffer (40% glycerol, 240 mM Tris-HCl pH 6.8, 8% SDS, 0.04% bromophenol blue, 5% β-mercaptoethanol) at 96°C for 5 min and separated on 8%, 10% or 12% SDS-polyacrylamide gels and transferred to nitrocellulose membranes (Whatman Protran BA 83; 0.2 µm pores) and blocked with 4% skimmed milk in a TBS-Tween buffer (TBST) for 20 min. Primary antibodies in this study are as follows: mouse anti-cyclin A (Novocastra, UK), mouse anti-cyclin B1 (Santa Cruz Biotechnology, USA), rabbit anti-cyclin D1 (Santa Cruz Biotechnology, USA), mouse anti-cyclin E1 (Santa Cruz Biotechnology, USA), mouse anti-p53 DO1 (Santa Cruz Biotechnology, USA). After incubation with appropriate horseradish peroxidaseconjugated secondary antibody, proteins were visualized by using Western Lightning Plus-ECL Enhanced Chemiluminiscence Substrate (Perkin Elmer, USA). Western blots were imaged using an Alliance 4.7 imaging system (UVitec, UK).
Hanžić N., Horvat A., Bibić J., Unfried K., Jurkin T., Dražić G., Marijanović I., Slade N, & Gotić M. (2018). Syntheses of gold nanoparticles and their impact on the cell cycle in breast cancer cells subjected to megavoltage X-ray irradiation. Materials science & engineering. C, Materials for biological applications, 91.
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