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Mouse Anti-CELF1 Recombinant Antibody (3B1) (CBMAB-1350-CN)

This product is a mouse antibody that recognizes CELF1 of human. The antibody 3B1 can be used for immunoassay techniques such as: IF, WB.
See all CELF1 antibodies
Published Data
Fig.1 Immunofluorescense and in situ images of DM1 myoblasts transfected with GFP. In control DM1 myoblasts transfected with GFP (green) CUGBP1 is predominantly in the nucleus (red).
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Fig.2 Western blot revealing co-immunoprecipitation between CUGBP1 and human SMAUG1.
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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat, Rabbit, Cattle, Pig
Clone
3B1
Antibody Isotype
IgG1, Κ
Application
IF, WB

Basic Information

Immunogen
CUG-BP1 human nuclear RNA binding protein
Specificity
Human, Mouse, Rat, Rabbit, Cattle, Pig
Antibody Isotype
IgG1, Κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 6.97% L-Arginine, pH 7.4
Preservative
0.02% Sodium azide
Concentration
0.8 mg/mL
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
CUGBP Elav-Like Family Member 1
Introduction
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. This gene may play a role in myotonic dystrophy type 1 (DM1) via interactions with the dystrophia myotonica-protein kinase (DMPK) gene. This protein 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.
Entrez Gene ID
Human10658
Mouse13046
Rat362160
Rabbit100354668
Cattle540475
Pig100514512
UniProt ID
HumanQ92879
MouseP28659
RatQ4QQT3
RabbitG1SF64
CattleA0A3Q1MNY3
PigF1SID9
Alternative Names
CUGBP; NAB50; NAPOR; CUG-BP; CUGBP1; hNab50; BRUNOL2; EDEN-BP
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 cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. 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. Activates SM exon 5 inclusion by antagonizing the repressive effect of PTB. Promotes exclusion of exon 11 of the INSR pre-mRNA. Inhibits, together with HNRNPH1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Increases translation and controls the choice of translation initiation codon of CEBPB mRNA. Increases mRNA translation of CEBPB in aging liver (By similarity).
Increases translation of CDKN1A mRNA by antagonizing the repressive effect of CALR3. Mediates rapid cytoplasmic mRNA deadenylation. Recruits the deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to promote their deadenylation. Required for completion of spermatogenesis (By similarity).
Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response elements (BREs). Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA. Binds to AU-rich sequences (AREs or EDEN-like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA. Binds to the 5'-region of CDKN1A and CEBPB mRNAs. Binds with the 5'-region of CEBPB mRNA in aging liver. May be a specific regulator of miRNA biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF2, negatively regulates the processing to mature miRNA (PubMed:28431233).
Biological Process
Embryo development ending in birth or egg hatching Source: UniProtKB
Germ cell development Source: UniProtKB
mRNA destabilization Source: ARUK-UCL
mRNA processing Source: ProtInc
mRNA splice site selection Source: UniProtKB
Negative regulation of cell population proliferation Source: ARUK-UCL
Negative regulation of gene expression Source: ARUK-UCL
Positive regulation of cell death Source: ARUK-UCL
Positive regulation of gene expression Source: ARUK-UCL
Posttranscriptional gene silencing Source: ARUK-UCL
Regulation of alternative mRNA splicing, via spliceosome Source: GO_Central
Regulation of inflammatory response Source: ARUK-UCL
Regulation of RNA splicing Source: UniProtKB
RNA interference Source: UniProtKB
Cellular Location
Nucleus; Cytoplasm. RNA-binding activity is detected in both nuclear and cytoplasmic compartments.
PTM
Phosphorylated. Its phosphorylation status increases in senescent cells.

Chang, K. T., Wang, L. H., Lin, Y. M., Cheng, C. F., & Wang, G. S. (2021). CELF1 promotes vascular endothelial growth factor degradation resulting in impaired microvasculature in heart failure. The FASEB Journal, 35(5), e21512.

Wang, H., Huang, R., Guo, W., Qin, X., Yang, Z., Yuan, Z., ... & Wang, H. (2020). RNA-binding protein CELF1 enhances cell migration, invasion, and chemoresistance by targeting ETS2 in colorectal cancer. Clinical Science, 134(14), 1973-1990.

Cox, D. C., Guan, X., Xia, Z., & Cooper, T. A. (2020). Increased nuclear but not cytoplasmic activities of CELF1 protein leads to muscle wasting. Human molecular genetics, 29(10), 1729-1744.

Yan, J. K., Zhang, T., Dai, L. N., Gu, B. L., Zhu, J., Yan, W. H., ... & Wang, Y. (2019). CELF1/p53 axis: a sustained antiproliferative signal leading to villus atrophy under total parenteral nutrition. The FASEB Journal, 33(3), 3378-3391.

Yan, J. K., Zhu, J., Gong, Z. Z., Wen, J., Xiao, Y. T., Zhang, T., & Cai, W. (2018). Supplementary choline attenuates olive oil lipid emulsion‐induced enterocyte apoptosis through suppression of CELF 1/AIF pathway. Journal of cellular and molecular medicine, 22(3), 1562-1573.

Cifdaloz, M., Osterloh, L., Graña, O., Riveiro-Falkenbach, E., Ximénez-Embún, P., Muñoz, J., ... & Soengas, M. S. (2017). Systems analysis identifies melanoma-enriched pro-oncogenic networks controlled by the RNA binding protein CELF1. Nature communications, 8(1), 1-18.

Chang, K. T., Cheng, C. F., King, P. C., Liu, S. Y., & Wang, G. S. (2017). CELF1 mediates connexin 43 mRNA degradation in dilated cardiomyopathy. Circulation research, 121(10), 1140-1152.

Yan, J. K., Zhu, J., Gong, Z. Z., Wen, J., Xiao, Y. T., Zhang, T., & Cai, W. (2017). Olive oil-supplemented lipid emulsion induces CELF1 expression and promotes apoptosis in Caco-2 cells. Cellular Physiology and Biochemistry, 41(2), 711-721.

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For research use only. Not intended for any clinical use.

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