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Merck
모든 사진(5)

Key Documents

MAB1864-I

Sigma-Aldrich

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

clone YL 1/2, from rat

동의어(들):

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 코드:
12352203
eCl@ss:
32160702
NACRES:
NA.41

생물학적 소스

rat

Quality Level

항체 형태

purified immunoglobulin

항체 생산 유형

primary antibodies

클론

YL 1/2, monoclonal

종 반응성

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

기술

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

동형

IgG2aκ

NCBI 수납 번호

UniProt 수납 번호

배송 상태

wet ice

타겟 번역 후 변형

unmodified

유전자 정보

human ... TUBA1A(7846)

일반 설명

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.

특이성

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.

면역원

Epitope: C-terminus
Purified yeast tubulin

애플리케이션

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).

품질

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.

표적 설명

~55 kDa observed

물리적 형태

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.

저장 및 안정성

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

기타 정보

Concentration: Please refer to lot specific datasheet.

면책조항

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


시험 성적서(COA)

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문서 라이브러리 방문

J Wehland et al.
The EMBO journal, 3(6), 1295-1300 (1984-06-01)
We have characterized the epitope of the rat monoclonal antibody YL 1/2 in detail using synthetic peptides and several alpha-tubulin derivatives. The epitope seems to be provided by the linear sequence spanning the carboxy-terminal residues of tyrosinated alpha-tubulin. By competitive
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
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
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

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