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Tyr-alpha-tubulin antibody - 302 117 K.O.

alpha-Tubulin is a major cytoskeleton protein
Rat monoclonal purified IgG
Cat. No.: 302 117
Amount: 100 µg
Price: $415.00
Cat. No. 302 117 100 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.
Antibodies should be stored at +4°C when still lyophilized. Do not freeze!
Applications
 
WB: 1 : 1000 up to 1 : 5000 (AP staining) gallery  
IP: yes
ICC: 1 : 500 gallery  
IHC: 1 : 500 gallery  
IHC-P: 1 : 200 up to 1 : 1000 gallery  
Clone YL1-2
Subtype IgG2a
Immunogen Recombinant protein corresponding to AA 1 to 447 from yeast Tyr-α-tubulin
Epitop maps to the last 8 residues (GEEEGEEY) at thecarboxy terminus of alpha tubulin when tyrosinated
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

References for Tyr-alpha-tubulin - 302 117

The role of α-tubulin tyrosination in controlling the structure and function of hippocampal neurons.
Hosseini S, van Ham M, Erck C, Korte M, Michaelsen-Preusse K
Frontiers in molecular neuroscience (2022) 15: 931859. 302 117 WB, IHC; KO verified; tested species: mouse
Parallel kinase pathways stimulate actin polymerization at depolarized mitochondria.
Fung TS, Chakrabarti R, Kollasser J, Rottner K, Stradal TEB, Kage F, Higgs HN
Current biology : CB (2022) 327: 1577-1592.e8. 302 117 WB; tested species: human,mouse
The role of α-tubulin tyrosination in controlling the structure and function of hippocampal neurons.
Hosseini S, van Ham M, Erck C, Korte M, Michaelsen-Preusse K
Frontiers in molecular neuroscience (2022) 15: 931859. 302 117 WB, IHC; KO verified; tested species: mouse
Cat. No.: 302 117
Amount: 100 µg
Price: $415.00
The role of α-tubulin tyrosination in controlling the structure and function of hippocampal neurons.
Hosseini S, van Ham M, Erck C, Korte M, Michaelsen-Preusse K
Frontiers in molecular neuroscience (2022) 15: 931859. 302 117 WB, IHC; KO verified; tested species: mouse
Parallel kinase pathways stimulate actin polymerization at depolarized mitochondria.
Fung TS, Chakrabarti R, Kollasser J, Rottner K, Stradal TEB, Kage F, Higgs HN
Current biology : CB (2022) 327: 1577-1592.e8. 302 117 WB; tested species: human,mouse
The role of α-tubulin tyrosination in controlling the structure and function of hippocampal neurons.
Hosseini S, van Ham M, Erck C, Korte M, Michaelsen-Preusse K
Frontiers in molecular neuroscience (2022) 15: 931859. 302 117 WB, IHC; KO verified; tested species: mouse
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.