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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
RERE antibody detects Arginine-glutamic acid dipeptide repeats protein, a predominantly nuclear transcriptional coregulator encoded by the RERE gene on chromosome 1p36.23. RERE belongs to the atrophin protein family and functions as a transcriptional regulator that influences embryonic development, cell differentiation, and apoptosis. The protein localizes mainly to the nucleus but can also be found in the cytoplasm depending on signaling state. RERE acts as a transcriptional coregulator that modulates gene expression by interacting with nuclear receptors and chromatin-modifying enzymes, integrating developmental signals and apoptotic pathways.
RERE serves as both a coactivator and corepressor for nuclear receptors such as retinoic acid receptor (RAR) and histone deacetylases (HDACs), linking transcriptional regulation with epigenetic modification. It plays an essential role in retinoic acid signaling, a pathway required for proper embryonic tissue differentiation. Through its interactions with transcription factors and epigenetic complexes, RERE controls gene expression patterns that direct neuronal patterning, heart formation, and eye morphogenesis. Its chromatin-association properties make it a central player in gene regulatory networks that define developmental outcomes.
Mutations or deletions in the RERE gene are associated with 1p36 deletion syndrome and RERE-related neurodevelopmental disorders, which cause developmental delay, hypotonia, and congenital malformations. Functional studies in model organisms show that loss of RERE disrupts neural crest migration, cardiac outflow tract formation, and craniofacial development. The proteins regulatory activity within retinoic acid signaling links it to both morphogenetic and metabolic control during embryogenesis.
At the molecular level, RERE interacts with HDAC1/2, p300/CBP, and other transcriptional repressors to modulate chromatin accessibility. These interactions determine whether RERE acts as a transcriptional activator or repressor depending on context. RERE also influences p53-dependent apoptosis and tumor suppression, highlighting its dual role in development and cancer. Reduced RERE expression has been observed in certain malignancies, suggesting a protective function against tumorigenesis.
Structurally, RERE contains an N-terminal Atrophin-1 domain, several arginine/glutamic acid-rich repeats, and nuclear localization signals that facilitate chromatin binding. Its modular architecture allows multiple protein interactions, and its Atrophin-like region contributes to transcriptional repression. Evolutionarily, RERE is conserved among vertebrates and classified within the atrophin family of transcriptional regulators, known for controlling gene silencing and differentiation. RERE is also implicated in pathways such as retinoic acid signaling and chromatin remodeling, reflecting its multifunctional nature.
Immunohistochemical staining using RERE antibody demonstrates nuclear localization in neurons, cardiac myocytes, and developing epithelia. The RERE antibody from NSJ Bioreagents is an excellent reagent for investigating transcriptional regulation, retinoic acid pathway dynamics, and developmental mechanisms at the molecular level.
Optimal dilution of the RERE antibody should be determined by the researcher.
E.coli-derived human RERE recombinant protein (Position: D109-H1037) was used as the immunogen for the RERE antibody.
After reconstitution, the RERE antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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