Human NAP2(CXCL7) Recombinant

Catalog #
90222-A
$130 *
Size: 2 µg
Qty
*US Pricing only. For international pricing, please contact your local distributor.
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Description

Recombinant NAP-2 is a disulfide-linked monomeric protein consisting of 71 amino acid residues and migrates as an approximately 8 kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE. Optimized DNA sequence encoding Human NAP-2 (CXCL7) mature chain was expressed in E. coli.

Synonyms
NAP2, CXCL7, NAP-2, Pro-Platelet Basic Protein, Chemokine (C-X-C Motif) Ligand 7, B-TG1, beta-TG, LDGF, PPBP, Neutrophil-Activating Peptide 2
Product Info
Storage and Usage
Citations
Species
Human
Host Species/Expression System
E. coli
Purity
≥98% by SDS-PAGE and HPLC
Format
lyophilized protein
Formulation
Lyophilized from a 0.2 µm filtered 20 mM Phosphate buffer, 100 mM NaCl, pH 7.5.
MW
8 kDa
Endotoxin Level
<0.1 ng/µg (1 EU/µg), using the LAL gel clot method.
Amino Acids
59–128
Biological Activity
Determined by its ability to chemoattract human monocytes using a concentration range of 2.0-40.0 ng/ml.
Genbank #
P02775
UniProt #
P02775
Background
The chemokine neutrophil- activating peptide 2 (NAP-2) is a 70-amino acid residue polypeptide that is formed from platelet-derived precursors by proteolytic processing. Mature NAP-2 stimulates various effector functions of polymorphonuclear neutrophil granulocytes (PMN) including directed chemotactic migration, exocytosis of lysosomal enzymes and secondary granule contents, and up-regulation of adhesion receptors. NAP-2 has been assigned to a subfamily now termed alpha-chemokines. The alpha-chemokines contain four cysteine residues at highly conserved positions, which enclose the core region of the molecules. The first two cysteines are separated by a single amino acid, forming a motif (CXC) that distinguishes the alpha-chemokine from the beta-chemokine subfamily, where these cysteines are in directly adjacent positions.
References
1. J. Nucl. Med., Jul 2004, 45: 1217 - 1223.
2. Genes Cells, Jan 2003, 8: 9 - 15.
3. J. Biol. Chem., Mar 1995, 270: 6338.