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Details for Product No. ABIN93891

Tubulin, alpha 1B (TUBA1B) antibody

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Antigen
Synonyms Tuba2, TUBA3, K-ALPHA-1, tuba, tuba1, k-alpha-1, RGD1565476, TUBAT
Reactivity
»Alternatives Various Species
Host
»Alternatives Mouse
Clonality (Clone) Monoclonal ()
Conjugate
»Alternatives Un-conjugated
Application
»Alternatives Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)), Immunocytochemistry (ICC)
Pubmed 17 references available
Catalog no. ABIN93891
Quantity 0.1 mg
Price
333.96 $   Plus shipping costs $45.00
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Availability Will be delivered in 4 to 5 Business Days
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 structuraldomain of alpha-tubulin.
Purification Purified from ascites by precipitation methods.
Purity > 95% (by SDS-PAGE)
Alternative Name alpha-tubulin
Background The microtubules are intracellular dynamic polymers made up of evolutionarily conservedpolymorphic alpha/beta-tubulin heterodimers and a large number of microtubule-associatedproteins (MAPs). The microtubules consist of 13 protofilaments and have an outer diameter25 nm. Microtubules have their intrinsic polarity, highly dynamic plus ends and less dynamicminus ends. Microtubules are required for vital processes in eukaryotic cells includingmitosis, meiosis, maintenance of cell shape and intracellular transport. Microtubules are alsonecessary for movement of cells by means of flagella and cilia. In mammalian tissue culturecells microtubules have their minus ends anchored in microtubule organizing centers(MTOCs).The GTP (guanosintriphosphate) molecule is an essential for tubulin heterodimerto associate with other heterodimers to form microtubule. In vivo, microtubule dynamics varyconsiderably. Microtubule polymerization is reversible and a populations of microtubules incells are on their minus ends either growing or shortening this phenomenon is calleddynamic instability of microtubules. On a practical level, microtubules can easily bestabilized by the addition of non-hydrolysable analogues of GTP (eg. GMPPCP) or morecommonly by anti-cancer drugs such as Taxol. Taxol stabilizes microtubules at roomtemperature for many hours. Using limited proteolysis by enzymes both tubulin subunits canbe divided into N-terminal and C-terminal structural domains.The alpha-tubulin (relative molecular weight around 50 kDa) is globular protein that existsin cells as part of soluble alpha/beta-tubulin dimer or it is polymerized into microtubules. Indifferent species it is coded by multiple tubulin genes that form tubulin classes (in human 6genes). Expressed tubulin genes are named tubulin isotypes. Some of the tubulin isotypesare expressed ubiquitously, while some have more restricted tissue expression.Alpha-tubulin is also subject of numerous post-translational modifications. Tubulin isotypesand their posttranslational modifications are responsible for multiple tubulin charge variants -tubulin isoforms. Heterogeneity of alpha-tubulin is concentrated in C-terminal structuraldomain.
Research Area Cytoskeleton
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 Proteaseinhibitor Cocktail). Incubate 60 min on ice. Centrifuge to remove cell debris. Mix lysate withreducing 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
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
Storage 4 °C
Storage Comment Do not freeze. Do not use after expiration date stamped on vial label.
Product cited in: Cancer: Krupkova, Loja, Redova et al.: "Analysis of nuclear nestin localization in cell lines derived from neurogenic tumors." in: Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine, 2011 (PubMed). Method employed by authors: Immunohistochemistry (IHC) (Sample species: Human).

Hrdinka, Dráber, Stepánek et al.: "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).

Sana, Zambo, Skoda et al.: "CD133 expression and identification of CD133/nestin positive cells in rhabdomyosarcomas and rhabdomyosarcoma cell lines." in: Analytical cellular pathology (Amsterdam), 2011 (PubMed).

Lueck, Hennig, Lommatzsch et al.: "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 et al.: "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).

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 et al.: "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 et al.: "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).

Smertenko, Blume, Viklický et al.: "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 et al.: "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).

Tsao, Tsai, Tung et al.: "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 (PubMed).

Miyajima, Maruyama, Nonomura et al.: "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 (PubMed).

Lukas, Mazna, Valenta et al.: "Dazap2 modulates transcription driven by the Wnt effector TCF-4." in: Nucleic acids research, Vol. 37, Issue 9, pp. 3007-20, 2009 (PubMed).

Bon, Di Carlo, Folgiero et al.: "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 (PubMed).

Honys, R?nuak, Fecikovua et al.: "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 (PubMed).

Buarta, Vinarskuy, Holubcovua et al.: "Human Embryonic Stem Cells are Capable of Executing G1/S Checkpoint Activation." in: Stem cells (Dayton, Ohio), 2010 (PubMed).

Pospichalova, Tureckova, Fafilek et al.: "Generation of two modified mouse alleles of the Hic1 tumor suppressor gene." in: Genesis (New York, N.Y. : 2000), 2011 (PubMed).

Alternatives for antigen "Tubulin, alpha 1B (TUBA1B)", type "Antibodies"
Hosts (91), (33), (10), (8), (2)
Reactivities (90), (45), (37), (28), (26), (12), (11), (8), (7), (7), (6), (5), (5), (5), (4), (4), (3), (3), (3), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1)
Applications (125), (54), (50), (47), (42), (38), (20), (9), (8), (7), (5), (2), (1), (1), (1)
Conjugates (10), (6), (3), (3), (2), (1), (1), (1), (1)
Epitopes (12), (10), (7), (6), (5), (2), (2), (1), (1), (1)
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