Ab52901

Manufactured by Abcam

Sourced in United States

Ab52901 is a laboratory equipment product. It is a tool used for scientific research and analysis.

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5 protocols using ab52901

Immunoblotting and Immunohistochemical Analysis of Caveolin-1

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Antibodies used in the study include: rabbit monoclonal anti-β III tubulin for Western blot analysis (Abcam; ab52901; 1/8,000); rabbit monoclonal anti-PHF1 (Abcam; ab184951; 1/5,000); rabbit monoclonal anti-tau (phospho T231) (Abcam; ab151559; 1/5,000); chickenanti-tau (Abcam; ab75714; 1/30000); rabbit monoclonal anti-mTOR (phospho S2448) (Abcam; ab109268; 1/5,000); rabbit anti-mTOR (Cell Signalling; 2983; 1/1,000); rabbit anti-Phospho-S6K (Thr421/Ser424) (Cell Signalling; 9204; 1/1,000); rabbit anti-S6K (Cell Signalling; 9202; 1/1,000); rabbit anti-Cav-1 for western blot analysis (Santa Cruz Biotechnology; sc-894; 1/500); rabbit anti-Cav-1 for immunohistochemical staining (Santa Cruz Biotechnology; sc-894; 1/100); rabbit anti-Cav-1 for immunofluorescence (Santa Cruz Biotechnology; sc-894; 1/50); rabbit monoclonal anti-Synaptophysin (Syn) (Abcam; ab32127; 1/50); rabbit monoclonal anti-β III tubulin for immunofluorescence (Abcam; ab52901; 1/100).
The adenoviral Cav-1 (Ad-Cav-1) and the empty adenovirus vector (Ad-null) were generously gifted from Dr. Duan-Fang Liao (Hunan University of Traditional Chinese Medicine, China).

Wu J., Zhou S.L., Pi L.H., Shi X.J., Ma L.R., Chen Z., Qu M.L., Li X., Nie S.D., Liao D.F., Pei J.J, & Wang S. (2017). High glucose induces formation of tau hyperphosphorylation via Cav-1-mTOR pathway: A potential molecular mechanism for diabetes-induced cognitive dysfunction. Oncotarget, 8(25), 40843-40856.

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Immunoblot Analysis of Stem Cell Markers

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The ENO1 antibody (ab227978), β-Tubulin antibody (ab52901), anti-CD44 antibody (ab157107), SOX2 antibody (ab97959), anti-Nanog antibody (ab80892), and anti-Oct4 antibody (ab18976) were from Abcam.

Yang T., Shu X., Zhang H.W., Sun L.X., Yu L., Liu J., Sun L.C., Yang Z.H, & Ran Y.L. (2020). Enolase 1 regulates stem cell-like properties in gastric cancer cells by stimulating glycolysis. Cell Death & Disease, 11(10), 870.

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Directed Differentiation of Embryoid Bodies

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Cells were chemically harvested by trypsinization and transferred to non-adherent bacteriological culture dishes in ES medium without Leukemia Inhibitory Factor (LIF) until formation of the aggregated cells of embryoid bodies was observed. Total RNA derived from plated embryoid bodies on day 6 was used for RT-PCR analysis for the three germ layer markers. The primers used for each germ layer are listed in Table 4. The cells were stained with anti-smooth muscle actin antibody (ab5694, Abcam, Cambridge, MA, USA), anti-Sox 17 antibody (cs-299, Santa Cruz, Dallas, TX, USA) and anti- βIII tubulin antibody (ab52901, Abcam, Cambridge, MA, USA). This was followed by incubation with the following secondary antibody: Alexa Fluor 488-labeled anti-rabbit IgG (A21206, Invitrogen, Carlsbad, CA, USA) or cy3^® anti-rabbit IgG (A10520, Invitrogen, Carlsbad, CA, USA). Nuclei were counterstained using DAPI (1 mg/mL PBS; Invitrogen, Carlsbad, CA, USA).

El-Sayed A.K., Zhang Z., Zhang L., Liu Z., Abbott L.C., Zhang Y, & Li B. (2014). Pluripotent State Induction in Mouse Embryonic Fibroblast Using mRNAs of Reprogramming Factors. International Journal of Molecular Sciences, 15(12), 21840-21864.

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Quantitative Analysis of Tubulin Isotypes

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The cells were washed twice with Ca/Mg-free PBS and then treated with a microtubule lysing buffer consisting of 100 mM PIPES, 5 mM MgCl₂, 1 mM EGTA, 30% glycerol, 0.1% IGEPAL, 0.1% Tween-20, 0.1% Triton X-100, 0.1% beta-mercaptoethanol, 1 mM ATP, 0.1 mM GTP and a complete protease inhibitor cocktail (Roche); the recipe is according to Cytoskeleton, Inc. (USA). The lysate was homogenized by Retsch Mixer Mill at 25 Hz for 2 min, and incubated for 30 min at 35 °C. The obtained cell lysates were clarified by centrifugation at 21000 x g for 40 min at 35 °C. The protein concentration in lysates was determined using the Pierce BCA Protein Kit. Proteins were separated by 12% SDS-PAGE and transferred onto the PVDF membrane by Trans-Blot Semi-Dry Transfer system (Bio-Rad, Inc., USA).
To determine the presence of beta-tubulin isotypes Abcam mono- and polyclonal antibodies (anti-beta I Tubulin (ab11312), anti-Tubb2A (ab170931) and anti-beta III Tubulin (ab52901) were used. After the chemiluminescence reaction, the PVDF membranes were stained with Coomassie brilliant blue R250 to measure the total protein amount. The tubulin signal intensity was normalized against total protein intensities obtained from Coomassie staining. Quantification was performed by ImageJ software.

Klepinin A., Ounpuu L., Mado K., Truu L., Chekulayev V., Puurand M., Shevchuk I., Tepp K., Planken A, & Kaambre T. (2018). The complexity of mitochondrial outer membrane permeability and VDAC regulation by associated proteins. Journal of Bioenergetics and Biomembranes, 50(5), 339-354.

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Monoclonal Antibodies for Canine Proteins

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Monoclonal anti-JCTdog 5D8 (epitope: residues 156-154) and anti-TRD_dog 8G5 (epitope: residues: 125-132) antibodies, raised towards purified canine JCT and canine TRD [14 (link), 26 (link)], were generated by standard mouse monoclonal technology, and epitopes determined using Pepspot, JTP Peptide. Canine TRD-specific rabbit polyclonal antibodies raised to the C-terminus of canine cardiac TRD were previously described [24 (link)]. Mouse anti-α-tubulin antibodies was Sigma T6074 and rabbit anti-βIII-tubulin was Abcam ab52901. Mouse monoclonal anti-rat TRD antibodies were from Thermo (MA3-927). Alexa Fluor 488 or 568 conjugated goat anti-rabbit IgG, Alexa Fluor 488 or 568-conjugated goat anti-mouse IgG secondary antibodies were purchased from Invitrogen. Relative specificity/selectivity of the antibodies used towards dog or rat jSR proteins indicated by (+) or (−) are shown in Table I.

Sleiman N.H., McFarland T.P., Jones L.R, & Cala S.E. (2015). Transitions of protein traffic from cardiac ER to junctional SR. Journal of molecular and cellular cardiology, 81, 34-45.

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