ERH Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids (1-104 a.a.) and having a molecular mass of 14.6kDa. The ERH is purified by proprietary chromatographic techniques.
MGSSHHHHHH SSGLVPRGSH MGSMSHTILL VQPTKRPEGR TYADYESVNE CMEGVCKMYE EHLKRMNPNS PSITYDISQL FDFIDDLADL SCLVYRADTQ TYQPYNKDWI KEKIYVLLRR QAQQAGK.
The ERH protein was initially discovered in the fruit fly, Drosophila melanogaster, where it was identified as an enhancer of the rudimentary gene involved in pyrimidine biosynthesis . The human homolog of this protein shares significant structural and functional similarities with its Drosophila counterpart, highlighting its evolutionary conservation .
ERH is a small protein consisting of 104 amino acids . Despite its modest size, it plays a crucial role in various cellular processes. The protein has been implicated in:
Recent studies have highlighted the importance of ERH in cancer biology. Cancer cells driven by mutations in the KRAS oncogene are particularly sensitive to RNAi-mediated suppression of ERH function . Additionally, ERH expression is inversely correlated with survival in colorectal cancer patients whose tumors harbor KRAS mutations . These findings suggest that ERH could be a potential therapeutic target for certain types of cancer.
Recombinant ERH protein is produced using recombinant DNA technology, which involves inserting the human ERH gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein is used in various research applications to study its structure, function, and role in disease .