|Description||Defensins (α and β) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins which include NP-1, NP-2 and NP-3, are distinguished from the β-defensins by the pairing of their three disulfide bonds. In addition to antimicrobial activity, NP-1 exhibits chemotactic activity on dendritic cells. NP-1 is expressed as the C-terminal portion of an inactive precursor protein, which also contains a 19 amino acid N-terminal signal sequence and a 45 amino acid polypeptide. NP-1 contains a six-cysteine motif that forms three intra-molecular disulfide bonds. Recombinant human NP-1 is a 3.4 kDa protein containing 30 amino acid residues.|
|BiologicalActivity||Determined by its ability to chemoattract immature dendritic cells using a concentration of 1.0-10.0 ng/ml.|
|Authenticity||Verified by N-terminal and Mass Spectrometry analyses (when applicable).|
|Endotoxin||Endotoxin level is <0.1 ng/ µg of protein (<1EU/ µg).|
|Protein Content||Verified by UV Spectroscopy and/or SDS-PAGE gel.|
|Precautions||Recombinant Human NP-1 is for research use only and not for use in diagnostic or therapeutic procedures.|
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