Recombinant Human Cytoplasmic Domain Polyadenylation Element-Binding Protein 1 (CPEB1) Protein (His-SUMO)

Name: Recombinant Human Cytoplasmic Domain Polyadenylation Element-Binding Protein 1 (CPEB1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-08730P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Cytoplasmic Domain Polyadenylation Element-Binding Protein 1 (CPEB1) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9BZB8
Target Symbol	CPEB1
Synonyms	CEBP; CPE binding protein 1; CPE BP1; CPE-binding protein 1; CPE-BP1; CPEB 1; CPEB; CPEB-1; CPEB1; CPEB1 protein; CPEB1_HUMAN; Cytoplasmic polyadenylation binding protein 1; Cytoplasmic polyadenylation element binding protein; Cytoplasmic polyadenylation element binding protein 1; Cytoplasmic polyadenylation element-binding protein 1; FLJ13203; h CEBP; h-CEBP; hCPEB 1; hCPEB-1; MGC34136; MGC60106; mKIAA0940; MKIAA0940 protein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MLFPTSAQESSRGLPDANDLCLGLQSLSLTGWDRPWSTQDSDSSAQSSTHSVLSMLHNPLGNVLGKPPLSFLPLDPLGSDLVDKFPAPSVRGSRLDTRPILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLSLSGGGPRDPLKMGVGSRMDQEQAALAAVTPSPTSASKRWPGASVWPSWDLLEAPKDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPIYSCKVFLGGVPWDITEAGLVNTFRVFGSLSVEWPGKDGKHPRCPPKGYVYLVFELEKSVRSLLQACSHDPLSPDGLSEYYFKMSSRRMRCKEVQVIPWVLADSNFVRSPSQRLDPSRTVFVGALHGMLNAEALAAILNDLFGGVVYAGIDTDKHKYPIGSGRVTFNNQRSYLKAVSAAFVEIKTTKFTKKVQIDPYLEDSLCHICSSQPGPFFCRDQVCFKYFCRSCWHWRHSMEGLRHHSPLMRNQKNRDSS
Expression Range	1-486aa
Protein Length	Full Length of isoform 4
Mol. Weight	69.6kDa
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	Sequence-specific RNA-binding protein that regulates mRNA cytoplasmic polyadenylation and translation initiation during oocyte maturation, early development and at postsynapse sites of neurons. Binds to the cytoplasmic polyadenylation element (CPE), an uridine-rich sequence element (consensus sequence 5'-UUUUUAU-3') within the mRNA 3'-UTR. RNA binding results in a clear conformational change analogous to the Venus fly trap mechanism. In absence of phosphorylation and in association with TACC3 is also involved as a repressor of translation of CPE-containing mRNA; a repression that is relieved by phosphorylation or degradation. Involved in the transport of CPE-containing mRNA to dendrites; those mRNAs may be transported to dendrites in a translationally dormant form and translationally activated at synapses. Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation. Induces the assembly of stress granules in the absence of stress. Required for cell cycle progression, specifically for prophase entry.
Subcellular Location	Cytoplasm. Nucleus. Cytoplasm, P-body. Cytoplasmic granule. Cell junction, synapse. Membrane. Cell junction, synapse, postsynaptic density. Cell projection, dendrite.
Protein Families	RRM CPEB family
Database References	HGNC: 21744 OMIM: 607342 KEGG: hsa:64506 STRING: 9606.ENSP00000457881 UniGene: PMID: 30106109 Upon binding to p27(Kip1) 3'UTR, CPEB1 promotes elongation of poly-A tail and the subsequent translation of p27(Kip1) mRNA. This leads to higher levels of p27(Kip1) in the cell, in turn significantly inhibiting cell proliferation, and confers to CPEB1 a potential value as a tumor suppressor in Glioblastoma. PMID: 27142352 CPEB1 regulation of MMP9 mRNA expression mediates metastasis of breast cancer cells PMID: 26411364 The host RNA-binding protein CPEB1 was highly induced after cytomegalovirus infection and ectopic expression of CPEB1 in non-infected cells recapitulated infection-related post-transcriptional changes. CPEB1 was also required for poly(A)-tail lengthening of viral RNAs important for productive infection. PMID: 27775709 Expression levels of CPEB4 and CPEB1 genes are correlated with overall survival in patients with glioma. PMID: 27000226 WEE1 is regulated at the translational level by CPEB1 and miR-15b in a coordinated and cell-cycle-dependent manner. PMID: 27027998 This mechanical catalysis makes possible a positive feedback loop that would help localize the formation of CPEB fibers to active synapse areas and mark those synapses for forming a long-term memory after the prion form is established. The functional role of the CPEB helical oligomers in this mechanism carries with it implications for targeting such species in neurodegenerative diseases. PMID: 27091989 Structural Analysis of the Pin1-CPEB1 interaction and its potential role in CPEB1 degradation has been described. PMID: 26456073 Identify a mechanism of VEGF overexpression in liver and mesentery that promotes pathologic, but not physiologic, angiogenesis, via sequential and nonredundant functions of CPEB1 and CPEB4. PMID: 26627607 CPEB1, 2, and 4, are essential to successful mitotic cell division. PMID: 26398195 Results suggest that CPEB1-mediated translational control is essential for the differentiation of GSCs. PMID: 25216517 CPEB accelerates deadenylation and decay of the c-myc mRNA by recruiting the Tob-Caf1 complex. PMID: 23178487 Downregulation of CPEB1 induces senescence of glioma cells in a p53-dependent manner. PMID: 23788032 FMRP and CPEB1, an activator of translation, are present in neuronal dendrites, are predicted to bind many of the same mRNAs and may mediate a translational homeostasis that, when imbalanced, results in fragile X syndrome. PMID: 24141422 The structural similarity to other ZZ domains suggests that the CPEB1-ZZ domain recruits sumoylated proteins during assembly of the ribonucleoprotein complex prior to mRNA export from the nucleus. PMID: 23500490 results reveal a novel function of CPEB1 in mediating alternative 3'-UTR processing, which is coordinated with regulation of mRNA translation, through its dual nuclear and cytoplasmic functions PMID: 23434754 poly(A) polymerase Gld2, deadenylase PARN, and translation inhibitory factor neuroguidin (Ngd) are components of a dendritic CPEB-associated polyadenylation apparatus PMID: 22727665 The first evidence of CPEB1 involvement in GC is presented, along with the molecular mechanism underlying the regulation of its expression and its potential role in invasion and angiogenesis. PMID: 22052064 CPEB-mediated zonal occludens-1 mRNA localization is essential for tight-junction assembly and mammary epithelial cell polarity PMID: 22334078 depleted of CPEB demonstrated that this protein directly regulates the translation of PTEN and Stat3 mRNAs. Our results show that CPEB regulated translation is a key process involved in insulin signaling PMID: 22253608 Gld4, a second non-canonical poly(A) polymerase, was found to regulate p53 mRNA polyadenylation/translation in a CPEB-dependent manner PMID: 21478871 The loss of function CPEB1 protein would enhance tumorigenesis by promoting the survival of rapidly dividing and hypermetabolic tumor cells as levels of available nutrients decline. PMID: 20339377 The authors show that the human CPEB1 can repress the activity of the reporter construct containing the HPV-16 early sequences. This repression can be counteracted by a human cytoplasmic poly(A) polymerase, hGLD-2 fused to CPEB1. PMID: 20144904 CPEB1 has a role in compartmentalization of mRNA metabolism in the cytoplasm, between dcp1 bodies and stress granules PMID: 15731006 Results show that CPEB1 is continuously shuttling between nucleus and cytoplasm, and its export is controlled by two redundant motifs dependent on the nuclear export receptor Crm1. PMID: 18923137 CPEB controls senescence and bioenergetics in human cells at least in part by modulating p53 mRNA polyadenylation-induced translation PMID: 19141477 U6snRNA, GAPDH mRNA and CPEB1 mRNA levels may be useful as tumor markers for genital cancers. PMID: 19161537

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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.

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