Hepatocyte growth factor (HGF) regulates cell growth, cell motility, and morphogenesis and plays a central role in angiogenesis, tumorogenesis, and tissue regeneration. HGF binds and activates the receptor tyrosine kinase, c-Met, activating PI3K/AKT, FAK, JNK, and ERK1/2 signaling.1
HGF is secreted as a single inactive polypeptide and is cleaved by serine proteases into a 62-kDa heavy-chain and 32-36-kDa light-chain. A disulfide bond between the heavy and light chains produces the active, heterodimeric molecule.2 Alternative splicing of HGF produces multiple transcript variants encoding different isoforms. The NK1 isoform is the smallest naturally occurring splice variant, comprising the N-terminus and first kringle domain.3
Bovine, porcine and human HGF are all members of the hepatocyte growth factor (HGF) family. While the sequence of porcine HGF is similar to human HGF, there are differences in structure and bioactivity. Porcine HGF is more resistant to protease digestion. Additionally, porcine HGF appears to be more potent than its counterparts when it comes to inducing muscle cell proliferation and differentiation. These findings demonstrate that porcine HGF could have important implications for cellular agriculture applications as it may provide a faster route towards creating tissues with improved regenerative qualities.
Qkine HGF (NK1) recombinant protein is produced in an animal-free microbial system that is compatible with production at scale. We are expanding our range of innovative growth factors for cellular agriculture and cultivated meat media development to support advances in the field, please reach out to cellag@qkine.com to discuss collaboration opportunities.
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