In this work, we introduce one new material which not only highly resists nonspecific protein adsorption, but also has active groups for protein immobilization. Its application to create a novel sensor surface is demonstrated using surface plasmon resonance (SPR) sensors. The sensor provided stability and nonfouling properties, as well as binding sites for protein immobilization. To prepare this sensor surface, a self-assembled monolayer (SAM) of ù-mercaptoundecyl bromoisobutyrate was formed on a gold surface. A caboxybetaine methacrylate (CBMA) polymer film of 10-20 nm was grafted on the SAM covered with initiators through the surface initiated atom transfer polymerization (ATRP) method. An antibody i.e., anti-human chorionic gonadotropin (anti-hCG), was immobilized on the poly(CBMA) surface via (N-ethyl-N'-(3-dimethyl aminopropyl)-carbodiimide/N-hydroxysuccinimide (EDC/NHS) chemistry. SPR results show that this surface not only highly resists nonspecific adsorption of proteins [e.g., fibrinogen and lysozyme], but also showed highly specific specific binding of hCG.