TRIP10/CIP4 Protein, Human (sf9, His)

TRIP10/CIP4 proteins coordinate cellular dynamics and are critical for insulin-induced GLUT4 translocation and membrane tubulation during endocytosis. Good at lipid binding, especially with phosphatidylinositol 4,5-bisphosphate and phosphatidylserine, promoting membrane invagination. TRIP10/CIP4 Protein, Human (sf9, His) is the recombinant human-derived TRIP10/CIP4 protein, expressed by Sf9 insect cells , with C-His labeled tag. The total length of TRIP10/CIP4 Protein, Human (sf9, His) is 545 a.a., with molecular weight of ~84.2 KDa.

TRIP10/CIP4 Protein emerges as a pivotal orchestrator in cellular dynamics, playing a crucial role in diverse processes ranging from insulin-induced GLUT4 translocation to the plasma membrane to the coordination of membrane tubulation during endocytosis. This multifaceted protein is adept at binding lipids, including phosphatidylinositol 4,5-bisphosphate and phosphatidylserine, thereby promoting membrane invagination and the formation of tubules. TRIP10/CIP4 also showcases its versatility by participating in CDC42-induced actin polymerization, recruiting the essential regulator WASL/N-WASP, and activating the Arp2/3 complex. The resultant actin polymerization facilitates the fission of membrane tubules, contributing to the formation of endocytic vesicles. Beyond endocytosis, TRIP10/CIP4 is a key player in podosome formation, specialized actin-rich adhesion structures found in monocyte-derived cells. Additionally, it may play a role in the lysosomal retention of FASLG/FASL. The intricate web of protein-protein interactions involves specific binding with GTP-bound RHOQ, CDC42, DNM2, PDE6G, and various other partners, underscoring its central role in cellular processes. The ability of TRIP10/CIP4 to homodimerize and form filamentous structures adds another layer to its dynamic functionality, making it a pivotal player in the intricate tapestry of cellular regulation.

Human

Sf9 insect cells

C-His

Q15642 (M1-N545)

9322  [NCBI]

Approximately 84.2 kDa.

Greater than 85% as determined by reducing SDS-PAGE

<1 EU/μg, determined by LAL method.