In the present study, SB was found to inhibit the adhesion and aggregation of platelets induced by collagen. The effect of SB might be related to its binding to integrin a2b1, the possible direct target protein of SB found in our previous study. The un-direct targetrelated proteins of SB in platelets were searched in the present study using a differential proteomic study. Proteomic technology has become an indispensable and efficient tool in biochemical research. And, this technology has successfully used to study signal pathways in platelets. Twenty possible target-related proteins of SB in platelets were found in the present study. Among the 20 proteins, 6 proteins including heat shock-related 70 kDa protein 2, LIM Reversine domain protein CLP-36, copine I, peroxiredoxin-2, coronin-1 B and cytoplasmic dynein intermediate chain 2C might be the most important ones and have close relationship with integrin a2b1 binding. The possible signal cascades network in platelets after binding of SB to integrin a2b1 was predicted based on previous reports and protein-protein interaction database. For example, previous works indicated that integrin a2b1 binding could cause change in calcium homeostasis and calcium-dependent functions. Previous report also suggested that, by binding to integrin a2b1, endorepellin could trigger transient activation of p38 mitogenactivated protein kinase and heat shock protein 27 and ultimately disassembly of actin stress fibers and focal adhesions. To certify the predicted signal network, against integrin a2b1 on the effects of SB in platelets were checked. The results indicated that SB had dose-dependently binding affinity to integrin a2b1 in vitro and could compete with antibody against integrin a2b1 for the binding site of integrin a2b1 on the membrane of platelets. Furthermore, flow cytometry analysis result confirmed that SB treatment caused dosedependently decrease in intracellular level of Ca level and the effect of SB on Ca level might be related to integrin a2b1 binding. And, the change in coronin-1 B protein level caused by SB treatment was also dependent on integrin a2b1 binding. The revised signal network of SB including binding with integrin a2b1, change in Ca level, reorganization of cytoskeleton as well as change in cytoskeleton-related proteins such as coronin-1 B was established. As to the SB-caused change in ROS level and heat shock protein 70 level, our results indicated that these effects of SB might not be dependent on binding with integrin a2b1. For example, the decrease in ROS might be caused by the potency of SB to act as direct ROS scavenger. Based on its chemical structure characteristic, SB could exhibit direct antioxidative effect in vitro as well as in vivo.