Product nameCPEB1 peptide
See all CPEB1 proteins and peptides
Our Abpromise guarantee covers the use of ab197860 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Blocking - Blocking peptide for Anti-CPEB1 antibody [EPR11775(2)] (ab181051)
This is the blocking peptide for ab181051
- First try to dissolve a small amount of peptide in either water or buffer. The more charged residues on a peptide, the more soluble it is in aqueous solutions.
- If the peptide doesn’t dissolve try an organic solvent e.g. DMSO, then dilute using water or buffer.
- Consider that any solvent used must be compatible with your assay. If a peptide does not dissolve and you need to recover it, lyophilise to remove the solvent.
- Gentle warming and sonication can effectively aid peptide solubilisation. If the solution is cloudy or has gelled the peptide may be in suspension rather than solubilised.
- Peptides containing cysteine are easily oxidised, so should be prepared in solution just prior to use.
Concentration information loading...
Preparation and Storage
Stability and Storage
Shipped at 4°C. Store at -20°C.
- CPE binding protein 1
- CPE BP1
FunctionSequence-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. 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 (By similarity). 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 (By similarity). Its interaction with APLP1 promotes local CPE-containing mRNA polyadenylation and translation activation (By similarity). Induces the assembly of stress granules in the absence of stress.
Tissue specificityIsoform 1 is expressed in immature oocytes, ovary, brain and heart. Isoform 2 is expressed in brain and heart. Isoform 3 and isoform 4 are expressed in brain. Expressed in breast tumors and several tumor cell lines.
Sequence similaritiesBelongs to the RRM CPEB family.
Contains 2 RRM (RNA recognition motif) domains.
DomainThe 2 RRM domains and the C-terminal region mediate interaction with CPE-containing RNA.
modificationsPhosphorylated on serine/threonine residues by AURKA/STK6 within positions 166 and 197. Phosphorylation and dephosphorylation on Thr-172 regulates cytoplasmic polyadenylation and translation of CPE-containing mRNAs. Phosphorylation on Thr-172 by AURKA/STK6 and CAMK2A activates CPEB1. Phosphorylation on Thr-172 may be promoted by APLP1. Phosphorylation increases binding to RNA.
Cellular localizationCytoplasm > P-body. Cytoplasmic granule. Cell junction > synapse. Membrane. Cell junction > synapse > postsynaptic cell membrane > postsynaptic density. Cell projection > dendrite. Also found in stress granules. Recruited to stress granules (SGs) upon arsenite treatment. In dendrites (By similarity). Localizes in synaptosomes at dendritic synapses of neurons (By similarity). Strongly enriched in postsynaptic density (PSD) fractions (By similarity). Transported into dendrites in a microtubule-dependent fashion and colocalizes in mRNA-containing particles with TACC3, dynein and kinesin (By similarity). Membrane-associated (By similarity). Colocalizes at excitatory synapses with members of the polyadenylation and translation complex factors (CPSF, APLP1, TACC3, AURKA/STK6, SYP, etc.) including CPE-containing RNAs.
- Information by UniProt
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
ab197860 has not yet been referenced specifically in any publications.