RERG Human
Description
RERG Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 219 amino acids (1-199 a.a.) and having a molecular mass of 24.7kDa (Molecular size on SDS-PAGE will appear higher). The RERG is purified by proprietary chromatographic techniques.
Product Specs
MGSSHHHHHH SSGLVPRGSH MAKSAEVKLA IFGRAGVGKS ALVVRFLTKR FIWEYDPTLE STYRHQATID DEVVSMEILD TAGQEDTIQR EGHMRWGEGF VLVYDITDRG SFEEVLPLKN ILDEIKKPKN VTLILVGNKA DLDHSRQVST EEGEKLATEL ACAFYECSAC TGEGNITEIF YELCREVRRR RMVQGKTRRR SSTTHVKQAI NKMLTKISS.
Product Science Overview
The RAS-like, Estrogen-Regulated, Growth Inhibitor (RERG) is a protein that belongs to the Ras superfamily of small GTPases. These proteins are involved in various cellular processes, including growth, differentiation, and apoptosis. RERG is particularly notable for its role in inhibiting cell proliferation and its regulation by estrogen, making it a significant protein in the context of breast cancer research.
The RERG gene is located on chromosome 12p12 and encodes a small GTP-binding and hydrolyzing protein. The human recombinant form of RERG is produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain containing 219 amino acids. This recombinant protein includes a 20 amino acid His tag at the N-terminus, which facilitates its purification .
RERG binds GDP/GTP and possesses intrinsic GTPase activity. It has a higher affinity for GDP than for GTP. Overexpression of RERG in cell lines leads to a reduction in the rate of proliferation, colony formation, and tumorigenic potential . This makes RERG a candidate tumor suppressor gene, particularly in breast cancer, where it is regulated by estrogen .
RERG functions by inhibiting cell proliferation, migration, and angiogenesis. It achieves this by interfering with the signaling pathways that promote these processes. The exact mechanisms are still under investigation, but it is known that RERG’s activity is modulated by estrogen, which can either upregulate or downregulate its expression depending on the cellular context .
The recombinant form of RERG is used extensively in research to study its role in cancer biology. By understanding how RERG inhibits cell growth and its regulation by estrogen, researchers hope to develop new therapeutic strategies for cancers that are driven by estrogen signaling, such as certain types of breast cancer.
The human recombinant RERG is produced in E. coli and purified using proprietary chromatographic techniques. The protein is typically supplied as a sterile filtered, colorless solution containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 5mM DTT, and 50% glycerol. It is recommended to store the protein desiccated below -18°C to maintain its stability .
