Home|||||||Technical Support|

alpha-Tubulin - 302 217

A major cytoskeleton protein
Monoclonal rat purified IgG
Cat. No.: 302 217
Amount: 100 µg
Price: $415.00
Cat. No. 302 217 100 µg purified IgG, lyophilized. Azide was added before lyophilization. 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.
Applications WB: 1 : 1000 up to 1 : 5000 (AP staining) gallery  
IP: not tested yet
ICC: 1 : 200 up to 1 : 500 gallery  
IHC: 1 : 400 gallery  
IHC-P/FFPE: not tested yet
Clone 37B5
Subtype IgG1
Immunogen Synthetic peptide corresponding to AA 443 to 449 from rat α-Tubulin 1A (UniProt Id: P68370-1)
Epitop Epitop: AA 443 to 449 from rat α-Tubulin 1A (UniProt Id: P68370-1)
Reactivity Reacts with: mammals, chicken.
Other species not tested yet.
Specificity Specific for α-tubulin.
Data sheet 302_217.pdf

References for alpha-Tubulin - 302 217

Developmental switch in the kinase dependency of long-term potentiation depends on expression of GluA4 subunit-containing AMPA receptors.
Luchkina NV, Huupponen J, Clarke VR, Coleman SK, Keinänen K, Taira T, Lauri SE
Proceedings of the National Academy of Sciences of the United States of America (2014) 11111: 4321-6. 302 217 WB; tested species: mouse,rat
Ongoing intrinsic synchronous activity is required for the functional maturation of CA3-CA1 glutamatergic synapses.
Huupponen J, Molchanova SM, Lauri SE, Taira T
Cerebral cortex (New York, N.Y. : 1991) (2013) 2311: 2754-64. 302 217 WB; tested species: rat
Cat. No.: 302 217
Quantity: 100 µg
Price: $415.00
Developmental switch in the kinase dependency of long-term potentiation depends on expression of GluA4 subunit-containing AMPA receptors.
Luchkina NV, Huupponen J, Clarke VR, Coleman SK, Keinänen K, Taira T, Lauri SE
Proceedings of the National Academy of Sciences of the United States of America (2014) 11111: 4321-6. 302 217 WB; tested species: mouse,rat
Ongoing intrinsic synchronous activity is required for the functional maturation of CA3-CA1 glutamatergic synapses.
Huupponen J, Molchanova SM, Lauri SE, Taira T
Cerebral cortex (New York, N.Y. : 1991) (2013) 2311: 2754-64. 302 217 WB; tested species: rat
Background

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.