Exbio — Research products — Antibodies — Cytoskeleton and ECM — Anti-gamma-Tubulin Purified

Anti-gamma-Tubulin Purified

Regulatory status

RUO

Antigen

gamma-Tubulin

Clone

TU-32

Format

Purified

Reactivity

Protozoa, Plants, Animals

Application

WB, ICC

Variant

0.1 mg

11-543-C100

In stock

187.00 USD

0.025 mg

11-543-C025

Delivery 1 week

93.50 USD

Variant

0.1 mg

11-543-C100

In stock

187.00 USD

0.025 mg

11-543-C025

Delivery 1 week

93.50 USD

Contact distributor

Product details

Description

Images

References

SDS download

Isotype

Mouse IgG1

Specificity

The antibody TU-32 recognizes C-terminus (amino acids 434-449 in human) of gamma-tubulin, a 48 kDa structural constituent of cytoskeleton and microtubule organizing center (MTOC). The epitope was located in the aminoacid sequence PDYISW (aa441-446 in human), which is identical for gamma-tubulin 1 and gamma-tubulin 2.

Application

WB, ICC

Application details

Western blotting: Recommended dilution: 1-2 μg/ml, reducing conditions.
Immunocytochemistry: Methanol/acetone fixation required.

Reactivity

Protozoa, Plants, Animals

Immunogen

human gamma-tubulin peptide EYHAATRPDYISWGTQ, amino acids 434-449

Concentration

1 mg/ml

Preparation

Purified by protein-A affinity chromatography.

Formulation

Phosphate buffered saline (PBS), pH 7.4, 15 mM sodium azide

Storage and handling

Store at 2-8°C. Do not freeze.

The product is intended For Research Use Only. Diagnostic or therapeutic applications are strictly forbidden. Products shall not be used for resale or transfer to third parties either as a stand-alone product or as a manufacture component of another product without written consent of EXBIO Praha, a.s. EXBIO Praha, a.s. will not be held responsible for patent infringement or any other violations of intellectual property rights that may occur with the use of the products. Orders for all products are accepted subject to the Term and Conditions available at www.exbio.cz. EXBIO, EXBIO Logo, and all other trademarks are property of EXBIO Praha, a.s.

Other names

TUBG

Antigen description

The gamma-tubulin (TUBG1; relative molecular weight about 48 kDa) is a minor member of tubulin family (less that 0.01% of tubulin dimer). The gamma-tubulin ring structures, however, serve to provide structural primer for initiation of microtubular nucleation and growth, thereby being crutial for microtubule-based cellular processes, above all for mitotic spindle formation. In animal cells, a center of microtubule organization is the centrosome composed of a pair of cylindrical centrioles surrounded by fibrous pericentriolar material containing gamma-tubulin. Formation of the mitotic spindle is preceded by duplication of centrosome during S phase. Before mitosis, both centrosomes increase their microtubule nucleation capacity and form two microtuble asters that are pushed apart from each other by the forces of motor proteins associated at the microtubule surface. Humans possess two gamma-tubulin genes. Gamma-tubulin 1 represents a ubiquitous isotype, whereas gamma-tubulin 2 is found predominantly in the brain, where it may be endowed with divergent functions beyond microtubule nucleation.

Entrez Gene ID 7283

UniProt ID P23258

Western blotting analysis of human gamma-tubulin using mouse monoclonal antibody TU-32 on lysates of various cell lines under reducing and non-reducing conditions. Nitrocellulose membrane was probed with 2 µg/ml of mouse anti-gamma-tubulin monoclonal antibody followed by IRDye800-conjugated anti-mouse secondary antibody. A specific band was detected for gamma-tubulin at approximately 46 kDa.

Western blotting analysis of differential reactivity of monoclonal antibodies to γ-tubulin with human γ-tubulin isotypes. (A) Immunoblots of total cell lysates from SH-SY5Y cells, expressing TagRFP-tagged human γ-tubulin 1 (γ-Tb1) or γ-tubulin 2 (γ-Tb2), probed with Abs to γ-tubulin (TU-30, TU-32), TagRFP (RFP) and GAPDH. In control samples, only secondary anti-mouse Ab was applied. (B) Immunoblots of immobilized GST-tagged human C-terminal regions (a.a. 362-451) of γ-Tb1 or γ-Tb2 probed with Abs to γ-tubulin (TU-30, TU-32) and GST. In control samples, only secondary anti-mouse Ab was applied.

General references:

Wiese C, Zheng Y: Microtubule nucleation: gamma-tubulin and beyond. J Cell Sci. 2006 Oct 15;119(Pt 20):4143-53.
PubMed

Haren L, Remy MH, Bazin I, Callebaut I, Wright M, Merdes A. NEDD1-dependent recruitment of the gamma-tubulin ring complex to the centrosome is necessary for centriole duplication and spindle assembly. J Cell Biol. 2006 Feb 13;172(4):505-15.
PubMed

Sulimenko V, Dráberová E, Sulimenko T, Macurek L, Richterová V, Dráber P, Dráber P: Regulation of microtubule formation in activated mast cells by complexes of gamma-tubulin with Fyn and Syk kinases. J Immunol. 2006 Jun 15;176(12):7243-53.
PubMed

Wiese C, Zheng Y: Microtubule nucleation: gamma-tubulin and beyond. J Cell Sci. 2006 Oct 15;119(Pt 20):4143-53.
PubMed

Draberova L, Draberova E, Surviladze Z, Draber P, Draber P: Protein tyrosine kinase p53/p56 (lyn) forms complexes with gamma-tubulin in rat basophilic leukemia cells. Int Immunol. 1999 Nov;11(11):1829-39.
PubMed

Product specific references:

Dráberová E, Sulimenko V, Vinopal S, Sulimenko T, Sládková V, D'Agostino L, Sobol M, Hozák P, Křen L, Katsetos CD, Dráber P: Differential expression of human γ-tubulin isotypes during neuronal development and oxidative stress points to a γ-tubulin-2 prosurvival function. FASEB J. 2017 May;31(5):1828-1846.
PubMed

Katsetos CD, Dráberová E, Smejkalová B, Reddy G, Bertrand L, de Chadarévian JP, Legido A, Nissanov J, Baas PW, Dráber P: Class III beta-tubulin and gamma-tubulin are co-expressed and form complexes in human glioblastoma cells. Neurochem Res. 2007 Aug;32(8):1387-98.
PubMed

Katsetos CD, Reddy G, Dráberová E, Smejkalová B, Del Valle L, Ashraf Q, Tadevosyan A, Yelin K, Maraziotis T, Mishra OP, Mörk S, Legido A, Nissanov J, Baas PW, de Chadarévian JP, Dráber P: Altered cellular distribution and subcellular sorting of gamma-tubulin in diffuse astrocytic gliomas and human glioblastoma cell lines. J Neuropathol Exp Neurol. 2006 May;65(5):465-77.
PubMed

Libusová L, Sulimenko T, Sulimenko V, Hozák P, Dráber P: gamma-Tubulin in Leishmania: cell cycle-dependent changes in subcellular localization and heterogeneity of its isoforms. Exp Cell Res. 2004 May 1;295(2):375-86.
PubMed

Sulimenko V, Sulimenko T, Poznanovic S, Nechiporuk-Zloy V, Böhm KJ, Macurek L, Unger E, Dráber P: Association of brain gamma-tubulins with alpha beta-tubulin dimers. Biochem J. 2002 Aug 1;365(Pt 3):889-95.
PubMed

Dráberová E, Macůrek L, Richterová V, Böhm KJ, Dráber P: Monoclonal antibody KN-01 against the heavy chain of kinesin. Folia Biol (Praha). 2002;48(2):77-9.

Linhartová I, Novotná B, Sulimenko V, Dráberová E, Dráber P: Gamma-tubulin in chicken erythrocytes: changes in localization during cell differentiation and characterization of cytoplasmic complexes. Dev Dyn. 2002 Mar;223(2):229-40.
PubMed

Nohýnková E., Dráber P., Reishig J., Kulda J: Cell-cycle dependent localization of gamma-tubulin in early branching eukaryote, a diplomonad flagellate Giardia intestinalis. Eur. J. Cell Biol. 78: 438-445, 2000.

Binarová P, Cenklová V, Hause B, Kubátová E, Lysák M, Dolezel J, Bögre L, Dráber P: Nuclear gamma-tubulin during acentriolar plant mitosis. Plant Cell. 2000 Mar;12(3):433-42.
PubMed

Dráberová L, Dráberová E, Surviladze Z, Dráber P, Dráber P. Protein tyrosine kinase p53/p56(lyn) forms complexes with gamma-tubulin in rat basophilic leukemia cells. Int Immunol. 1999 Nov;11(11):1829-39.
PubMed

Binarová P., Doležel J., Hause B., Dráber P: Association of g-tubulin with kinetochore/centromeric region of plant chromosomes. Plant J. 14: 751-757, 1998.
PubMed

Nováková M, Dráberová E, Schürmann W, Czihak G, Viklický V, Dr-aber P: gamma-Tubulin redistribution in taxol-treated mitotic cells probed by monoclonal antibodies. Cell Motil Cytoskeleton. 1996;33(1):38-51.
PubMed