• Purity

  >95%, by SDS-PAGE under reducing conditions and visualized by silver stain

• Endotoxin Level

  <0.1 EU per 1 μg of the protein by the LAL method.  

• Activity

  Measured by its ability to enhance LPS-induced TNF-alpha secretion from human monocytes. Rasmussen, P.B.     et al. (1996) FEBS Letters     390:109. The ED    ₅₀ for this effect is 0.5-3 μg/mL.

• Source

  Mouse myeloma cell line, NS0-derived Ile27-Pro250, with a C-terminal 10-His tag

• Accession #

• N-terminal Sequence    
  Analysis

  Ile27

• Predicted Molecular Mass

  26 kDa

• SDS-PAGE

  39 kDa, reducing conditions

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: Azurocidin/CAP37/HBP

Azurocidin, also known as cationic antimicrobial protein 37 (CAP37) and heparin-binding protein (HBP), is a member of the serine protease family that includes Cathepsin G, neutrophil elastase (NE), and proteinase 3 (PR3). These proteases are found in the specialized azurophilic granules of neutrophils (1, 2). Human Azurocidin 1 is encoded by the AZU1 gene located in a cluster with NE and PR3 on chromosome 19pter (2). The open reading frame predicts a 251 amino acid (aa) protein with an N-terminal 26 aa signal sequence and a 7 aa propeptide. There are also eight cysteine residues and 3 putative N-linked glycosylation sites (1).

Although Azurocidin 1 shares a significant degree of aa sequence identity with Cathepsin G, NE, and PR3, it lacks serine protease activity due to mutations at two of the three residues in the catalytic triad (His41Ser and Ser175Gly) (1, 3). Crystallographic analysis suggests that the antibacterial activity of Azurocidin is mediated by a hydrophobic pocket (residues 20 to 44) that binds Gram-negative bacteria lipid A. These structural data also imply that the heparin binding capacity is mediated by non-specific electrostatic interactions between the negatively charged heparin molecule and a large patch of positively charged residues near the lipid A binding site (3).

Azurocidin has also been identified as a modulator of endothelial permeability. Neutrophils arriving first at sites of inflammation release Azurocidin, which acts in a paracrine fashion on endothelial cells causing the development of intercellular gaps and allowing leukocyte extravasation. These findings imply that Azurocidin may be a reasonable therapeutic target for a variety of inflammatory disease conditions (4).

• References:

1. Morgan, J.G. et al. (1991) J. Immunol. 147:3210.

2. Zimmer, M. et al. (1992) Proc. Natl. Acad. Sci. USA 89:8215.

3. Iverson, L.F. et al. (1997) Nat. Struct. Biol. 4:265.

4. Gautam, N. et al. (2001) Nat. Med. 7:1123.

• Long Name:

  Azurocidin/Cationic Antimicrobial Protein-37/Heparin Binding Protein

• Entrez Gene IDs:

  566 (Human)

• Alternate Names:

  AZAMP; AZU; AZU1; azurocidin 1; Azurocidin; CAP37; CAP37Heparin-binding protein; cationic antimicrobial protein 37; HBP; HBPCationic antimicrobial protein CAP37; HUMAZUR; NAZC; neutrophil azurocidin