Recombinant Human SHB protein

SHB (Src homology 2 domain-containing adaptor protein B) is a signaling adaptor protein involved in regulating diverse cellular processes, including proliferation, differentiation, apoptosis, and angiogenesis. It belongs to the SH2 domain-containing protein family, which mediates protein-protein interactions by binding phosphorylated tyrosine residues on target molecules. SHB contains an N-terminal phosphotyrosine-binding (PTB) domain, a central proline-rich region, and a C-terminal SH2 domain, enabling it to scaffold signaling complexes.

First identified in the 1990s, SHB gained attention for its role in receptor tyrosine kinase (RTK) signaling, particularly downstream of vascular endothelial growth factor receptor (VEGFR), platelet-derived growth factor receptor (PDGFR), and fibroblast growth factor receptor (FGFR). It interacts with phosphorylated receptors or docking proteins, recruiting effectors like PI3K, Grb2. and PLCγ to activate pathways such as MAPK/ERK and AKT, influencing cell survival and motility. SHB also regulates immune responses by modulating T-cell receptor signaling and cytokine production.

Recombinant SHB protein is produced using expression systems (e.g., E. coli, mammalian cells) for in vitro studies. Its purified form enables mechanistic exploration of signaling networks, protein interactions, and therapeutic targeting. Research links SHB dysregulation to cancer progression, cardiovascular disorders, and autoimmune diseases, making it a potential biomarker or drug target. For instance, SHB deletion in mice reveals vascular defects and impaired angiogenesis, underscoring its physiological relevance.

Overall, SHB serves as a critical node in cellular signaling, with recombinant tools advancing both basic research and translational applications in disease mechanisms and intervention strategies.