MABS276
Anti-pan polyglycylated Tubulin Antibody, clone AXO 49
clone AXO 49, from mouse
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About This Item
Código UNSPSC:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Productos recomendados
origen biológico
mouse
Nivel de calidad
forma del anticuerpo
purified immunoglobulin
tipo de anticuerpo
primary antibodies
clon
AXO 49, monoclonal
reactividad de especies
Apis, porcine, snail, pig, sea urchin, protista, sheep, mouse, lemur, Drosophila, Paramecium, trout
no debe reaccionar con
Euglena, human (cilia)
técnicas
dot blot: suitable
immunofluorescence: suitable
western blot: suitable
isotipo
IgG1κ
Condiciones de envío
wet ice
modificación del objetivo postraduccional
unmodified
Información sobre el gen
human ... TUBA1A(7846)
Descripción general
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.
Especificidad
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 .
Inmunógeno
Insoluble fraction of Paramecium cilia (Paramecium axonemes)
Aplicación
Detect Tubulin using this mouse monoclonal antibody, Anti-pan polyglycylated Tubulin Antibody, clone AXO 49 validated for use in western blotting, Immunofluorescence & Dot Blot.
Calidad
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.
Descripción de destino
~55 kDa observed
Forma física
Format: Purified
Otras notas
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
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Código de clase de almacenamiento
12 - Non Combustible Liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
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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