Recombinant Human Azurocidin/CAP37/HBP Protein, CF
Recombinant Human Azurocidin/CAP37/HBP Protein, CF Summary
Product Specifications
Ile27-Pro250, with a C-terminal 10-His tag
Analysis
Product Datasheets
Carrier Free
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.
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.
2200-SE/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in HEPES and NaCl with Trehalose. |
| Reconstitution | Reconstitute at 200 μg/mL in sterile PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
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).
- Morgan, J.G. et al. (1991) J. Immunol. 147:3210.
- Zimmer, M. et al. (1992) Proc. Natl. Acad. Sci. USA 89:8215.
- Iverson, L.F. et al. (1997) Nat. Struct. Biol. 4:265.
- Gautam, N. et al. (2001) Nat. Med. 7:1123.
Citations for Recombinant Human Azurocidin/CAP37/HBP Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 3
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Heparin-binding protein is important for vascular leak in sepsis
Authors: Adam Linder
Intensive Care Med Exp, 2016-10-04;4(1):33.
Species: Human
Sample Types: Whole Cells
Applications: Bioassay -
Phenol-soluble modulin ?4 mediates Staphylococcus aureus-associated vascular leakage by stimulating heparin-binding protein release from neutrophils
Sci Rep, 2016-07-07;6(0):29373.
Species: Human
Sample Types: Cell Culture Supernates
Applications: ELISA (Standard) -
Low anticoagulant heparin targets multiple sites of inflammation, suppresses heparin-induced thrombocytopenia, and inhibits interaction of RAGE with its ligands.
Authors: Rao NV, Argyle B, Xu X, Reynolds PR, Walenga JM, Prechel M, Prestwich GD, MacArthur RB, Walters BB, Hoidal JR, Kennedy TP
Am. J. Physiol., Cell Physiol., 2010-04-07;299(1):C97-110.
Applications: Binding Assay
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