γ tubulin clone gtu 88

Manufactured by Merck Group

Sourced in United States

γ-tubulin (clone GTU-88) is a laboratory reagent used for the detection and study of γ-tubulin, a key component of the microtubule organizing center (MTOC) in eukaryotic cells. This monoclonal antibody can be used in various applications, such as immunofluorescence, immunohistochemistry, and Western blotting, to investigate the localization and expression of γ-tubulin in cells and tissues.

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Lab products found in correlation

Anti mouse alexa 488, by Thermo Fisher Scientific (2 mentions) Monoclonal anti acetylated α tubulin clone 6 11b 1, by Merck Group (2 mentions) Phospho chk1, by Cell Signaling Technology (1 mentions) Phospho chk2 thr68, by Cell Signaling Technology (1 mentions) Parp1, by Cell Signaling Technology (1 mentions) T6199, by Merck Group (1 mentions) Antifade mounting medium, by Thermo Fisher Scientific (1 mentions) Cryostat, by Leica (1 mentions) Gm130, by BD (1 mentions) Ab290, by Abcam (1 mentions) Phospho histone h3 serine 10, by Cell Signaling Technology (1 mentions) Ab89314, by Abcam (1 mentions) Hrp conjugated anti mouse immunoglobulin, by Bio-Rad (1 mentions) Igepal, by Merck Group (1 mentions) Cyclin b1, by Merck Group (1 mentions) α tubulin clone dm1a, by Merck Group (1 mentions) Complete mini protease inhibitor cocktail, by Roche (1 mentions)

Close spelling variants of this product

Mouse monoclonal anti–γ–tubulin (clone GTU-88; T5326 Mouse anti-γ-tubulin (clone GTU-88, Anti-γ-tubulin antibody (clone GTU-88, γ-tubulin (GTU-88; (clone GTU-88, GTU-88 γ-tubulin

7 protocols using γ tubulin clone gtu 88

Immunofluorescence Staining of Galectin-3

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Rat (dilution 1:50) and rabbit polyclonal (1:100) antibodies directed
against Galectin-3 were kindly provided by Dr. H. Leffler (Lund University,
Sweden) and Dr. H.P. Elsässer (Philipps University, Marburg),
respectively. Monoclonal anti-acetylated α-tubulin (clone 6-11B-1, 1:200)
and γ-tubulin (clone GTU-88, 1:50) were from Sigma (Saint-Louis, MO) and
Abcam (Cambridge), respectively. Rabbit polyclonal IFT88 (1:100) was from
Proteintech (Chicago, IL). Anti-mouse Alexa-488 and anti-rabbit Alexa-568
secondary antibodies (1:250) were from Life Technologies (Paisley, UK).

Clare D.K., Magescas J., Piolot T., Dumoux M., Vesque C., Pichard E., Dang T., Duvauchelle B., Poirier F, & Delacour D. (2014). Basal foot MTOC organizes pillar MTs required for coordination of beating cilia. Nature communications, 5, 4888.

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Western Blot Analysis of DNA Repair Proteins

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Cells were harvested by trypsinization, lysed in 2X Laemmli buffer (100 mM Tris-HCl pH 6.8, 200 µM DTT, 3% SDS, 20% glycerol, 0.05% bromophenol blue) at 10⁴ cell/µl. The lysate was denatured for 10 min at 95°C, and sheared by forcing it through a 28-gauge insulin needle 10 times. Lysate from 10⁵ cells was loaded on an SDS/PAGE and transferred to a nitrocellulose membrane. The membrane was blocked in 5% milk in TBS with 0.1% Tween-20 and incubated with primary antibody in TBS/5% milk/0.1% Tween-20 for 2 hours at room temperature. The following primary antibodies were utilized: Polθ (ab80906, Abcam); TRF1 (1449, rabbit polyclonal); Rap1 (1252, rabbit polyclonal); Phospho-Chk2 (Thr68) (Rabbit polyclonal, Cell Signaling); Chk2 (rabbit polyclonal, Cell Signaling); Phospho-Chk1 (Ser 345) (mouse monoclonal, Cell Signaling); Chk1 (mouse monoclonal, Santa Cruz); Lig3 (mouse monoclonal, Santa Cruz); Myc (9E10; Calbiochem); γ- tubulin (clone GTU-88, Sigma); PARP1 (Polyclonal, Cell signaling). (From http://delangelab.rockefeller.edu/protocols)

Mateos-Gomez P.A., Gong F., Nair N., Miller K.M., Lazzerini-Denchi E, & Sfeir A. (2015). Mammalian Polymerase Theta Promotes Alternative-NHEJ and Suppresses Recombination. Nature, 518(7538), 254-257.

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Western Blot Analysis of Cell Lysates

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Cells were harvested by trypsinization, lysed in 2X Laemmli buffer (100 mM Tris-HCl pH 6.8, 200 ∝M DTT, 3% SDS, 20% glycerol, 0.05% bromophenol blue) at 10⁴ cell/μl. The lysate was denatured for 10 min at 95°C, and sheared by forcing it through a 28-gauge insulin needle 5 times. Lysates from 10⁵ cells were loaded on an SDS/PAGE and transferred to a nitrocellulose membrane. The membrane was blocked in 5% milk in TBS with 0.1%Tween-20 and incubated with primary antibody in TBS/5% milk/0.1% Tween-20 for 2 hours at room temperature. The following primary antibodies were utilized: Myc (9E10; Calbiochem); γ-tubulin (clone GTU-88, Sigma); Flag (anti-Flag M2, Sigma); Rad51 (H2 sc8349, Santa Cruz); RPA1 (A300-241A, Bethyl).

Mateos-Gomez P.A., Kent T., Deng S.K., McDevitt S., Kashkina E., Hoang T.M., Pomerantz R.T, & Sfeir A. (2017). The helicase domain of Polθ counteracts RPA to promote alt-NHEJ. Nature structural & molecular biology, 24(12), 1116-1123.

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Western Blot Analysis of PLK4

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Western immunoblot analyses were performed as described previously (46 (link)) using antibodies recognizing PLK4 (3258; Cell Signaling Technology and Abcam), phospho-PLK4 (Ab#3 and 14299), γ-tubulin (clone GTU-88; Sigma), and α-tubulin (DM1A mouse monoclonal antibody T6199; Sigma).

Press M.F., Xie B., Davenport S., Zhou Y., Guzman R., Nolan G.P., O’Brien N., Palazzolo M., Mak T.W., Brugge J.S, & Slamon D.J. (2019). Role for polo-like kinase 4 in mediation of cytokinesis. Proceedings of the National Academy of Sciences of the United States of America, 116(23), 11309-11318.

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Immunohistochemical Analysis of Retinal Inflammation

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Cx3cr1^gfp/+ control mice were sacrificed at P70. CTRL (sham) and LPS intravitreally injected adult C57BL6/J mice were sacrificed 20 h after the injection procedure. Eyes were removed and kept in 4% PFA solution overnight. Eyes were then cryoprotected in 30% sucrose and, after precipitation, frozen in isopentane prior to storage at 80°C. Frozen eyes were cut in 50-μm-thick sections with a Leica cryostat and processed for IF as published.^{55 (link)} Briefly, slices were immersed for 30 min in a boiling 1 mm EDTA solution (pH = 8.0) for antigen retrieval, then incubated with blocking solution (0.1% Triton X-100, 3% BSA and 0.05% Tween 20 in PBS) for 1 h at RT. Sections were incubated with primary antibodies (Iba1, FujiFilm Wako, 1:500; γ-tubulin, clone GTU-88, Sigma-Aldrich, 1:500; GM130, BD bioscience, 1:500) in diluted blocking solution overnight at 4°C and 1 h at RT with fluorophore-conjugated secondary antibodies (Alexa Fluor 488 goat anti-rabbit, 594 goat anti-mouse) and Hoechst for nuclei visualization. The sections were mounted with anti-fade mounting medium (Invitrogen).

Lakhlani P.P., MacMillan L.B., Guo T.Z., McCool B.A., Lovinger D.M., Maze M, & Limbird L.E. (1997). Substitution of a mutant α2a-adrenergic receptor via “hit and run” gene targeting reveals the role of this subtype in sedative, analgesic, and anesthetic-sparing responses in vivo. Proceedings of the National Academy of Sciences of the United States of America, 94(18), 9950-9955.

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Immunofluorescence Staining of Galectin-3

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Protein Extraction and Western Blot Analysis

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Cells were washed in PBS and lysed in the following buffer: 50 mM Tris–HCl, pH 7.4, 0.5% IGEPAL (Sigma‐Aldrich, St. Louis, MO, USA), 150 mM NaCl, 1 mM DTT, 5% glycerol, 50 mM NaF, 1 mM PMSF, 25 mM β‐glycerophosphate, 1 mM vanadate, Complete Mini Protease Inhibitor Cocktail (Roche Diagnostics, Basel, Switzerland). Proteins were then resolved by SDS–PAGE and transferred onto a nitrocellulose membrane. Primary antibodies were directed against α‐tubulin (clone DM1A, 1:5,000; Sigma‐Aldrich, St. Louis, MO, USA), γ‐tubulin (clone GTU‐88, 1:5,000; Sigma‐Aldrich, St. Louis, MO, USA), GFP (ab290; 1:5,000; Abcam, Cambridge, UK), STIL (ab89314, 1:2,000; Abcam, Cambridge, UK), Sas‐6 (Kleylein‐Sohn et al, 2007), CP110 (1:2,000, Schmidt et al, 2009), cyclin A (1:2,000, Maridor et al, 1993), cyclin B1 (05‐373, 1:2,000, Merck Millipore, Darmstadt, Germany), and phospho‐histone H3/serine 10 (3377, 1:1,000, Cell Signaling Technology, Danvers, MA, USA); secondary antibodies were HRP‐conjugated anti‐mouse immunoglobulin (170‐6516, 1:3,000, Bio‐Rad, Hercules, CA, USA) or anti‐rabbit immunoglobulin (170‐6515, 1:3,000, Bio‐Rad, Hercules, CA, USA).

Bauer M., Cubizolles F., Schmidt A, & Nigg E.A. (2016). Quantitative analysis of human centrosome architecture by targeted proteomics and fluorescence imaging. The EMBO Journal, 35(19), 2152-2166.

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