Recombinant Human NP-1 0 ReviewsSubmit a Review Product Details Catalogue Number: 300-42 Description: Defensins (alpha and beta) 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. Source: E.coli Synonyms: Neutrophil Peptide-1, alpha Defensin-1, HNP-1, Cryptdin AA Sequence: ACYCRIPACI AGERRYGTCI YQGRLWAFCC Purity: ≥ 98% by SDS-PAGE gel and HPLC analyses. Biological Activity: Determined by its ability to chemoattract immature dendritic cells using a concentration of 1.0-10.0 ng/ml. Calculated Molecular Weight: 3.4 kDa Accession Number: P59665 Gene ID: 1667 Endotoxin: Endotoxin level is < 0.1 ng/ug of protein (< 1 EU/ug) crossreactivity: Human References PubMed SDS CoA Search Product Line Country Of Origin: USA Not for human use. Research Interest Chemotaxis Immune System product.subtitle.recentcitations First Author Wang, Y Title Intratumoral expression of mature human neutrophil peptide-1 mediates antitumor immunity in mice. Citation Clinical cancer research : an official journal of the American Association for Cancer Research; 15(22) pg6901-11 PubMed Id 19861439 First Author Grigat, J Title Chemoattraction of macrophages, T lymphocytes, and mast cells is evolutionarily conserved within the human alpha-defensin family. Citation Journal of immunology (Baltimore, Md. : 1950); 179(6) pg3958-65 PubMed Id 17785833 First Author Mount, K L Title Haemophilus ducreyi is resistant to human antimicrobial peptides. Citation Antimicrobial Agents and Chemotherapy; 51(9) pg3391-3 PubMed Id 17620373
