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Neutrophil-activating peptide 2 (NAP2) is the carboxy-terminal fragment of platelet basic protein (PBP), present in human platelet alpha granules. NAP-2 is one of the CXC chemokines. Similar to other ELR domain-containing CXC chemokines such as IL-8 and GRO proteins, NAP-2 has been shown to bind CXCR-2 and chemoattract and activate neutrophils. Although CTAP-III, β-TG and PBP represent N-terminally extended variants of NAP-2 and share the same CXC chemokine domain, these proteins do not exhibit NAP-2 activity. Recently, it was shown that the additional amino-terminal residues of CTAP-III mask the critical ELR receptor-binding domain exposed on NAP-2, which may be responsible for the lack of NAP-2 activity.