Rabbit anti β tubulin

Manufactured by Merck Group

Sourced in United States

Rabbit anti-β-tubulin is a primary antibody designed to specifically recognize and bind to the β-tubulin protein. β-tubulin is a key component of microtubules, which are essential structures involved in cell division, intracellular transport, and cellular morphology. This antibody can be used in various immunodetection techniques, such as Western blotting, immunohistochemistry, and immunocytochemistry, to study the expression and localization of β-tubulin in biological samples.

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Anti-tubulin (542 citations) β-tubulin (395 citations) Anti-β-tubulin (260 citations) Rabbit anti-β-tubulin III (5 citations) Rabbit anti-tubulin (4 citations) Rabbit β-tubulin (2 citations) Rabbit anti- (2 citations) Rabbit anti-β-tubulin antibody (2 citations)

9 protocols using rabbit anti β tubulin

Cloning and Mutagenesis of SHANK1

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Human SHANK1 was cloned into the pcDNA3.1(+)-N-HA
plasmid and mutagenesis for p.Gly1105fs and p.Glu1119* was performed using
GenScript (Piscataway, NJ). Homer1b, and pClneo-GKAP-myc plasmids were used for
biochemical and imaging experiments. The commercial antibodies used in this
study were mouse rabbit anti-Homer1/2/3 (Synaptic Systems, 160103), mouse
anti-PSD-95 (Neuromab, clone K28/43), guinea pig anti-VGLUT1 (Millipore,
AB5905), mouse anti-myc (Cell Signaling, clone 9B11), rabbit anti-HA (Abcam,
ab9110), rat anti-HA (Roche), rabbit anti-β tubulin (Sigma, T2200), and
mouse anti-β actin (ABM, G043).

May H.J., Jeong J., Revah-Politi A., Cohen J.S., Chassevent A., Baptista J., Baugh E.H., Bier L., Bottani A., Rodrigues M.T., Conlon C., Fluss J., Guipponi M., Kim C.A., Matsumoto N., Person R., Primiano M., Rankin J., Shinawi M., Smith-Hicks C., Telegrafi A., Toy S., Uchiyama Y., Aggarwal V., Goldstein D.B., Roche K.W, & Anyane-Yeboa K. (2021). Truncating variants in the SHANK1 gene are associated with a spectrum of neurodevelopmental disorders. Genetics in medicine : official journal of the American College of Medical Genetics, 23(10), 1912-1921.

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Antibody Source and Generation

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Rabbit anti-β-actin (catalog number 3700) was purchased from Cell Signaling Technology. Rabbit anti-β-tubulin (catalog number T8328), mouse antiluciferase (catalog number L2164), and rabbit anti-Flag (catalog number F7425) were purchased from Sigma-Aldrich. Anti-Renilla luciferase (catalog number ab185926) was purchased from Abcam. Rabbit anti-MARV NP (catalog number 0303-012) and mouse anti-MARV VP40 (clone 6B1) (catalog number 0203-016) were purchased from IBT BioServices. Rabbit anti-MARV VP24 (peptide 230-REHSQMEKGQPLNLTQ-259) and anti-MARV VP30 (peptides 4-PRGRSRTRNHQVTPTIYHETQLPSK-28 and 258-CESSISVQASYDHFILPQSQGK-279) antibodies to the peptides indicated in parentheses were generated by Pacific Immunology.

Edwards M.R., Vogel O.A., Mori H., Davey R.A, & Basler C.F. (2022). Marburg Virus VP30 Is Required for Transcription Initiation at the Glycoprotein Gene. mBio, 13(5), e02243-22.

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Western Blot Analysis of αSMA and β-Tubulin

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Total protein was harvested from 2 × 10⁶ cells and lysed in 60 mM Tris, pH 6.8, 2% SDS, containing 1× protease inhibitor cocktail (Sigma, St Louis, Mo), and analyzed for αSMA (mouse anti-αSMA, cat. # A2547; Sigma-Aldrich) and β-tubulin (rabbit anti-β-tubulin, cat. # 2146; Cell Signaling Technology, Danvers, Mass) by Western blot as previously described.13 (link) Anti-mouse or anti-rabbit horseradish peroxidase (HRP)–conjugated secondary antibodies were obtained from Jackson Immunoresearch (West Grove, Pa). Western blot signals were visualized using Immobilon Western chemiluminescent HRP substrate (Millipore, Billerica, Mass), with images captured using a c-DiGit Blot Scanner and Image Studio software (Li-Cor, Lincoln, Neb).

Woeller C.F., Woodroof A., Lacy S.H., Cottler P.S., Gui J.L., Piñeros-Fernandez A., Pollock S.J, & Phipps R.P. (2018). Evaluating a Variable Porosity Wound Dressing With Anti-Scar Properties in a Porcine Model of Wound Healing. Eplasty, 18, e20.

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Western Blot Protein Detection Protocol

Cited 1 time

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Proteins were separated on 4–12% gradient NuPAGE Novex Bis-Tris gel (Life Technologies), transferred to PVDF membrane (Millipore), blocked in 1 × TBS-Tween with 5% non-fat dry milk and incubated with corresponding primary antibody and secondary antibodies. The following antibodies were used: rabbit anti-TGM2, (1:1,000; Cat. No. HPA021019, Sigma-Aldrich, Prestige Antibodies Powered by Atlas Antibodies), Rabbit anti-CLIC3 (1:3,000; produced in house31 (link)), Rabbit anti-β-tubulin (1:1,000; Cat. No. sc-9104, Santa Cruz), Mouse anti-Vinculin (1:1,000; Cat. No. V9131, Sigma-Aldrich) and Mouse anti-αSMA (1:1,000; Cat. No. A5228, Sigma). As secondary antibodies, horseradish peroxidase-conjugated (1:10,000; Cat. No. HAF008 and HAF007, H&D systems,), IRDye 680RD (1:10,000; Cat. No. 926-68072, LI-COR) and IRDye 800CW (1:10,000; Cat. No. 926-32213, LI-COR) were used. Images were captured with a Bio-Rad GS-800 Calibrated densitometer (Quantity-One software version 4.6.3) or a LI-COR Odyssey CLx scanner (Image Studio software, version 5.0.21) for chemluminiscent or fluorescence western blots, respectively. Representative images from reproducible, independent experiments are shown. Uncropped scans of the western blots are reported in Supplementary Information (Supplementary Figs 9 and 10).

Hernandez-Fernaud J.R., Ruengeler E., Casazza A., Neilson L.J., Pulleine E., Santi A., Ismail S., Lilla S., Dhayade S., MacPherson I.R., McNeish I., Ennis D., Ali H., Kugeratski F.G., Al Khamici H., van den Biggelaar M., van den Berghe P.V., Cloix C., McDonald L., Millan D., Hoyle A., Kuchnio A., Carmeliet P., Valenzuela S.M., Blyth K., Yin H., Mazzone M., Norman J.C, & Zanivan S. (2017). Secreted CLIC3 drives cancer progression through its glutathione-dependent oxidoreductase activity. Nature Communications, 8, 14206.

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GABAB Receptor Antibodies Protocol

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The following antibodies were used in this study: sheep anti-GABA_BR1 antibody (Pontier et al., 2006 (link)), mouse anti-GABA_BR1 (University of California–Davis/National Institutes of Health NeuroMab Facility, 75-183, clone N93A/49; Sigma, WH0002550M1-100UG, clone 2D7), rabbit anti-GABA_BR2 (GlaxoSmithKline) (Pontier et al., 2006 (link)), sheep IgG (Thermo Fisher Scientific, 31243), rabbit anti-C terminus KCC2 (Millipore, 07-432), rabbit anti-β-tubulin (Sigma, T2200) rabbit anti-GFP (Thermo Fisher Scientific, A11122), rabbit IgG (Thermo Fisher Scientific, 31235), mouse anti-β-tubulin (Cambridge Bioscience, MMS-435P-250), mouse anti-transferrin receptor (Thermo Fisher Scientific, 13-6890), mouse anti-NKCC1 (Developmental Studies Hybridoma Bank, T4 clone), mouse anti-actin (Sigma, A3854), HRP-conjugated donkey anti-rabbit (Stratech, 711-055-152), HRP-conjugated goat anti-mouse (Stratech, 115-055-166), donkey anti-rabbit Cy3-conjugated monovalent Fab fragment (Stratech, 111-167-003), and donkey anti-rabbit Alexa-488-conjugated secondary (Thermo Fisher Scientific, A21206).

Wright R., Newey S.E., Ilie A., Wefelmeyer W., Raimondo J.V., Ginham R., Mcllhinney R.A, & Akerman C.J. (2017). Neuronal Chloride Regulation via KCC2 Is Modulated through a GABAB Receptor Protein Complex. The Journal of Neuroscience, 37(22), 5447-5462.

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Immunoblotting of Alzheimer's Markers

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Cerebral cortex and hippocampus extracts were loaded onto 10-16 % Tris/tricine SDS gels, and transferred to nitrocellulose membranes before overnight incubation with one of the following primary antibodies: rabbit anti-APP (1:1000; Millipore), rabbit anti-Aβ_1–42 (1:1000; Sigma-Aldrich, Saint Louis, MO, USA) and mouse anti-SAPPβ (1:1000; Sigma-Aldrich), mouse anti-CTFβ (1:1500; Millipore), mouse anti-BACE1 (1:2000; Millipore), rabbit anti-PS1 (1:1000; Sigma-Aldrich), rabbit anti-NEP (1:1000; Millipore), rabbit anti-IDE (1:1000; Abcam, Cambridge, MA, USA), mouse anti-GFAP (1:2000; Millipore), mouse anti-Iba-1 (1:500; Wako), mouse anti-SYP (1:1500; Millipore), rabbit anti-PSD-95 (1:1000; Abcam), mouse anti-BDNF (1:500; Sigma-Aldrich) or rabbit anti-β-tubulin (1:3000; Sigma-Aldrich). Horseradish peroxidase-conjugated secondary antibodies (Vector Laboratories) were used, and bands were visualized using ECL plus detection system. β-tubulin was utilized as an internal control for protein loading and transfer efficiency.

Xu Z., Xiao N., Chen Y., Huang H., Marshall C., Gao J., Cai Z., Wu T., Hu G, & Xiao M. (2015). Deletion of aquaporin-4 in APP/PS1 mice exacerbates brain Aβ accumulation and memory deficits. Molecular Neurodegeneration, 10, 58.

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Shank3 Plasmid and Antibody Characterization

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HA-tagged rat Shank3 plasmid was kindly provided by Eunjoon Kim. CaMKII and CaMKII R42K plasmids were characterized in our previous studies. pClneo-GKAP-myc plasmids were used for biochemical and imaging experiments. The commercial antibodies used in this study were rabbit anti-Shank3 (Synaptic System, 162 302), mouse anti-PSD-95 (Neuromab, clone K28/43), mouse anti-myc (Cell Signaling, clone 9B11), rabbit anti-HA (Abcam, ab9110), rat anti-HA (Roche), rabbit anti-β tubulin (Sigma, T2200), and mouse anti-β actin (ABM, G043).

Jeong J., Li Y, & Roche K.W. (2021). CaMKII Phosphorylation Regulates Synaptic Enrichment of Shank3. eNeuro, 8(3), ENEURO.0481-20.2021.

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Antibody Characterization for Amyloid-β

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15B3 was obtained from Prionics (now Thermo Fisher Scientific, Rockford, IL USA). Three batches of 15B3 were used: most of the studies were carried out with batch # 071114A, with a nominal concentration of 5 mg/mL; when indicated, batches # 110531 (0.9 mg/mL) and # 061013 (0.8 mg/mL) were also used.
Control mouse IgM was from Thermo Fisher Scientific, Rockford, IL, USA; anti-Aβ monoclonal antibody 4G8 was from Covance, Princeton, NJ, USA; anti-Aβ oligomer polyclonal antibodies OC and A11 were from Merck Millipore, Darmstadt, Germany; mouse monoclonal anti-Aβ 6E10 was from Covance, Emerville, CA, USA; rabbit anti-β-tubulin was from Sigma, St. Louis, MO, USA and guinea pig anti-Bassoon was from Synaptic System, Gottingen, Germany.

Stravalaci M., Tapella L., Beeg M., Rossi A., Joshi P., Pizzi E., Mazzanti M., Balducci C., Forloni G., Biasini E., Salmona M., Diomede L., Chiesa R, & Gobbi M. (2016). The Anti-Prion Antibody 15B3 Detects Toxic Amyloid-β Oligomers. Journal of Alzheimer's Disease, 53(4), 1485-1497.

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Immunofluorescence of Tubulin and Kinesin

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Primary antibodies for immunofluorescence were: mouse anti-β-tubulin (Sigma-Aldrich, 1:1000), rabbit anti-β-tubulin (Sigma-Aldrich, 1:1000) and rabbit anti-KIF5B (Abcam), Alexa488-, Alexa568-, and Alexa647-conjugated highly cross-absorbed secondary antibodies (Invitrogen). Coverslips were mounted in Vectashield Mounting Medium (Vector Labaratories). Cells were treated with indicated drugs for three hours unless otherwise indicated. Drugs used were: Kinesore (Tocris Bioscience).

Bracey K.M., Noguchi P., Edwards C., Cario A., Gu G, & Kaverina I. (2023). Glucose-stimulated KIF5B-driven microtubule sliding organizes microtubule networks in pancreatic beta cells. bioRxiv.

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