NRG1 B1 Human

Neuregulin-1 (NRG1), also known as Heregulin-b1, is a member of the neuregulin family of proteins, which are part of the epidermal growth factor (EGF) family. These proteins play a crucial role in cell signaling, particularly in the development and function of the nervous system and heart. NRG1 is produced in various isoforms through alternative splicing, allowing it to perform a wide range of functions .

Neuregulin-1/Heregulin-b1 is characterized by its EGF-like domain, which is essential for binding to receptor tyrosine kinases, specifically erbB3 and erbB4 . This binding stimulates the heterodimerization of erbB3 and erbB4 with erbB2, leading to the activation of intrinsic kinase activity and subsequent tyrosine phosphorylation . This signaling pathway is vital for various cellular processes, including cell proliferation, differentiation, and survival.

The biological activity of Neuregulin-1/Heregulin-b1 has been extensively studied. It has been shown to promote the motility and invasiveness of breast cancer cells, potentially through the up-regulation of the autocrine motility-promoting factor (AMF) . Additionally, NRG1 plays a significant role in neural development, neurotransmission, and synaptic plasticity .

Recombinant Human Neuregulin-1/Heregulin-b1 is typically produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain . The recombinant protein is purified using proprietary chromatographic techniques to achieve a purity greater than 97% . The protein is lyophilized from a filtered solution and can be reconstituted in sterile water or PBS for use in various applications .

Recombinant Neuregulin-1/Heregulin-b1 is widely used in research to study its effects on cell proliferation and differentiation. It is particularly useful in cancer research, where it is used to investigate the mechanisms underlying cancer cell motility and invasiveness . Additionally, it is employed in studies related to neural development and cardiac function .