Cat. No.: 302 117
Amount: 100 µg
Price:
$415.00
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| Cat. No. 302 117 |
100 µg purified IgG, lyophilized. Albumin and azide were added for stabilization. For reconstitution add 100 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C to -80°C until use. Antibodies should be stored at +4°C when still lyophilized. Do not freeze! |
| Applications | |
| Clone | YL1-2 |
| Subtype | IgG2a |
| Immunogen | Recombinant protein corresponding to AA 1 to 447 from yeast Tyr-α-tubulin |
| Reactivity |
Reacts with: human, rat (P68370), mouse, vertebrates, invertebrates, yeast. Other species not tested yet. |
| Specificity | Specific for tyrosinated α-tubulin (tyr-tubulin). No cross reaction to glu-α-tubulin. K.O. validated PubMed: 36340693 |
| Data sheet | 302_117.pdf |
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Microtubules are involved in a wide variety of cellular activities ranging from mitosis and transport events to cell movement and the maintainance of cell shape.
Tubulin itself is a globular protein which consists of two polypeptides, α-tubulin and β-tubulin. α- and β-tubulin dimers are assembled to 13 protofilaments that form a microtubule of 22 nm diameter. Tyrosine ligase ads a C-terminal tyrosin to monomeric α-tubulin.
Assembled microtubules can again be detyrosinated by a cytoskeleton associated carboxypeptidase. Detyrosinated α-tubulin is referred to as Glu-α-tubulin. Another post-translational modification of detyrosinated α-tubulin is C-terminal polyglutamylation which is characteristic for microtubules in neuronal cells and the mitotic spindle. A third variant of detyrosinated α-tubulin is Δ2-tubulin which lacks the C-terminal glutamic acid. It cannot be tyrosinated by tyrosine ligase and is one of the dominant α-tubulin isoforms in neurons.