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CELF1 Antibody

  • 中文名稱：
    CELF1兔多克隆抗體
  • 貨號：
    CSB-PA991834
  • 規(guī)格：
    ￥2024
  • 圖片：
    • Western blot analysis of extracts from HeLa cells and HepG2 cells, using CELF-1 antibody.
  • 其他：

產(chǎn)品詳情

  • 產(chǎn)品名稱：
    Rabbit anti-Homo sapiens (Human) CELF1 Polyclonal antibody
  • Uniprot No.：
  • 基因名：
    CELF1
  • 宿主：
    Rabbit
  • 反應(yīng)種屬：
    Human,Mouse,Rat
  • 免疫原：
    Synthesized peptide derived from internal of Human CELF-1.
  • 免疫原種屬：
    Homo sapiens (Human)
  • 克隆類型：
    Polyclonal
  • 純化方式：
    The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
  • 濃度：
    It differs from different batches. Please contact us to confirm it.
  • 產(chǎn)品提供形式：
    Liquid
  • 應(yīng)用范圍：
    ELISA,WB
  • 推薦稀釋比：
    Application Recommended Dilution
    WB 1:500-1:3000
  • Protocols：
  • 儲存條件：
    Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
  • 貨期：
    Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

產(chǎn)品評價

靶點詳情

  • 功能：
    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. 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. 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.
  • 基因功能參考文獻：
    1. results underscore novel roles of CELF1 in melanoma, illustrating tumor type-restricted functions of mRNA binding proteins in cancer. PMID: 29269732
    2. These data present an 11-component genetic pathway, invisible to transcriptional profiling approaches, in which the CELF1 protein functions as a central node controlling translational activation of genes driving EMT and ultimately tumour progression. PMID: 27869122
    3. High CELF1 expression is associated with aberrant splicing in Type 1 diabetes. PMID: 28512194
    4. CELF1 globally regulates the alternative splicing. PMID: 28733224
    5. Findings indicate that IGF2R expression is controlled posttranscriptionally by two factors that associate with Igf2r mRNA and suggest that miR-195 and CUGBP1 dampen IGF signaling by inhibiting IGF2R translation. PMID: 28716948
    6. In the course of these studies, we found that RNA binding protein CUGBP1 is a new tumor suppressor protein which is reduced in all HBL samples. Therefore, we generated CUGBP1 KO mice and examined HBL signatures in the liver of these mice. Micro-array studies revealed that the HBL-specific molecular signature is developed in livers of CUGBP1 KO mice at very early ages PMID: 28535186
    7. Results show that CELF1 is a potential target of TUG1 interaction and could be negatively regulated by TUG1 RNA. PMID: 27485439
    8. CUG-binding protein 1 regulates HSC activation and liver fibrogenesis. PMID: 27853137
    9. High expression of CUGBP1 is associated with recurrence in lung adenocarcinoma. PMID: 26728670
    10. CUG-BP1 affected the calcium release activity in single myofibers and the extent of atrophy was significantly reduced upon gene silencing of CUG-BP1 in atrophic muscle. PMID: 26531141
    11. these data provided a comprehensive view of the CELF1 mRNA regulatory network in oral cancer PMID: 26498364
    12. forced expression of miR-214-3p enhances the sensitivity of esophageal cancer cells to cisplatin-induced apoptosis. This effect is abrogated with rescue expression of survivin or CUG-BP1 PMID: 26234674
    13. Expression of several genes within the CELF1 locus, including MTCH2, were highly correlated with one another and were associated with Alzheimer's disease status. PMID: 26919393
    14. CUGBP1 and HuR negate each other's effects in regulating E-cadherin translation by altering the recruitment of E-cadherin mRNA to PBs and play important roles in the regulation of intestinal barrier integrity. PMID: 26491048
    15. CUGBP1 promotes cell proliferation and suppresses apoptosis via down-regulating C-EBPalpha in human non-small cell lung cancers. PMID: 25701464
    16. The results indicate that the cellular level of miR-122 is determined by the balance between the opposing effects of GLD-2 and PARN/CUGBP1 on the metabolism of its 3'-terminus. PMID: 26130707
    17. CELF1 dysfunction in malignant T cells led to the up-regulation of a subset of GRE-containing transcripts that promote cell growth and down-regulation of another subset that suppress cell growth PMID: 26249002
    18. Celf1 has a role in vegetal RNA localization during Xenopus oogenesis PMID: 26164657
    19. These results demonstrate the importance of CUGBP1 in the biological and pathological functions of NSCLC and indicate its potential as a therapeutic target for NSCLC. PMID: 25619475
    20. The result is consistent with the hypothesis that MBNL proteins are trapped by expanded CUG repeats and inactivated in myotonic dystrophy type 1 (DM1) and that CELF1 is activated in DM1. PMID: 25403273
    21. CUGBP1 has a critical role in modulating cell growth and apoptosis PMID: 25077823
    22. the size and the number of colonies formed in gastric cancer MGC-803 cells were markedly reduced in the absence of CUGBP1 PMID: 24818870
    23. CUGBP1 seems to play a role in classic DM1 but not in DM2 PMID: 24376746
    24. The Alzheimer's disease single nucleotide polymorphism rs10838725 (pAD = 1.1 x 10(-08)) at the locus CELF1 is also genome-wide significant for obesity. PMID: 24788522
    25. Data suggest a model for RNA binding protein CELF1/CUGBP1-mediated regulation of alternative polyadenylation (APA). PMID: 25123787
    26. CUGBP1 was expressed in 85.7% hepatocellular carcinoma specimens compared with 50% in normal liver specimens. CUGBP1 silencing remarkably decreased the proliferation of HepG2 cells. PMID: 24502807
    27. High CUGBP1 expression is associated with non-small cell lung cancer. PMID: 23359188
    28. CELF1 depletion induces apoptosis in tumor cells, but not in normal cells. PMID: 23324604
    29. CUGBP1 represses occludin translation by increasing occludin mRNA recruitment to P-bodies. PMID: 23155001
    30. study suggests that regulation of CUGBP1 and MBNL1 is essential for accurate control of destabilization of a broad spectrum of mRNAs as well as of alternative splicing events PMID: 22355723
    31. The results suggest that CUG-BP1 binds to nucleotides 51-100 of the human albumin 3'UTR. In human cells CUG-BP1 binding may thus play a role in regulation of albumin expression and, additionally, it may have a function in post-transcriptional control in CHO cells. PMID: 22982313
    32. CUG-BP1 is overexpressed in oesophageal cancer cell lines and human oesophageal cancer specimens. CUG-BP1 associates with the 3'-untranslated region of survivin mRNA. PMID: 22646166
    33. CUG-binding protein represses translation of p27Kip1 mRNA through its internal ribosomal entry site PMID: 21508681
    34. CUGBP1 binding to certain GRE-containing target transcripts decreased following T cell activation through activation-dependent phosphorylation of CUGBP1. PMID: 22117072
    35. Stress granules component CUGBP1 was identified as a factor required for p21 mRNA stabilization. PMID: 21637851
    36. Data show that crystal structures of CUGBP1 RRM1 and tandem RRM1/2 domains bound to RNAs containing tandem UGU(U/G) elements. PMID: 20947024
    37. Overexpression of CUGBP1 in mouse skeletal muscle reproduces features of myotonic dystrophy type 1. PMID: 20603324
    38. identified 613 putative mRNA targets of CUGBP1 and found that the UGUUUGUUUGU GU-rich elements (GREs) sequence and a GU-repeat sequence were both highly enriched in the 3' UTRs of these targets PMID: 20547756
    39. These results strongly support a role for CUGBP1 up-regulation in myotonic dystrophy type 1 pathogenesis. PMID: 20051426
    40. CUGBP1 directly controls CD9 expression. PMID: 20227387
    41. CUG-BP and Xenopus EDEN-BP have very similar RNA-binding specificities; it is suggested that the CUG expansion associated with Type 1 myotonic dystrophy can affect the function of CUG-BP, leading to a trans-dominant effect on normal RNA processing PMID: 12799066
    42. Data show that epidermal growth factor receptor signaling results in phosphorylation of CUG-BP1, and leads to increased binding of CUG-BP1 to CCAAT/enhancer binding protein beta (C/EBP beta) mRNA and elevated expression of the C/EBPbeta LIP isoform. PMID: 15082764
    43. The results of this study suggest that the CUG expansion may bind to complementary sequences within the CUGBP1 mRNA and that this molecular interaction may affect CUGBP1 mRNA expression in DM1. PMID: 15099703
    44. CUG-BP, therefore, is the first RNA-binding protein shown to directly recruit a deadenylase to an RNA substrate.CUG-BP interacts with PARN in extracts by coimmunoprecipitation, and this interaction can be recapitulated using recombinant proteins PMID: 16601207
    45. coordinated physical and functional interactions between hnRNP H, CUG-BP1 and MBNL1 dictate IR splicing in normal and DM1 myoblasts PMID: 16946708
    46. transcription of Cugbp1 gene in muscle is regulated by myogenin and E proteins PMID: 17531403
    47. Insertional disruption of the CUGBP1 gene is associated with leukemogenesis PMID: 17854664
    48. Data show that expression of DMPK-CUG-repeat RNA results in hyperphosphorylation and stabilization of CUGBP1, and suggest that inappropriate activation of the PKC pathway contributes to the pathogenic effects of a noncoding RNA. PMID: 17936705
    49. CUG-BP1 specifically recognized UG repeats, probably through cooperative binding of RNA recognition motifs at both ends of the protein. PMID: 18039683
    50. These results demonstrate the dynamic behavior of CUGBP-1 during stress response and that the linker region, in concert with RRMs, plays a significant role in defining its subcellular localization and dynamics. PMID: 18164289

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  • 亞細(xì)胞定位：
    Nucleus. Cytoplasm. Note=RNA-binding activity is detected in both nuclear and cytoplasmic compartments.
  • 蛋白家族：
    CELF/BRUNOL family
  • 組織特異性：
    Ubiquitous.
  • 數(shù)據(jù)庫鏈接：

    HGNC: 2549

    OMIM: 601074

    KEGG: hsa:10658

    STRING: 9606.ENSP00000435926

    UniGene: Hs.595333