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A9979

Sigma-Aldrich

Anti-Aly antibody, Mouse monoclonal

clone 11G5, purified from hybridoma cell culture

Synonym(s):

Anti-mREF1-I

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About This Item

MDL number:
MFCD07785404
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

Quality Level

200

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

11G5, monoclonal

form

buffered aqueous solution

mol wt

antigen ~30 kDa

species reactivity

Xenopus, human

concentration

~2 mg/mL

technique(s)

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
microarray: suitable
western blot: 0.5-1 μg/mL using total cell extract of HeLa cells

isotype

IgG1

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... THOC4(10189)

General description

Aly is a nuclear chaperone protein that may modulate DNA binding, mRNA synthesis, and dimerization of basic region-leucine zipper proteins. Mouse Monoclonal Anti-Aly antibody recognizes human and Xenopus Aly.
Anti-Aly antibody, Mouse monoclonal (mouse IgG1 isotype) is derived from the 11G5 hybridoma produced by the fusion of mouse myeloma cells (SP2/O) and splenocytes from BALB/c mice immunized with recombinant human Aly/REF protein. Aly is also known as mREF1-I which is an RNA-binding protein that contains an RNA-binding domain and is recruited to the mRNA-protein complex (mRNP) complexes during the mRNA splicing.

Immunogen

recombinant human Aly/REF protein.

Application

Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Co-immunoprecipitation and western blot studies were performed in Hela cells using a monoclonal mouse anti-Aly antibody. The results indicated that Aly which was observed as a 30 kDa band interacted with the Herpes Simplex Virus I protein, ICP27.
Mouse Monoclonal Anti-Aly antibody can be used for immunocytochemistry, immunoprecipitation, indirect ELISA, microarray and western blot (0.5-1.0μg/ml) assays.

Biochem/physiol Actions

Excess of recombinant expression of Aly in the cells increases both the rate and efficiency of spliced and unspliced mRNA export (in vivo) from the nucleus to the cytoplasm. Aly is dissociated from the mRNAs after the export to the cytoplasm.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, and 15 mM sodium azide.

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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Certificates of Analysis (COA)

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Messenger-RNA-binding proteins and the messages they carry
Dreyfuss G, et al.
Nature Reviews in Molecular and Cell Biology, 3(3), 195-195 (2002)
The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans
Zhou Z, et al.
Nature, 407(6802), 401-401 (2000)
V N Kim et al.
The EMBO journal, 20(8), 2062-2068 (2001-04-11)
We recently described an RNA-binding protein, Y14, that binds preferentially to spliced mRNAs and persists in the cytoplasm. Y14 is part of a multi-protein complex that also contains the mRNA export factor TAP. This suggests that splicing imprints the mRNA
Kara A Corbin-Lickfett et al.
Journal of virology, 84(5), 2212-2222 (2009-12-18)
Herpes simplex virus 1 (HSV-1) protein ICP27 is a multifunctional regulatory protein that is phosphorylated. Phosphorylation can affect protein localization, protein interactions, and protein function. The major sites of ICP27 that are phosphorylated are serine residues 16 and 18, within
Eleonora Zonta et al.
Nucleic acids research, 41(1), 554-564 (2012-11-13)
It is widely accepted that pre-mRNA maturation, including splicing, is tightly coupled to both transcription and mRNA export, but factors linking the three processes are less understood. By analysing the estrogen-regulated expression of the c-fos mRNA that is processed during
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