CELF1 antibody (CUGBP, Elav-Like Family Member 1) (N-Term)

Details for Product anti-CELF1 Antibody No. ABIN965946, Supplier: Log in to see
Antigen
  • CUGBP1
  • BRUNOL2
  • CUG-BP
  • CUGBP
  • EDEN-BP
  • NAB50
  • NAPOR
  • hNab50
  • 1600010O03Rik
  • AA407467
  • Brunol2
  • CUG-BP1
  • Cugbp1
  • D2Wsu101e
  • HNAB50
  • Bruno-like
  • brul
  • cb920
  • cugbp1
  • brunol2
  • cug-bp
  • cug-bp1
  • cugbp
  • cugbp1-a
  • eden-bp
  • edenbp
  • nab50
  • CUGBP, Elav-like family member 1
  • cugbp, Elav-like family member 1
  • CELF1
  • Celf1
  • celf1
  • celf1-a
Alternatives
anti-Cow (Bovine) CELF1 antibody for Immunofluorescence
Epitope
N-Term
17
14
3
3
3
3
2
1
1
1
1
1
1
Reactivity
Human, Mouse (Murine), Rat (Rattus)
85
47
43
25
22
20
18
4
4
2
2
2
1
1
1
1
Host
Rabbit
57
28
Clonality
Polyclonal
Conjugate
This CELF1 antibody is un-conjugated
3
3
3
3
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
Application
Immunohistochemistry (IHC)
78
39
29
28
28
19
16
15
5
2
2
1
1
Options
Supplier
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Supplier Product No.
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Immunogen Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to N-terminal residues of human CUGBP1 (CUG-BP- and ETR-3-like factor 1)
Alternative Name CUGBP1 (CELF1 Antibody Abstract)
Background CUGBP1 (CUG-BP- and ETR-3-like factor 1) is implicated in the regulation of several post-transcriptional events. CUGBP1 is involved in pre-mRNA alternative splicing, mRNA translation and stability. CUGBP1 mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. CUGBP1 specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. CUGBP1 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. CUGBP1 activates SM exon 5 inclusion by antagonizing the repressive effect of PTB. CUGBP1 promotes exclusion of exon 11 of the INSR pre-mRNA. CUGBP1 increases translation and controls the choice of translation initiation codon of CEBPB mRNA. CUGBP1 increases mRNA translation of CEBPB in aging liver. CUGBP1 increases translation of CDKN1A mRNA by antagonizing the repressive effect of CALR3. CUGBP1 mediates rapid cytoplasmic mRNA deadenylation. CUGBP1 recruits the deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to promote their deadenylation. Required for completion of spermatogenesis (By similarity). CUGBP1 binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response elements (BREs).
Synonyms: BRUNOL2, CELF1, CUGBP, NAB50( CELF-1, Bruno-like protein 2, RNA-binding protein BRUNOL-2, CUG triplet repeat RNA-binding protein 1, Deadenylation factor CUG-BP, 50 kDa nuclear polyadenylated RNA-binding protein, Embryo deadenylation element-binding protein homolog, CUG-BP1, EDEN-BP homolog)
Pathways Ribonucleoprotein Complex Subunit Organization
Restrictions For Research Use only
Product cited in: Iakova, Wang, Timchenko, Michalak, Pereira-Smith, Smith, Timchenko: "Competition of CUGBP1 and calreticulin for the regulation of p21 translation determines cell fate." in: The EMBO journal, Vol. 23, Issue 2, pp. 406-17, 2004 (PubMed).

Paillard, Legagneux, Beverley Osborne: "A functional deadenylation assay identifies human CUG-BP as a deadenylation factor." in: Biology of the cell / under the auspices of the European Cell Biology Organization, Vol. 95, Issue 2, pp. 107-13, 2003 (PubMed).

Paillard, Legagneux, Maniey, Osborne: "c-Jun ARE targets mRNA deadenylation by an EDEN-BP (embryo deadenylation element-binding protein)-dependent pathway." in: The Journal of biological chemistry, Vol. 277, Issue 5, pp. 3232-5, 2002 (PubMed).

Takahashi, Sasagawa, Usuki, Kino, Kawahara, Sorimachi, Maeda, Suzuki, Ishiura: "Coexpression of the CUG-binding protein reduces DM protein kinase expression in COS cells." in: Journal of biochemistry, Vol. 130, Issue 5, pp. 581-7, 2001 (PubMed).

Good, Chen, Warner, Herring: "A family of human RNA-binding proteins related to the Drosophila Bruno translational regulator." in: The Journal of biological chemistry, Vol. 275, Issue 37, pp. 28583-92, 2000 (PubMed).

Background publications Hillman, Green, Brenner: "An unappreciated role for RNA surveillance." in: Genome biology, Vol. 5, Issue 2, pp. R8, 2004 (PubMed).

Timchenko, Miller, Timchenko, DeVore, Datar, Lin, Roberts, Caskey, Swanson: "Identification of a (CUG)n triplet repeat RNA-binding protein and its expression in myotonic dystrophy." in: Nucleic acids research, Vol. 24, Issue 22, pp. 4407-14, 1997 (PubMed).

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