Neutrophil Activating Peptide 2 (NAP-2) is proteolytically processed carboxyl-terminal fragments of platelet basic protein (PBP) which is found in the alpha-granules of human platelets. NAP-2 is a member of the CXC chemokines. Similar to other ELR domain containing CXC chemokines such as IL-8 and the GRO proteins, NAP-2 has been shown to bind CXCR-2 and to chemoattract and activate neutrophils. Although CTAP-III, beta-TG and PBP represent amino-terminal extended variants of NAP-2 and possess the same CXC chemokine domains, these proteins do not exhibit NAP-2 activity. Recently, it has been shown that the additional amino-terminal residues of CTAP-III masks the critical ELR receptor binding domain that is exposed on NAP-2 and may account for lack of NAP-2 activity.
Molecular Weight:
7.6 kDa, a single non-glycosylated polypeptide chain containing 70 amino acids.
Source:
Escherichia coli.
Purity:
>97% by SDS-PAGE and HPLC analyses.
Form:
Sterile Filtered White lyophilized (freeze-dried) powder.
Lyophilized from a 0.2mm filtered concentrated solution in 20mM PB, pH 7.4, 50mM NaCl.
Application Notes:
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20C. Further dilutions should be made in appropriate buffered solutions.
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