SH2B2. also known as APS (Adaptor Protein with Pleckstrin Homology and Src Homology 2 Domains), is a member of the SH2B family of adaptor proteins involved in signal transduction pathways. It contains critical functional domains, including a pleckstrin homology (PH) domain, an SH2 domain, and a C-terminal dimerization domain, enabling interactions with tyrosine kinase receptors and downstream signaling components. SH2B2 is primarily expressed in metabolic tissues, such as adipose tissue, liver, and skeletal muscle, where it regulates signaling cascades initiated by insulin, leptin, and growth factors. Studies suggest it modulates receptor tyrosine kinase activity, influencing cell proliferation, differentiation, and metabolic homeostasis. Dysregulation of SH2B2 has been linked to metabolic disorders, including diabetes and obesity, as well as certain cancers.
Antibodies targeting SH2B2 are essential tools for investigating its expression, localization, and molecular interactions. They are widely used in techniques like Western blotting, immunoprecipitation, and immunohistochemistry to study SH2B2’s role in cellular processes. For example, SH2B2 antibodies help elucidate mechanisms by which SH2B2 enhances or inhibits receptor tyrosine kinase signaling, such as its interaction with insulin receptors or Trk neurotrophin receptors. Additionally, these antibodies aid in exploring SH2B2’s involvement in immune regulation, as it interacts with T-cell receptor signaling components. The development of specific, high-affinity SH2B2 antibodies continues to support research into metabolic diseases, cancer biology, and therapeutic targeting of signaling pathways.