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alpha Tubulin antibody (TUBA1) (N-Term)

Details for Product anti-TUBA1 Antibody No. ABIN93891, Supplier: Log in to see
Antigen
  • K-ALPHA-1
  • mec-12
  • TUBA2
  • tuba4
Alternatives
anti-General alpha Tubulin antibody for Immunocytochemistry
Epitope
N-Term
16
13
5
4
4
4
3
2
2
2
2
1
1
1
1
Reactivity
General
111
65
57
28
27
18
15
11
9
8
7
5
5
3
3
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
Host
Mouse
96
41
16
6
2
Clonality (Clone)
Monoclonal ()
Conjugate
This alpha Tubulin antibody is un-conjugated
9
5
5
1
1
1
1
1
1
1
1
1
1
1
Application
Immunocytochemistry (ICC), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Western Blotting (WB)
139
49
44
44
42
40
39
15
9
6
2
1
1
1
Supplier
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Immunogen Fraction of tubulin purified from porcine brain by two cycles of polymerization - depolymerization.
Clone TU-01
Isotype IgG1
Specificity The antibody TU-01 recognizes the defined epitope (aa 65-97) on N-terminal structural domain of alpha-tubulin.
Purification Purified from ascites by precipitation methods.
Purity > 95 % (by SDS-PAGE)
Alternative Name alpha-tubulin (TUBA1 Antibody Abstract)
Background The microtubules are intracellular dynamic polymers made up of evolutionarily conserved polymorphic alpha/beta-tubulin heterodimers and a large number of microtubule-associated proteins (MAPs). The microtubules consist of 13 protofilaments and have an outer diameter 25 nm. Microtubules have their intrinsic polarity, highly dynamic plus ends and less dynamic minus ends. Microtubules are required for vital processes in eukaryotic cells including mitosis, meiosis, maintenance of cell shape and intracellular transport. Microtubules are also necessary for movement of cells by means of flagella and cilia. In mammalian tissue culture cells microtubules have their minus ends anchored in microtubule organizing centers (MTOCs).The GTP (guanosintriphosphate) molecule is an essential for tubulin heterodimer to associate with other heterodimers to form microtubule. In vivo, microtubule dynamics vary considerably. Microtubule polymerization is reversible and a populations of microtubules in cells are on their minus ends either growing or shortening -, this phenomenon is called dynamic instability of microtubules. On a practical level, microtubules can easily be stabilized by the addition of non-hydrolysable analogues of GTP (eg. GMPPCP) or more commonly by anti-cancer drugs such as Taxol. Taxol stabilizes microtubules at room temperature for many hours. Using limited proteolysis by enzymes both tubulin subunits can be divided into N-terminal and C-terminal structural domains. The alpha-tubulin (relative molecular weight around 50 kDa) is globular protein that exists in cells as part of soluble alpha/beta-tubulin dimer or it is polymerized into microtubules. In different species it is coded by multiple tubulin genes that form tubulin classes (in human 6 genes). Expressed tubulin genes are named tubulin isotypes. Some of the tubulin isotypes are expressed ubiquitously, while some have more restricted tissue expression.Alpha-tubulin is also subject of numerous post-translational modifications. Tubulin isotypes and their posttranslational modifications are responsible for multiple tubulin charge variants - tubulin isoforms. Heterogeneity of alpha-tubulin is concentrated in C-terminal structural domain.
Pathways Microtubule Dynamics
Application Notes Western Blotting: Recommended dilution: 1-2 µg/mL,
Incubation 60 min in room temperature
Positive control: HPB-ALL human peripheral blood leukemia cell line (
Incubation 60 min) Porcine brain lysate (
Incubation 90 min)
Sample preparation: Resuspend approx. 50 mil. cells in 1 mL cold Lysis buffer (1 % laurylmaltoside in 20 mM Tris/Cl, 100 mM NaCl pH 8.2, 50 mM NaF including Protease inhibitor Cocktail). Incubate 60 min on ice. Centrifuge to remove cell debris. Mix lysate with reducing Laemmli SDS-PAGE sample buffer.
Application note: Reducing conditions.
Immunohistochemistry (paraffin sections) Recommended dilution: 5 µg/mL
Positive tissue: heart.
Immunocytochemistry
Staining technique: fixed and permeabilized cells

Working concentrations should be determined by the investigator.
Restrictions For Research Use only
Concentration 1 mg/mL
Buffer Phosphate buffered saline (PBS) with 15 mM sodium azide, approx. pH 7.4
Preservative Sodium azide
Precaution of Use WARNING: Reagents contain sodium azide. Sodium azide is very toxic if ingested or inhaled. Avoid contact with skin, eyes, or clothing. Wear eye or face protection when handling. If skin or eye contact occurs, wash with copious amounts of water. If ingested or inhaled, contact a physician immediately. Sodium azide yields toxic hydrazoic acid under acidic conditions. Dilute azide-containing compounds in running water before discarding to avoid accumulation of potentially explosive deposits in lead or copper plumbing.
Handling Advice Do not freeze.
Storage 4 °C
Storage Comment Store at 2-8 °C. Do not use after expiration date stamped on vial label.
Supplier Images
Immunofluorescence (IF) image for anti-alpha Tubulin antibody (TUBA1) (N-Term) (ABIN93891) Immunofluorescence staining of 3T3 mouse embryonal fibroblast cell line using anti-al...
Immunofluorescence (IF) image for anti-alpha Tubulin antibody (TUBA1) (N-Term) (ABIN93891) Immunofluorescence staining of HeLa human cervix carcinoma cell line using anti-alpha...
Immunofluorescence (IF) image for anti-alpha Tubulin antibody (TUBA1) (N-Term) (ABIN93891) Nucleus is stained with DAPI (blue).
Western Blotting (WB) image for anti-alpha Tubulin antibody (TUBA1) (N-Term) (ABIN93891) Use of anti-alpha-tubulin antibody as a loading control (A) in an Western blotting ex...
Western Blotting (WB) image for anti-alpha Tubulin antibody (TUBA1) (N-Term) (ABIN93891) Use of anti-alpha-tubulin antibody as a loading control (A) in an Western blotting ex...
Product cited in: Lueck, Hennig, Lommatzsch, Pauleikhoff, Wasmuth: "Complement and UV-Irradiated Photoreceptor Outer Segments Increase the Cytokine Secretion by Retinal Pigment Epithelial Cells." in: Investigative ophthalmology & visual science, Vol. 53, Issue 3, pp. 1406-13, 2012

Dolezalova, Mraz, Barta, Plevova, Vinarsky, Holubcova, Jaros, Dvorak, Pospisilova, Hampl: "MicroRNAs regulate p21(Waf1/Cip1) protein expression and the DNA damage response in human embryonic stem cells." in: Stem cells (Dayton, Ohio), Vol. 30, Issue 7, pp. 1362-72, 2012

Pospichalova, Tureckova, Fafilek, Vojtechova, Krausova, Lukas, Sloncova, Takacova, Divoky, Leprince, Plachy, Korinek: "Generation of two modified mouse alleles of the Hic1 tumor suppressor gene." in: Genesis (New York, N.Y. : 2000), 2011

Cancer: Krupkova, Loja, Redova, Neradil, Zitterbart, Sterba, Veselska: "Analysis of nuclear nestin localization in cell lines derived from neurogenic tumors." in: Tumour biology, 2011 Method employed by authors: Immunohistochemistry(IHC) (Sample species: Human).

Sana, Zambo, Skoda, Neradil, Chlapek, Hermanova, Mudry, Vasikova, Zitterbart, Hampl, Sterba, Veselska: "CD133 expression and identification of CD133/nestin positive cells in rhabdomyosarcomas and rhabdomyosarcoma cell lines." in: Analytical cellular pathology (Amsterdam), 2011

Hrdinka, Dráber, Stepánek, Ormsby, Otáhal, Angelisová, Brdicka, Paces, Horejsí, Drbal: "PRR7 is a transmembrane adaptor protein expressed in activated T cells involved in regulation of T cell receptor signaling and apoptosis." in: The Journal of biological chemistry, Vol. 286, Issue 22, pp. 19617-29, 2011

Buarta, Vinarskuy, Holubcovua, Dole?alovua, Verner, Pospui?ilovua, Dvo?uak, Hampl: "Human Embryonic Stem Cells are Capable of Executing G1/S Checkpoint Activation." in: Stem cells (Dayton, Ohio), 2010

Lukas, Mazna, Valenta, Doubravska, Pospichalova, Vojtechova, Fafilek, Ivanek, Plachy, Novak, Korinek: "Dazap2 modulates transcription driven by the Wnt effector TCF-4." in: Nucleic acids research, Vol. 37, Issue 9, pp. 3007-20, 2009

Kukharskyy, Sulimenko, Mac?rek, Sulimenko, Dráberová, Dráber: "Complexes of gamma-tubulin with nonreceptor protein tyrosine kinases Src and Fyn in differentiating P19 embryonal carcinoma cells." in: Experimental cell research, Vol. 298, Issue 1, pp. 218-28, 2004

Smertenko, Blume, Viklický, Opatrný, Dráber: "Post-translational modifications and multiple tubulin isoforms in Nicotiana tabacum L. cells." in: Planta, Vol. 201, Issue 3, pp. 349-58, 1997

Smertenko, Blume, Viklický, Dráber: "Exposure of tubulin structural domains in Nicotiana tabacum microtubules probed by monoclonal antibodies." in: European journal of cell biology, Vol. 72, Issue 2, pp. 104-12, 1997

Nováková, Dráberová, Schürmann, Czihak, Viklický, Dr-aber: "gamma-Tubulin redistribution in taxol-treated mitotic cells probed by monoclonal antibodies." in: Cell motility and the cytoskeleton, Vol. 33, Issue 1, pp. 38-51, 1996

Linhartová, Dráber, Dráberová, Viklický: "Immunological discrimination of beta-tubulin isoforms in developing mouse brain. Post-translational modification of non-class-III beta-tubulins." in: The Biochemical journal, Vol. 288 ( Pt 3), pp. 919-24, 1993

Dráber, Dráberová, Viklický: "Immunostaining of human spermatozoa with tubulin domain-specific monoclonal antibodies. Recognition of a unique beta-tubulin epitope in the sperm head." in: Histochemistry, Vol. 95, Issue 5, pp. 519-24, 1991

Dráber, Dráberová, Linhartová, Viklický: "Differences in the exposure of C- and N-terminal tubulin domains in cytoplasmic microtubules detected with domain-specific monoclonal antibodies." in: Journal of cell science, Vol. 92 ( Pt 3), pp. 519-28, 1990

Dráber, Dráberová, Zicconi, Sellitto, Viklický, Cappuccinelli: "Heterogeneity of microtubules recognized by monoclonal antibodies to alpha-tubulin." in: European journal of cell biology, Vol. 41, Issue 1, pp. 82-8, 1987

Background publications Miyajima, Maruyama, Nonomura, Hatakeyama: "TRIM36 interacts with the kinetochore protein CENP-H and delays cell cycle progression." in: Biochemical and biophysical research communications, Vol. 381, Issue 3, pp. 383-7, 2009

Honys, R?nuak, Fecikovua, Jedelskuy, Nebesuarovua, Dobrev, Capkovua: "Cytoskeleton-associated large RNP complexes in tobacco male gametophyte (EPPs) are associated with ribosomes and are involved in protein synthesis, processing, and localization." in: Journal of proteome research, Vol. 8, Issue 4, pp. 2015-31, 2009

Bon, Di Carlo, Folgiero, Avetrani, Lazzari, DOrazi, Brizzi, Sacchi, Soddu, Blandino, Mottolese, Falcioni: "Negative regulation of beta4 integrin transcription by homeodomain-interacting protein kinase 2 and p53 impairs tumor progression." in: Cancer research, Vol. 69, Issue 14, pp. 5978-86, 2009

Tsao, Tsai, Tung, Chen, Yue, Liao, Wang, Jiang: "Function of CSE1L/CAS in the secretion of HT-29 human colorectal cells and its expression in human colon." in: Molecular and cellular biochemistry, Vol. 327, Issue 1-2, pp. 163-70, 2009