MABS276
Anti-pan polyglycylated Tubulin Antibody, clone AXO 49
clone AXO 49, from mouse
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
AXO 49, monoclonal
species reactivity
Apis, porcine, snail, pig, sea urchin, protista, sheep, mouse, lemur, Drosophila, Paramecium, trout
should not react with
Euglena, human (cilia)
technique(s)
dot blot: suitable
immunofluorescence: suitable
western blot: suitable
isotype
IgG1κ
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... TUBA1A(7846)
General description
Several post-translational modifications of tubulin have been identified in eukaryotic cells. Glycylation is a poly-modification which occurs as lateral branching of glycine chains of variable length identified in axonemal tubulin of Paramecium cilia. This modification has been detected on tubulin and/or cilia/flagella of many unicellular and pluricellular organisms. The differential distribution of distinct polyglycylated tubulin isoforms between cytoplasmic and axonemal compartments indicates that polyglycylation levels of tubulin is highly regulated at the cell level. The AXO49 antibody is reactive mainly on axonemal tubulin of motile cilia and flagella which are polyglycylated. In some cases, reactivity may also be observed on other very stable microtubule networks. This antibody is useful for cilia and flagella detection.
Specificity
This antibody recognizes the lateral connecting branches of a polymer, which contains at least 3 glycine residues. This antibody demonstrates cross reactivity against polyglycylated tubulin, as well as with other polyglycylated proteins .
Immunogen
Insoluble fraction of Paramecium cilia (Paramecium axonemes)
Application
Detect Tubulin using this mouse monoclonal antibody, Anti-pan polyglycylated Tubulin Antibody, clone AXO 49 validated for use in western blotting, Immunofluorescence & Dot Blot.
Quality
Evaluated by Western Blotting on total cytoskeletal proteins of Paramecium. : A 1:50,000 dilution of this antibody detected polyglycylated Tubulin in 10 µg of Paramecium total cytoskeletal proteins.
Target description
~55 kDa observed
Physical form
Format: Purified
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Giardia duodenalis 14-3-3 protein is polyglycylated by a tubulin tyrosine ligase-like member and deglycylated by two metallocarboxypeptidases.
Lalle, Marco, et al.
The Journal of Biological Chemistry, 286, 4471-4484 (2011)
C Bressac et al.
European journal of cell biology, 67(4), 346-355 (1995-08-01)
Using two antibodies raised against Paramecium axonemal tubulin, a monoclonal antibody, AXO 49 (Callen et al., Biol. Cell 81, 95-119 (1994)), and a polyclonal antibody, PAT (Cohen et al., Biol. Cell 44, 35-44 (1982)), which have been shown elsewhere to
Polyglycylation of tubulin: a posttranslational modification in axonemal microtubules.
Redeker, V, et al.
Science (New York, N.Y.), 266, 1688-1691 (1994)
Krzysztof Rogowski et al.
Cell, 137(6), 1076-1087 (2009-06-16)
Polyglycylation is a posttranslational modification that generates glycine side chains on proteins. Here we identify a family of evolutionarily conserved glycine ligases that modify tubulin using different enzymatic mechanisms. In mammals, two distinct enzyme types catalyze the initiation and elongation
A M Callen et al.
Biology of the cell, 81(2), 95-119 (1994-01-01)
Ciliates are very good models for studying post-translationally generated tubulin heterogeneity because they exhibit highly differentiated microtubular networks in combination with reduced genetic diversity. We have approached the analysis of tubulin heterogeneity in Paramecium through extensive isolation and characterization of
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