Recombinant Human DOCK10 protein

DOCK10. a member of the Dedicator of Cytokinesis (DOCK) protein family, is a guanine nucleotide exchange factor (GEF) that specifically activates Rho GTPases such as Cdc42 and Rac1. These GTPases regulate cytoskeletal dynamics, cell migration, and intracellular signaling. The DOCK family is divided into four subfamilies (DOCK-A to DOCK-D), with DOCK10 belonging to the DOCK-D subfamily. Unlike other DOCK proteins, DOCK10 contains a unique C-terminal CZH2 domain, which facilitates interactions with membrane-associated proteins and GTPase activation. It is predominantly expressed in immune cells (e.g., B lymphocytes) and epithelial tissues, suggesting roles in immune regulation, tissue development, and cancer progression. Studies link DOCK10 to B-cell receptor signaling, lymphocyte trafficking, and tumor metastasis, particularly in hematological malignancies and solid tumors.

Recombinant DOCK10 protein is engineered using expression systems (e.g., E. coli, mammalian cells) to produce functional domains or full-length protein for research. It enables in vitro studies on GTPase binding, GEF activity, and signaling mechanisms. Purification often involves affinity tags (e.g., GST, His-tag) followed by biochemical validation (e.g., SDS-PAGE, Western blot). Researchers utilize recombinant DOCK10 to investigate its role in diseases, screen inhibitors, or develop diagnostic tools. Its dysregulation in cancers and immune disorders highlights its potential as a therapeutic target. However, structural complexity and post-translational modifications pose challenges in producing active recombinant forms, necessitating optimized expression strategies. Current research focuses on elucidating DOCK10’s molecular interactions and therapeutic applications in precision medicine.