NRG4 Human

NRG4 contains one EGF-like domain and is a low-affinity ligand for the ERBB4 tyrosine kinase receptor. It activates type-1 growth factor receptors, initiating cell-to-cell signaling through tyrosine phosphorylation . NRG4 also recruits ERBB1 and ERBB2 coreceptors, resulting in ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors .

Recent studies have shown that NRG4 serum levels are associated with insulin resistance, metabolic syndrome, nonalcoholic fatty liver disease, and the severity of atherosclerosis . Additionally, loss of expression of NRG4 is frequently seen in advanced bladder cancer, while increased NRG4 expression correlates with better survival .

Recombinant human NRG4 is typically produced using bacterial, yeast, baculovirus-insect, or mammalian expression systems. The recombinant protein is often purified to a high degree of purity, with endotoxin levels kept low to ensure its suitability for research and therapeutic applications .

The recombinant human NRG4 consists of 63 amino acids and has a calculated molecular mass of approximately 6.7 kDa as estimated in SDS-PAGE under reducing conditions . It is usually provided as a lyophilized powder, which can be reconstituted for use in various experimental setups .

Recombinant human NRG4 samples are stable for up to twelve months when stored at -20°C to -80°C under sterile conditions. It is recommended to aliquot the protein for optimal storage and to avoid repeated freeze-thaw cycles .