ADAM10 Protein, Human (HEK293, His)

The ADAM10 protein serves as a multifaceted protease with a broad substrate specificity, playing a central role in diverse biological processes. Notably, ADAM10 cleaves the membrane-bound precursor of TNF-alpha, releasing its mature soluble form. Additionally, it is responsible for the proteolytic release of various cell-surface proteins, including JAM3, heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2, and the constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). ADAM10 contributes to the normal cleavage of the cellular prion protein and is involved in the cleavage of adhesion molecules such as L1. Furthermore, it controls the proteolytic processing of Notch, mediates lateral inhibition during neurogenesis, and is responsible for FasL ectodomain shedding. ADAM10 exhibits a versatile role in mediating the proteolytic cleavage of various integral membrane proteins, including CORIN, ITM2B, LAG3, IL6R, IL11RA, CHL1, NRCAM, and TREM2. Additionally, ADAM10 plays a crucial role in the development and maturation of glomerular and coronary vasculature, contributes to pillar cell separation during the development of the cochlear organ of Corti, and regulates EFNA5-EPHA3 signaling. In microbial infection, ADAM10 promotes the cytotoxic activity of S.aureus hly by binding to the toxin at zonula adherens and promoting the formation of toxin pores.