Recombinant Human Cugbp Elav-Like Family Member 1 (CELF1)

Name: Recombinant Human Cugbp Elav-Like Family Member 1 (CELF1)
Brand: Beta LifeScience
SKU: BLC-01629P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins, Recombinant proteins fall special offers - full-length proteins, Recombinant proteins fall special offers - tag-free proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Cugbp Elav-Like Family Member 1 (CELF1) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q92879
Target Symbol	CELF1
Synonyms	CELF-1;50 kDa nuclear polyadenylated RNA-binding protein;Bruno-like protein 2;CUG triplet repeat RNA-binding protein 1;CUG-BP1;CUG-BP- and ETR-3-like factor 1;Deadenylation factor CUG-BP;Embryo deadenylation element-binding protein homolog;EDEN-BP homolog;RNA-binding protein BRUNOL-2
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	MNGTLDHPDQPDLDAIKMFVGQVPRTWSEKDLRELFEQYGAVYEINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNMKVLPGMHHPIQMKPADSEKNNAVEDRKLFIGMISKKCTENDIRVMFSSFGQIEECRMLRGPDGLSRGCAFVTFTTRAMAQTAIKAMHQAQEMEGCDSPMVVKFADTQKDKEQKRMAQQLQQQMQQISAASVWGNLAGLNTLGPQYLALLQQTASSGNLNTLSSLHPMGGLNAMQLQNLAALAAAASAAQNTPSGTNALTTSSDPLDVLTSSGDDPDSSSSNSVNPIASLGALQTLAGATAGLNVGSLAGMAALNGGLGSSGLSNGTGSTMEALTQAYSGIQQYAAAALPTLYNQNLLTQQSIGAAGSQKEGPEGANLFIYHLPQEFGDQDLLQMFMPFGNVVSAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQSMNGFQIGMKRLKVQLKRSKNDSKPY
Expression Range	1-482aa (T173E,S178D,S285D,S288D,S295D,S296D,S298D)
Protein Length	Full Length
Mol. Weight	53.7 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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. 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.
Subcellular Location	Nucleus. Cytoplasm. Note=RNA-binding activity is detected in both nuclear and cytoplasmic compartments.
Protein Families	CELF/BRUNOL family
Database References	HGNC: 2549 OMIM: 601074 KEGG: hsa:10658 STRING: 9606.ENSP00000435926 UniGene: Hs.595333
Tissue Specificity	Ubiquitous.

Gene Functions References

results underscore novel roles of CELF1 in melanoma, illustrating tumor type-restricted functions of mRNA binding proteins in cancer. PMID: 29269732
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
High CELF1 expression is associated with aberrant splicing in Type 1 diabetes. PMID: 28512194
CELF1 globally regulates the alternative splicing. PMID: 28733224
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
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
Results show that CELF1 is a potential target of TUG1 interaction and could be negatively regulated by TUG1 RNA. PMID: 27485439
CUG-binding protein 1 regulates HSC activation and liver fibrogenesis. PMID: 27853137
High expression of CUGBP1 is associated with recurrence in lung adenocarcinoma. PMID: 26728670
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
these data provided a comprehensive view of the CELF1 mRNA regulatory network in oral cancer PMID: 26498364
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
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
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
CUGBP1 promotes cell proliferation and suppresses apoptosis via down-regulating C-EBPalpha in human non-small cell lung cancers. PMID: 25701464
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
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
Celf1 has a role in vegetal RNA localization during Xenopus oogenesis PMID: 26164657
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
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
CUGBP1 has a critical role in modulating cell growth and apoptosis PMID: 25077823
the size and the number of colonies formed in gastric cancer MGC-803 cells were markedly reduced in the absence of CUGBP1 PMID: 24818870
CUGBP1 seems to play a role in classic DM1 but not in DM2 PMID: 24376746
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
Data suggest a model for RNA binding protein CELF1/CUGBP1-mediated regulation of alternative polyadenylation (APA). PMID: 25123787
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
High CUGBP1 expression is associated with non-small cell lung cancer. PMID: 23359188
CELF1 depletion induces apoptosis in tumor cells, but not in normal cells. PMID: 23324604
CUGBP1 represses occludin translation by increasing occludin mRNA recruitment to P-bodies. PMID: 23155001
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
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
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
CUG-binding protein represses translation of p27Kip1 mRNA through its internal ribosomal entry site PMID: 21508681
CUGBP1 binding to certain GRE-containing target transcripts decreased following T cell activation through activation-dependent phosphorylation of CUGBP1. PMID: 22117072
Stress granules component CUGBP1 was identified as a factor required for p21 mRNA stabilization. PMID: 21637851
Data show that crystal structures of CUGBP1 RRM1 and tandem RRM1/2 domains bound to RNAs containing tandem UGU(U/G) elements. PMID: 20947024
Overexpression of CUGBP1 in mouse skeletal muscle reproduces features of myotonic dystrophy type 1. PMID: 20603324
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
These results strongly support a role for CUGBP1 up-regulation in myotonic dystrophy type 1 pathogenesis. PMID: 20051426
CUGBP1 directly controls CD9 expression. PMID: 20227387
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
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
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
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
coordinated physical and functional interactions between hnRNP H, CUG-BP1 and MBNL1 dictate IR splicing in normal and DM1 myoblasts PMID: 16946708
transcription of Cugbp1 gene in muscle is regulated by myogenin and E proteins PMID: 17531403
Insertional disruption of the CUGBP1 gene is associated with leukemogenesis PMID: 17854664
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
CUG-BP1 specifically recognized UG repeats, probably through cooperative binding of RNA recognition motifs at both ends of the protein. PMID: 18039683
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

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.