Anti γ tubulin

Manufactured by Santa Cruz Biotechnology

Sourced in France

Anti-γ-tubulin is a specific antibody that binds to the gamma-tubulin protein. Gamma-tubulin is a key component of the microtubule organizing center (MTOC) and plays a crucial role in the nucleation and organization of microtubules, which are essential for cell division and other cellular processes. The Anti-γ-tubulin antibody can be used to detect and study the localization and abundance of gamma-tubulin in biological samples.

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8 protocols using anti γ tubulin

Protein Extraction and Western Blotting

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Protein extraction and western blotting experiments were performed as already described^{61 (link),62}. The antibodies used were: anti-β-actin (sc-1616, Santa Cruz Biotechnology, Inc., Santa Cruz, CA), anti-γ-tubulin (sc-17787, Santa Cruz), anti-GAPDH (sc-32233, Santa Cruz), anti-vinculin (sc-7649, Santa Cruz), anti-PAX8^{63 (link)}, anti-NKX2.1^{33 (link)}, anti-FOXE1^{64 (link)}, anti-SP-B (ab3430, Millipore), anti-SP-C (90716, Abcam), anti-HIPK2 (Novus Biologicals), anti-HMGA1^{65 (link)}. Densitometric analyses of western blot were performed with Image J software.

Gerlini R., Amendola E., Conte A., Valente V., Tornincasa M., Credendino S.C., Cammarota F., Gentile C., Di Guida L., Paladino S., De Vita G., Fusco A, & Pierantoni G.M. (2019). Double knock-out of Hmga1 and Hipk2 genes causes perinatal death associated to respiratory distress and thyroid abnormalities in mice. Cell Death & Disease, 10(10), 747.

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Protein Immunoprecipitation and Western Blot Analysis

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Cells were lysed using cell extraction buffer (50 mM Tris-HCl [pH 7.5], 150 mM NaCl, 1 mM EDTA, 1% Nonidet P-40, and protease inhibitor cocktail from Roche). Soluble proteins were subjected to immunoprecipitation with anti-γ-tubulin (Santa Cruz), anti-Flag (Sigma-Aldrich), anti-p-Tyr (Merck), anti-GCP5 (Santa Cruz) antibodies, or anti-mouse IgG (Sigma-Aldrich). An aliquot of the total lysate (5%, v/v) was included as the input. Protein samples were separated by SDS-PAGE and transferred onto PVDF membranes. anti-γ-tubulin (Sigma-Aldrich), anti-c-Abl (Santa Cruz), anti-Arg (Santa Cruz), anti-GCP5 (Santa Cruz), anti-GCP2 (Novus), and anti-GCP3 (Proteintech) antibodies were used as primary antibodies to detect the corresponding proteins. Horseradish peroxidase (HRP)-conjugated anti-mouse IgG (Sigma-Aldrich) or anti-rabbit IgG (Sigma-Aldrich) was used as the secondary antibody. HRP-conjugated anti-p-Tyr (Merck), anti-Flag (Sigma-Aldrich), anti-Myc (Sigma-Aldrich), anti-GST (Santa Cruz), and anti-β-actin (Sigma-Aldrich) antibodies were used directly to detect the corresponding proteins. The protein bands were visualized using an ECL detection system (Millipore) at the final step with a chemical imaging analyzer (GE Healthcare).

Wang G.F., Dong Q., Bai Y., Gu J., Tao Q., Yue J., Zhou R., Niu X., Zhu L., Song C., Zheng T., Wang D., Jin Y., Liu H., Cao C, & Liu X. (2022). c-Abl kinase-mediated phosphorylation of γ-tubulin promotes γ-tubulin ring complexes assembly and microtubule nucleation. The Journal of Biological Chemistry, 298(4), 101778.

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Antibody Panel for CPEB Regulatory Pathway

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The following antibodies were used from Abcam: anti-Phospho CPEB1 S174 (ab10890) (Calderone et al. 2015 (link)), anti-CPEB4, anti-TACC3 (ab56595), TACC2 (ab17916), anti-Aurora-A (ab13824), DDX6 (ab40684), anti-Nek9, and anti-PRC1; from Sigma: anti-PARN (HPA006314), anti-α-tubulin and anti-γ-tubulin; from Santa Cruz Biotechnology: anti-CPEB1 (H-300), anti-CPSF1 (B-5; sc-166282), anti-CPSF3 (ww-2; sc-100691), TTP (sc-8458), anti-eIF4E (c-20), and anti-GAPDH (sc32233); from Cell Signaling: anti-phospho-Aurora A (Thr288; 2914), anti-4ET (2297), anti-PABP (4992), anti-S6 (2317), anti-eIF4G (2498), and anti-CPEB1 (13583); and anti-CPEB1 (Proteintech).

Pascual R., Segura-Morales C., Omerzu M., Bellora N., Belloc E., Castellazzi C.L., Reina O., Eyras E., Maurice M.M., Millanes-Romero A, & Méndez R. (2021). mRNA spindle localization and mitotic translational regulation by CPEB1 and CPEB4. RNA, 27(3), 291-302.

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Protein Extraction and Immunoblotting Protocol

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For protein extraction, cells were lysed in lysis buffer containing 1% NP40, 1 mM EDTA, 50 mM Tris-HCl (pH 7.5) and 150 mM NaCl, supplemented with complete protease inhibitors mixture (Roche, Monza, Italy). Total proteins were separated on a 8–10% polyacrylamide-SDS gel electrophoresis and transferred to nitrocellulose membranes (GE Healthcare, Milano, Italy) by electroblotting. Membranes were blocked with 1X TBS, 0.1% Tween-20 with 5% BSA and incubated with antibodies. The antibodies used were as follows: anti-PATZ1 (polyclonal antibody raised against a conserved peptide recognizing all PATZ isoforms of mouse and human origin), anti-EpCam (sc-25308; Santa Cruz), anti-γ-tubulin (sc-17787; Santa Cruz), anti-vinculin (sc-7649; Santa Cruz).

Chiappetta G., Valentino T., Vitiello M., Pasquinelli R., Monaco M., Palma G., Sepe R., Luciano A., Pallante P., Palmieri D., Aiello C., Rea D., Losito S.N., Arra C., Fusco A, & Fedele M. (2015). PATZ1 acts as a tumor suppressor in thyroid cancer via targeting p53-dependent genes involved in EMT and cell migration. Oncotarget, 6(7), 5310-5323.

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Protein Extraction and Western Blotting

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Protein extraction and Western blotting were performed as previously described43 (link)44 (link). The primary antibodies used were anti-IGF2 (#32592) from Sabbiotech; anti-GAPDH (sc-32233) and anti-γ-Tubulin (sc-17787) from Santa Cruz Biotechnology. Blots were visualized by using the Western blotting detection reagents (Thermo Fisher Scientific Inc).

De Martino M., Forzati F., Marfella M., Pellecchia S., Arra C., Terracciano L., Fusco A, & Esposito F. (2016). HMGA1P7-pseudogene regulates H19 and Igf2 expression by a competitive endogenous RNA mechanism. Scientific Reports, 6, 37622.

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Western Blot Analysis of Protein Extracts

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Total protein extracts were obtained by using the JS lysis buffer (20 mM Tris-HCl pH 7.5, 5 mM EDTA, 150 mM NaCl, 1% Nonidet P40) completed with a mix of inhibitors of proteases and phosphatases. The extracted proteins were separated by SDS-PAGE and then transferred onto Protran membranes (Perkin Elmer, Boston, MA). Membranes were blocked with BSA or 5% non-fat milk and then incubated with the following antibodies: anti-V5 (Invitrogen, Carlsband, CA), anti-HA (Roche Applied Science, Mannheim, Germany), anti-CBX7 (Santa Cruz Biotechnology, Inc., Santa Cruz, CA), anti-FLAG (clone M2, Sigma-Aldrich, St. Louis, MO), anti-osteopontin (ab8448, Abcam, Cambridge, UK). To normalize the amount of protein loaded membranes were incubated with anti-γ-Tubulin, anti-β-Actin and anti-Vinculin (Santa Cruz Biotechnology, Inc.). Membranes were then incubated with horseradish peroxidase-conjugated secondary antibody (1:3000) for 60 min at room temperature and the signals were detected by enhanced chemiluminescence (ECL) detection system (Thermo Fisher Scientific, Inc., Waltham, MA). Human osteopontin recombinant full length protein was purchased from Life Technologies.

Sepe R., Formisano U., Federico A., Forzati F., Bastos A.U., D'Angelo D., Cacciola N.A., Fusco A, & Pallante P. (2015). CBX7 and HMGA1b proteins act in opposite way on the regulation of the SPP1 gene expression. Oncotarget, 6(5), 2680-2692.

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Detecting HCMV-Infected Cells with Antibodies

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To identify HCMV-infected cells, we used mouse monoclonal antibodies against the viral proteins IE1 and IE2 (clone E13; Biomérieux, 11–003). Additional primary antibodies used included anti-ZO-1 (Zonula Occludens) (provided by Isabelle Beau, Inserm UMR-S 1185, Le Kremlin Bicêtre, France), anti-γ-tubulin (Santa Cruz Biotechnology, sc-10732), anti-acetylated tubulin (Sigma-Aldrich, T7451), anti-LC3 (MBL-PM036), anti-LC3B (Sigma L7543, used for immunoblot analysis), anti-β-actin (Merck Millipore MAB1501 clone C4) and 4′,6-diamidino-2-phenylindole (DAPI) (Invitrogen, D1306). Secondary antibodies included Alexa Fluor 555 goat anti-mouse and anti-rabbit (Life technology, A21424 – A21428), Alexa Fluor 488 goat anti-rabbit and anti-mouse (Jacskon ImmunoResearch, 111-545-003 and 115-545-003), Alexa Fluor 647 donkey anti-mouse (life technology, A32787). Horseradish peroxidase (HRP)-labeled goat anti-mouse and anti-rabbit secondary antibodies were purchased from Jackson ImmunoResearch Laboratories (115–035–003, 111–035–003).

López Giuliani A.C., Hernández E., Tohmé M.J., Taisne C., Roldán J.S., García Samartino C., Lussignol M., Codogno P., Colombo M.I., Esclatine A, & Delgui L.R. (2020). Human Cytomegalovirus Inhibits Autophagy of Renal Tubular Epithelial Cells and Promotes Cellular Enlargement. Frontiers in Cellular and Infection Microbiology, 10, 474.

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BPA Analogs and MT-aster Formation

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To examine the effect of BPA analogs on MT-aster formation, cells were treated for 3 days with concentrations as follows: For LNCaP BPA 0.1nM, BPS 0.1nM, TBBPA 0.01nM, DMBPA 0.1nM, TMBPA 0.1nM; for C4-2 BPA 0.1nM, BPS 0.1nM, TBBPA 0.01nM, DMBPA 0.01nM, TMBPA 0.1nM. Cells were then treated with nocodazole (Sigma, 1.5Vg/ml) for 40 min on ice in order to depolymerize the interphase MTs. Cells were rinsed to remove the nocodazole, then cells were incubated in fresh warm medium for 7 min at 37°C to allow for MT regrowth. Cells were fixed with methanol at room temperature and stained for centrosomes (anti-γ-tubulin Sigma GTU88 T6557 mouse monoclonal; anti-γ-tubulin Santa Cruz, CA C-20 sc7396 goat polyclonal) and MTs (anti-alpha-tubulin Santa Cruz DM1A sc32296 mouse monoclonal). Cells were scored (~300 cells counted) for MT-aster formation.

Ho S.M., Rao R., To S., Schoch E, & Tarapore P. (2016). Bisphenol A and its analogues disrupt centrosome cycle and microtubule dynamics in prostate cancer. Endocrine-related cancer, 24(2), 83-96.

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