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MAB1864-I

Sigma-Aldrich

Anti-alpha-Tubulin Antibody, tyrosinated, clone YL1/2

clone YL 1/2, from rat

Synonym(s):

Tubulin alpha-1A chain, Alpha-tubulin 3, Tubulin B-alpha-1, Tubulin alpha-3 chain, alpha-Tubulin, tyrosinated

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rat

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

YL 1/2, monoclonal

species reactivity

yeast, porcine, rat, chicken, bovine, human, mouse

technique(s)

ELISA: suitable
electron microscopy: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
radioimmunoassay: suitable
western blot: suitable

isotype

IgG2aκ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... TUBA1A(7846)

General description

Tubulin alpha-1 chain (UniProt P09733; also known as alpha-tubulin) is encoded by the TUB1 gene (Gene ID 854889) in yeast. Microtubules are dynamic protein filaments involved in a wide variety of cellular activities ranging from mitosis and transport events to cell movement and the maintenance of cell shape. Microtubules are assembled from α- and β-tubulin subunits, both of which are subjected to posttranslational modifications, including the removal of the C-terminus aromatic amino acid from α-tubulin (tyrosine in mammals and phenylalanine in yeast) by carboxypeptidase actifvity. Because the C-terminus tyrosine/phenylalanine is preceded by glutamate (E) residues, the detyrosinated/dephenylalaninated α-tubulin is also referred to as Glu-tubulin. While tyrosine can be reattached to the C-terminus of the Glu-tubulin by tubulin-tyrosine ligase in mammals, phenylalanine is not added posttranslationally to the Glu-tubulin in yeast despite the presence of the yeast YBR094w gene that exhibits significant homology to tubulin-tyrosine ligase in other organisms.

Specificity

Expected to react with a broad range of species based on 100% sequence homology.
Reacts with alpha-tubulin with phenylalanine (yeast) or tyrosine (mammalian and chicken) at the C-terminus (PMID 6204858). Does not react toward posttranslationally modified alpha-tubulin lacking the C-terminus Phe or Tyr.

Immunogen

Epitope: C-terminus
Purified yeast tubulin

Application

Research Category
Cell Structure
Research Sub Category
Adhesion (CAMs)
This Anti-alpha-Tubulin Antibody, tyrosinated, clone YL1/2 is validated for use in Western Blotting, Immunocytochemistry, Immunohistochemistry, Electron Microscopy, ELISA and Radioimmunoassay for the detection of alpha-Tubulin.
Western Blotting Analysis: 1.0 µg/mL from a representative lot detected tyrosinated alpha-tubulin in 10 µg of C2C12 cell lysate.
Immunocytochemistry Analysis: 4.0 µg/mL from a representative lot detected tyrosinated alpha-tubulin in A431, HeLa and HUVEC cells.
Immunocytochemistry Analysis: Representative lots detected phenylalaninated alpha-tubulin immunoreactivity in yeast and tyrosinated alpha-tubulin immunoreactivity in HEK293 cells (Kilmartin J.V., et al. (1982). J Cell Biol. 93(3):576-582; Bandyopadhyay, B., et al. (2007). J Biol Chem. 282(22):16454-16464).
Immunohistochemistry Analysis: A representative lot detected microtubules tyrosinated alpha-tubulin immunoreactivity in mid-streak level section of Hamburger-Hamilton stage 4 (HH4) chick embryos (Nakaya, Y., et al. (2008). Nat. Cell Biol. 10(7):765-775).
Electron Microscopy Analysis: Representative lots detected microtubules phenylalaninated alpha-tubulin immunoreactivity using crude yeast nuclear envelope preparations and microtubules tyrosinated alpha-tubulin immunoreactivity in NIH/3T3 cells (Wehland, J., and Willingham, M.C. (1983). J Cell Biol. 97(5 Pt 1):1476-1490; Kilmartin J.V., et al. (1982). J Cell Biol. 93(3):576-582).
ELISA Analysis: The antigenicity of clone YL1/2 was determined by competitive ELISA using pig brain-derived tubulin against alpha-tubulin peptides with or without Tyr/Phe at the C-terminal end (Wehland, J., et al. (1984). EMBO J. 3(6):1295-1300).
Radioimmunoassay Analysis: The immunoreactivity of clone YL1/2 toward chick brain tubulin and yeast tubulin was determined by radioimmunoassays (Kilmartin J.V., et al. (1982). J Cell Biol. 93(3):576-582).

Quality

Evaluated by Western Blotting in A431 cell lysate.

Western Blotting Analysis: 1.0 µg/mL of this antibody detected tyrosinated alpha-tubulin in 10 µg of A431 cell lysate.

Target description

~55 kDa observed

Physical form

Format: Purified
Protein G Purified
Purified rat monoclonal IgG2aκ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Other Notes

Concentration: Please refer to lot specific datasheet.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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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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A rat monoclonal antibody reacting specifically with the tyrosylated form of alpha-tubulin. II. Effects on cell movement, organization of microtubules, and intermediate filaments, and arrangement of Golgi elements.
Wehland, J; Willingham, MC
The Journal of cell biology null
Pierre Romé et al.
The Journal of cell biology, 189(4), 651-659 (2010-05-19)
Aurora A is a spindle pole-associated protein kinase required for mitotic spindle assembly and chromosome segregation. In this study, we show that Drosophila melanogaster aurora A phosphorylates the dynactin subunit p150(glued) on sites required for its association with the mitotic
Tau aggregation and toxicity in a cell culture model of tauopathy.
Bandyopadhyay, B; Li, G; Yin, H; Kuret, J
The Journal of Biological Chemistry null
RhoA and microtubule dynamics control cell-basement membrane interaction in EMT during gastrulation.
Nakaya, Y; Sukowati, EW; Wu, Y; Sheng, G
Nature Cell Biology null
Robert L Douglas et al.
Journal of cell science, 133(13) (2020-06-07)
Trypanosoma brucei, the causative agent of African sleeping sickness, has a flagellum that is crucial for motility, pathogenicity, and viability. In most eukaryotes, the intraflagellar transport (IFT) machinery drives flagellum biogenesis, and anterograde IFT requires kinesin-2 motor proteins. In this

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