alpha Tubulin Antikörper

Produktnummer ABIN93891

Produktdetails anti-alpha Tubulin Antikörper

Target: alpha Tubulin (TUBA1)

Reaktivität: Human, Maus, Schwein, Saccharomyces cerevisiae, Arabidopsis, Nicotiana tabacum, Pute, Paramecium, Eisenia fetida

Wirt: Maus

Klonalität: Monoklonal

Konjugat: Dieser alpha Tubulin Antikörper ist unkonjugiert

Applikation: Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Immunocytochemistry (ICC), Immunoprecipitation (IP), Flow Cytometry (FACS)

Spezifität: The antibody TU-01 recognizes a defined epitope (aa 65-97) on N-terminal structural domain of alpha-tubulin.

Kreuzreaktivität (Details): Broad species reactivity

Aufreinigung: Purified by protein-A affinity chromatography.

Reinheit: > 95 % (by SDS-PAGE)

Immunogen: Fraction of tubulin purified from porcine brain by two cycles of polymerization - depolymerization.

Klon: TU-01

Isotyp: IgG1

Anwendungsinformationen

Applikationshinweise: Flow cytometry: Recommended dilution: 1-4 μg/mL, intracellular staining.
Western blotting: Recommended dilution: 1-2 μg/mL, reducing conditions.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Konzentration: 1 mg/mL

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

Konservierungsmittel: Sodium azide

Vorsichtsmaßnahmen: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Handhabung: Do not freeze.

Lagerung: 4 °C

Informationen zur Lagerung: Store at 2-8°C. Do not freeze.

Referenzen für anti-alpha Tubulin Antikörper (ABIN93891)

Peskova, Cerna, Oppelt, Mraz, Barta: "Oct4-mediated reprogramming induces embryonic-like microRNA expression signatures in human fibroblasts." in: Scientific reports, Vol. 9, Issue 1, pp. 15759, (2019) (PubMed).

Bohaciakova, Renzova, Fedorova, Barak, Kunova Bosakova, Hampl, Cajanek: "An Efficient Method for Generation of Knockout Human Embryonic Stem Cells Using CRISPR/Cas9 System." in: Stem cells and development, Vol. 26, Issue 21, pp. 1521-1527, (2018) (PubMed).

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) (PubMed).

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) (PubMed).

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) (PubMed).

Krupkova, Loja, Redova, Neradil, Zitterbart, Sterba, Veselska: "Analysis of nuclear nestin localization in cell lines derived from neurogenic tumors." in: Tumour biology, (2011) (PubMed).

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) (PubMed).

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) (PubMed).

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) (PubMed).

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) (PubMed).

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) (PubMed).

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) (PubMed).

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) (PubMed).

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) (PubMed).

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) (PubMed).

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) (PubMed).

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) (PubMed).

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) (PubMed).

Grimm, Breitling, Little: "Location of the epitope for the alpha-tubulin monoclonal antibody TU-O1." in: Biochimica et biophysica acta, Vol. 914, Issue 1, pp. 83-8, (1987) (PubMed).

Viklický, Dráber, Hasek, Bártek: "Production and characterization of a monoclonal antitubulin antibody." in: Cell biology international reports, Vol. 6, Issue 8, pp. 725-31, (1982) (PubMed).

Details zu alpha Tubulin

Target: alpha Tubulin (TUBA1)

Andere Bezeichnung: alpha-tubulin (TUBA1 Produkte)

Synonyme: Tuba1 antikoerper, K-ALPHA-1 antikoerper, Tuba-1 antikoerper, cb944 antikoerper, fb22g06 antikoerper, tuba1 antikoerper, wu:fb22g06 antikoerper, Calpha1 antikoerper, tubulin, alpha 1A antikoerper, tubulin alpha 1b antikoerper, tubulin, alpha 1b antikoerper, tubulin, alpha 1B antikoerper, Tuba1a antikoerper, TUBA1B antikoerper, tuba1b antikoerper, Tuba1b antikoerper

Hintergrund: Tubulin alpha 1,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.,TUBA

Gen-ID: 7277

UniProt: Q71U36

Pathways: Microtubule Dynamics