A9979
Anti-Aly antibody, Mouse monoclonal
clone 11G5, purified from hybridoma cell culture
Synonym(s):
Anti-mREF1-I
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About This Item
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biological source
mouse
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)
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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Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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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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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