|Related Categories||Alphabetical Index, Antibodies, Antibodies for Cell Biology, Antibodies to Cell and Organelle Proteins, Antibodies to Centrosome,|
|species reactivity||Xenopus, canine, chicken, hamster, human, rat, bovine, mouse|
|application(s)||immunocytochemistry: 1:5,000-1:10,000 using HeLa cells|
|indirect ELISA: suitable|
|western blot: 1:10,000 using cultured chicken fibroblast extract|
|antibody form||ascites fluid|
|mol wt||antigen mol wt 48 kDa|
|contains||15 mM sodium azide|
|shipped in||dry ice|
human ... TUBG1(7283)|
mouse ... Tubg1(103733)
rat ... Tubg1(252921)
synthetic γ-tubulin peptide (amino acids 38-53), conjugated to KLH.
Gamma-Tubulin (48kDa) is a ubiquitous and highly conserved protein within the microtubule organizing centers (MTOCs) in eukaryotic cells. Gamma-Tubulin binds microtubule minus ends and is responsible for mediating the link between microtubules and the centrosome. It functions as the microtubule nucleator at the MTOC. It binds to the β-tubulin half of the tubulin molecule, thus establishing the polarity of a microtubule, leaving the α-tubulin half exposed at the plus end. gamma-Tubulin abundance is less than 1% of the level of either α- or β-tubulin.
Monoclonal Anti-gamma-Tubulin recognizes an epitope located in the N-terminal amino acids 38-53 of gamma-tubulin (48 kDa). Cross reactivity has been observed with human, bovine, dog, hamster, rat, mouse, chicken, and Xenopus gamma-tubulin.
The antibody recognizes an epitope located within the N-terminal region of γ-tubulin.
Monoclonal Anti-gamma-Tubulin is suitable for use in immunochemical applications such as immunoblotting, immunocytochemical staining of cultured cells, and in ELISA.
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Keywords: Buffers, Cell biology, Epigenetics, Immunohistochemistry, Immunoprecipitation, Molecular biology, Neuroscience, Western blot
Ovarian Hyperstimulation Induces Centrosome Amplification and Aneuploid Mammary Tumors Independently of Alterations in p53 in a Transgenic Mouse Model of Breast Cancer Sutton, A.L., et al. Oncogene 3, e2366, (2008)
Mutual Inhibition between Kaposi’s Sarcoma-Associated Herpesvirus and Epstein-Barr Virus Lytic Replication Initiators in Dually-Infected Primary Effusion Lymphoma Zhang, L., et al. PLoS ONE 3, e1569, (2008)
Accumulation of polyubiquitylated proteins in response to Ala-Ala-Phe-chloromethylketone is independent of the inhibition of Tripeptidyl peptidase II. Villasevil, E.M., et al. Biochim. Biophys. Acta 1803, 1094-105, (2010)
Human RASSF7 regulates the microtubule cytoskeleton and is required for spindle formation, Aurora B activation and chromosomal congression during mitosis. Recino, A., et al. Biochem. J. 430, 207-13, (2010)
Mutations in mouse Aspm (abnormal spindle-like microcephaly associated) cause not only microcephaly but also major defects in the germline. Pulvers, J.N., et al. Proc. Natl. Acad. Sci. U. S. A. 107, 16595-600, (2010)
MyD88 interacts with interferon regulatory factor (IRF) 3 and IRF7 in Atlantic salmon (Salmo salar): transgenic SsMyD88 modulates the IRF-induced type I interferon response and accumulates in aggresomes. Iliev, D.B., et al. J. Biol. Chem. 286, 42715-24, (2011)
Human mineralocorticoid receptor (MR) gene haplotypes modulate MR expression and transactivation: implication for the stress response. van Leeuwen, N., et al. Psychoneuroendocrinology 36, 699-709, (2011)
Small GTPase Rab5 participates in chromosome congression and regulates localization of the centromere-associated protein CENP-F to kinetochores. Serio, G., et al. Proc. Natl. Acad. Sci. U. S. A. 108, 17337-42, (2011)
The ARF tumor suppressor inhibits tumor cell colonization independent of p53 in a novel mouse model of pancreatic ductal adenocarcinoma metastasis. Muniz, V.P., et al. Mol. Cancer Res. 9, 867-77, (2011)
Loss of Cyclin-Dependent Kinase 2 (CDK2) Inhibitory Phosphorylation in a CDK2AF Knock-In Mouse Causes Misregulation of DNA Replication and Centrosome Duplication. Zhao, H., et al. Mol. Cell. Biol. 32, 1421-32, (2012)
Depletion of primary cilia in articular chondrocytes results in reduced Gli3 repressor to activator ratio, increased Hedgehog signaling, and symptoms of early osteoarthritis. Chang, C.F., et al. Osteoarth. Cartil. 20, 152-61, (2012)
Low plasma membrane expression of the miltefosine transport complex renders Leishmania braziliensis refractory to the drug. María P. Sánchez-Cañete et al Antimicrob. Agents Chemother. 53, 1305-13, (2009)
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