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C9367

Sigma-Aldrich

Anti-CUGBP2 antibody, Mouse monoclonal

clone HL1889 (1H2-1F12), purified from hybridoma cell culture

Synonym(s):

Anti-CUG Triplet Repeat, RNA-binding protein 2, Anti-ETR3, RNA-binding protein

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200 μL
$670.00

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200 μL
$670.00

About This Item

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

$670.00


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Request a Bulk Order

biological source

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

HL1889 (1H2-1F12), monoclonal

form

buffered aqueous solution

mol wt

antigen ~52 kDa

species reactivity

mouse, human, chicken

concentration

~1.5 mg/mL

technique(s)

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: 30-40 μg/mL using total cell extract of mouse heart

isotype

IgG1

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

chicken ... CUGBP2(374111)
human ... CUGBP2(10659)
mouse ... Cugbp2(14007)

Immunogen

divergent domain of human CUGBP2 corresponding to amino acids 209-415 (accession no. NP006552).

Application

Suitable for immunocytochemistry, immunoprecipitation and western blotting at a working concentration of 30-40 μg/mL using total cell extract of mouse heart.

Biochem/physiol Actions

CUGBP2 is an RNA-binding protein that specifically binds to CUG repeat sequences and is responsible for the regulation of both nuclear and cytoplasmic RNA processing events such as alternative splicing, RNA editing, mRNA stability, and translation. It is mainly expressed in muscle and brain. It regulates a specific alternative slicing of exons 5 and 21 of the N-methyl-D-aspartate receptor 1 (NMDA R1) RNA in rat. It binds to U/G-rich motifs within muscle specific enhancer elements (MSEs) and activates inclusion of an alternative exon in cardiac troponin T (cTNT) pre-mRNAs. It interacts with A/U rich sequences in the 3′ UTR and inhibits translation of cycloxygenase-2 (COX-2) mRNAs.

Target description

CUGBP2 is an RNA-binding protein that specificallybinds to CUG repeat sequences.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 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

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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Astrid-Solveig Schultz et al.
Molecular and cellular biology, 37(7) (2016-12-30)
Cell-type-specific and inducible alternative splicing has a fundamental impact on regulating gene expression and cellular function in a variety of settings, including activation and differentiation. We have recently shown that activation-induced skipping of TRAF3 exon 8 activates noncanonical NF-κB signaling
Andrea N Ladd et al.
Journal of cell science, 117(Pt 16), 3519-3529 (2004-07-01)
Embryonic lethal abnormal vision (ELAV) type RNA binding protein 3 (ETR-3; also called NAPOR, CUGBP2, or BRUNOL3) has been implicated in the regulation of nuclear and cytoplasmic RNA processing events, including alternative splicing, RNA editing, stability and translation. Here, we
Debnath Mukhopadhyay et al.
Molecular cell, 11(1), 113-126 (2003-01-22)
Cyclooxygenase-2 (COX-2) expression is translationally silenced in epithelial cells undergoing radiation-induced apoptosis. CUGBP2, a predominantly nuclear protein, is also rapidly induced in response to radiation and translocates to the cytoplasm. Antisense-mediated suppression of CUGBP2 renders radioprotection through a COX-2-dependent prostaglandin
Wenqing Zhang et al.
RNA (New York, N.Y.), 8(5), 671-685 (2002-05-23)
Alternative RNA splicing generates extensive proteomic diversity in the nervous system, yet few neural-specific RNA binding proteins have been implicated in splicing control. Here we show that the biochemical properties and spatial expression of mouse neuroblastoma apoptosis-related RNA-binding protein (NAPOR;
A N Ladd et al.
Molecular and cellular biology, 21(4), 1285-1296 (2001-02-07)
Alternative splicing of cardiac troponin T (cTNT) exon 5 undergoes a developmentally regulated switch such that exon inclusion predominates in embryonic, but not adult, striated muscle. We previously described four muscle-specific splicing enhancers (MSEs) within introns flanking exon 5 in

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