The Recombinant Human EREG Protein is a biologically active recombinant protein that plays a significant role in various cellular processes and signaling pathways in human biology. This protein is widely employed in immunological research, cell biology studies, protein-protein interaction analyses, and therapeutic development, providing researchers with a reliable tool for investigating EREG function and its implications in health and disease.
This product (SKU: RPCB1256) is produced using advanced expression systems and features a N-hFc tag for convenient detection and purification. The protein exhibits a calculated molecular weight of 31.23 kDa with an observed molecular weight of 35-40 kDa under denaturing conditions, achieving ≥ 95% as determined by SDS-PAGE., ensuring exceptional quality and consistency for research applications.
High quality, high purity and low endotoxin recombinant Recombinant Human EREG Protein (RPCB1256), tested reactivity in HEK293 cells and has been validated in SDS-PAGE.100% guaranteed.
Endotoxin:
< 0.01 EU/μg of the protein by LAL method
Purity:
≥ 95% as determined by SDS-PAGE.
Formulation:
Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.
Reconstitution:
Centrifuge the vial before opening. Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water. Avoid vortex or vigorously pipetting the protein. For long term storage, it is recommended to add a carrier protein or stablizer (e.g. 0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose), and aliquot the reconstituted protein solution to minimize free-thaw cycles.
Storage:
Store at -20℃.Store the lyophilized protein at -20℃ to -80 ℃ up to 1 year from the date of receipt. After reconstitution, the protein solution is stable at -20℃ for 3 months, at 2-8℃ for up to 1 week.
Epiregulin (EREG) is a member of the epidermal growth factor family. Epiregulin (EREG) can function as a ligand of EGFR (epidermal growth factor receptor), as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors. Epiregulin (EREG) exhibit bifunctional regulatory properties: it inhibit the growth of several epithelial tumor cells and stimulated the growth of fibroblasts and various other types of cells. Epiregulin (EREG) bound to the EGF receptors of epidermoid carcinoma A431 cells much more weakly than did EGF, but was nevertheless much more potent than EGF as a mitogen for rat primary hepatocytes and Balb/c 3T3 A31 fibroblasts. These findings suggest that epiregulin (EREG) plays important roles in regulating the growth of epithelial cells and fibroblasts by binding to receptors for EGF-related ligands. Epiregulin (EREG) is the broadest specificity EGF-like ligand so far characterized: not only does it stimulate homodimers of both ErbB-1 and ErbB-4, it also activates all possible heterodimeric ErbB complexes.
Recombinant Human EREG Protein was determined by SDS-PAGE under reducing conditions with Coomassie Blue.
