|Application ||WB, E|
|Other Accession||Q7ZXE2, Q792H5, Q9Z0H4, Q6P0B1, Q7T2T1, Q4QQT3, P28659, Q92879, Q9IBD0, Q5F3T7, Q6PF35, O57406, NP_001020247.1, NP_001020248.1|
|Predicted||Xenopus, Chicken, Zebrafish, Mouse, Rat|
|Calculated MW||54285 Da|
|Antigen Region||481-508 aa|
|Other Names||CUGBP Elav-like family member 2, CELF-2, Bruno-like protein 3, CUG triplet repeat RNA-binding protein 2, CUG-BP2, CUG-BP- and ETR-3-like factor 2, ELAV-type RNA-binding protein 3, ETR-3, Neuroblastoma apoptosis-related RNA-binding protein, hNAPOR, RNA-binding protein BRUNOL-3, CELF2, BRUNOL3, CUGBP2, ETR3, NAPOR|
|Target/Specificity||This CUGBP2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 481-508 amino acids from the C-terminal region of human CUGBP2.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||CUGBP2 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||BRUNOL3, CUGBP2, ETR3, NAPOR|
|Function||RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of TNNT2 in embryonic, but not adult, skeletal muscle. Activates TNNT2 exon 5 inclusion by antagonizing the repressive effect of PTB. Acts as both an activator and repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs. Promotes inclusion of exonS 21 and exclusion of exon 5 of the NMDA receptor R1 pre- mRNA. Involved in the apoB RNA editing activity. Increases COX2 mRNA stability and inhibits COX2 mRNA translation in epithelial cells after radiation injury (By similarity). Modulates the cellular apoptosis program by regulating COX2-mediated prostaglandin E2 (PGE2) expression (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK. Binds to the muscle-specific splicing enhancer (MSE) intronic sites flanking the TNNT2 alternative exon 5. Binds preferentially to UG-rich sequences, in particular UG repeat and UGUU motifs. Binds to apoB mRNA, specifically to AU-rich sequences located immediatly upstream of the edited cytidine. Binds AU-rich sequences in the 3'-UTR of COX2 mRNA (By similarity). Binds to an intronic RNA element responsible for the silencing of exon 21 splicing (By similarity). Binds to (CUG)n repeats (By similarity).|
|Cellular Location||Nucleus. Cytoplasm. Note=Accumulates in the cytoplasm after ionizing radiation (By similarity). Colocalizes with APOBEC1 and A1CF. RNA-binding activity is detected in both nuclear and cytoplasmic compartments.|
|Tissue Location||Expressed in frontal cortex. Isoform 1 is expressed in brain and lung. Isoform 2 is expressed in heart, brain, placenta, lung, liver, kidney, skeletal muscle and pancreas. Isoform 4 is expressed in heart, lung, skeletal muscle, kidney and pancreas.|
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Provided below are standard protocols that you may find useful for product applications.
Members of the CELF/BRUNOL protein family contain two N-terminal RNA recognition motif (RRM) domains, one C-terminal RRM domain, and a divergent segment of 160-230 aa between the second and third RRM domains. Members of this protein family regulate pre-mRNA alternative splicing and may also be involved in mRNA editing, and translation. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq].
Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Talmud, P.J., et al. Am. J. Hum. Genet. 85(5):628-642(2009)
Anney, R.J., et al. Am. J. Med. Genet. B Neuropsychiatr. Genet. 147B (8), 1369-1378 (2008) :
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