Human recombinant β-NGF is produced in Chinese Hamster Ovary (CHO) cells. This recombinant protein is a noncovalently disulfide-linked homodimer, glycosylated, and consists of two identical polypeptide chains. Each chain contains 118 amino acids, with a molecular mass of approximately 26.5 kDa . The protein is typically purified using proprietary chromatographic techniques to ensure high purity and biological activity.
β-NGF has nerve growth-stimulating activity and is involved in the regulation of growth and differentiation of sympathetic and certain sensory neurons . It prevents neurons from undergoing apoptosis (programmed cell death) and promotes their maturation while supporting axonal branching. β-NGF interacts with two primary receptors: p75NTR and TrkA. The NGF-TrkA signaling pathway induces two pathways through the activation of PI3K-Akt or Ras-MAPK, leading to CREB phosphorylation and increased expression of anti-apoptosis genes .
β-NGF is critical for the survival and maintenance of neurons and has become a therapeutic target in neuron regeneration studies. In animal models, β-NGF has been shown to prevent neuronal degeneration and promote myelin repair of neurons in the peripheral nervous system . Clinical studies indicate that dysregulation of NGF signaling is related to neurodegenerative diseases such as Alzheimer’s disease .
Lyophilized β-NGF is stable at room temperature for up to three weeks but should be stored desiccated below -18°C for long-term storage. Upon reconstitution, it should be stored at 4°C for short-term use (2-7 days) and below -18°C for future use. To prevent freeze-thaw cycles, it is recommended to add a carrier protein such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA) .