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T9154-01H Mouse Anti-Tubulin, alpha (Alpha Tubulin, Tubulin alpha Ubiquitous, H2-Alpha, K-alpha-1, TUBA3, Tubulin alpha 1 Chain, TUBA1, TUBA1A, Tubulin K alpha 1)

Specifications
References
Clone Type
Monoclonal
Host
Mouse
Source
Porcine
Swiss Prot
Q71U36
Isotype
IgM
Clone Number
TU-02
Grade
Purified
Applications
WB
Crossreactivity
Hu Mo Po
Gene ID
7277
Shipping Temp
Blue Ice
Storage Temp
-20°C

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 ~50kD) 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.
Applications
Suitable for use in Western Blot. Other applications not tested.
Recommended Dilution
Western Blot: 1-2ug/ml, reducing conditions. Not suitable for use in non-reducing conditions on RIPA cell extracts. Optimal dilutions to be determined by the researcher.
Storage and Stability
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Immunogen
Microtubule proteins from porcine brain
Form
Supplied as a liquid in TBS, pH 8.0, 0.09% sodium azide.
Purity
Purified
Specificity
Recognizes an epitope on N-terminal structural domain of alpha-tubulin in various species. Species Crossreactivity: porcine, human, mouse and Nicotiana
References
1. Dráber, P. et al., Heterogeneity of microtubules recognizied by monoclonal antibodies to alpha-tubulin. Eur.J.Cell.Biol. (1986) 41: 82-88. 2. Dráber, P. et al., Immunohistochemical heterogeneity of alpha-tubulin in human epithelia revealed with monoclonal antibodies. Histochemistry (1987) 87: 151-155. 3. Dráber, P. et al., Differences in the exposure of C- and N-terminal tubulin domains in cytoplasmic microtubules detected with domain-specific monoclonal antibodies. J. Cell Science (1989) 92: 519-528. 4. Smertenko et al., Exposure of tubulin structural domains in Nicotiana tabacum microtubules probed by monoclonal antibodies. Eur. J. Cell. Biol. (1997) 72: 104-112.
USBio References
No references available
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