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Polyglutamylated Tubulin; Glutamylated Tubulin; Postranslational Protein Glutamylation

Monoclonal Antibody

GT335

Mouse IgG1κ

Purified from concentrated hybridoma tissue culture supernatant.

Octapeptide EGEGE*EEG, modified by the addition of two glutamyl units onto the fifth E (indicated by an asterisk).

Biotin

Immunocytochemistry: (1:2000)Immunohistochemistry: (paraffin sections; 1:1000)Immunoprecipitation Western Blot: (1:4000) Optimal conditions must be determined individually for each application.

All

Recognizes the posttranslational modification (poly)glutamylation on proteins. Reacts with polyglutamylated α- and β-tubulin.

≥95% (SDS-PAGE)

Protein G-affinity purified.

1mg/ml

Liquid. In PBS containing 0.02% sodium azide.

Recognizes most forms of polyglutamylated tubulin (α- and β-tubulin), independent of the length of the glutamate side chains. No specificity to particular tubulin isoforms nor to tubulin from particular species are observed. Detects also other (poly)glutamylated proteins. Since no consensus modification site is known for protein (poly)glutamylation, the detection is not sequence-specific. However, an acidic environment of the modification site is required. The use of the antibody at too high concentrations obscures its specificity in immunofluorescence.

BLUE ICE

+4°C

-20°C

After opening, prepare aliquots and store at -20°C.Avoid freeze/thaw cycles.

Stable for at least 1 year after receipt when stored at -20°C.

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Polyglutamylation is a post-translational modification in which glutamate side chains of variable lengths are formed on the modified protein. It is evolutionarily conserved and the most prominent substrate is tubulin, the microtubule (MT) building block. Polyglutamylation has been proposed to be involved in the functional adaptation of MTs, as it occurs within the carboxy-terminal tubulin tails that participate directly in the binding of many structural and motor MT-associated proteins. The recent identification of new substrates of polyglutamylation indicates that this post-translational modification could be a potential regulator of diverse cellular processes and be involved in cell cycle and cell proliferation.

Product References

Distribution of glutamylated alpha and beta-tubulin in mouse tissues using a specific monoclonal antibody, GT335: A. Wolff, et al.; Eur. J. Cell Biol. 59, 425 (1992)

Polyglutamylation of nucleosome assembly proteins: C. Regnard, et al.; J. Biol. Chem. 275, 15969 (2000)

Glutamylated tubulin: diversity of expression and distribution of isoforms: M.L. Kann, et al.; Cell Motil. Cytoskeleton 55, 14 (2003)

Polyglutamylation Is a Post-translational Modification with a Broad Range of Substrates: J. van Dijk, et al.; J. Biol. Chem. 283, 3915 (2008)

Unique post-translational modifications in specialized microtubule architecture: K. Ikegami & M. Setou; Cell Struct. Funct. 35, 15 (2010) (Review)

Tubulin detyrosination promotes monolayer formation and apical trafficking in epithelial cells: S. Zink|et al.; J. Cell Sci. 125, 5998 (2012)

Microtubule detyrosination guides chromosomes during mitosis: M. Barisic, et al.; Science 348, 6236 (2015) (Supplement)

Loss of RPGR glutamylation underlies the pathogenic mechanism of retinal dystrophy caused by TTLL5 mutations: X. Sun, et al.; PNAS 113, E2925 (2016)

Alterations in the balance of tubulin glycylation and glutamylation inphotoreceptors leads to retinal degeneration: M. Bosch Grau, et al.; J. Cell. Sci. 130, 938 (2017)

The actin-MRTF-SRF transcriptional circuit controls tubulin acetylation via α-TAT1 gene expression: J. Fernández-Barrera, et al.; J. Cell Biol. ahead of print (2018)

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