Human Azurocidin/CAP37/HBP Alexa Fluor® 532-conjugated Antibody

Catalog #: AF2200X Datasheet
Catalog # Availability Size / Price Qty
AF2200X-100UG
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Human Azurocidin/CAP37/HBP Alexa Fluor® 532-conjugated Antibody Summary

Species Reactivity
Human
Specificity
Detects human Azurocidin/CAP37/HBP in direct ELISAs and Western blots.
Source
Polyclonal Goat IgG
Purification
Antigen Affinity-purified
Immunogen
Mouse myeloma cell line NS0-derived recombinant human Azurocidin/CAP37/HBP
Ile27-Pro250
Accession # P20160
Formulation
Supplied 0.2mg/ml in 1X PBS with RDF1 and 0.09% Sodium Azide
Label
Alexa Fluor 532 (Excitation= 534 nm, Emission= 553 nm)

Applications

Recommended Concentration
Sample
Western Blot
Optimal dilution of this antibody should be experimentally determined.
 
Immunoprecipitation
Optimal dilution of this antibody should be experimentally determined.
 

Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.

Preparation and Storage

Shipping
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze. 12 months from date of receipt, 2 to 8 °C as supplied

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).

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

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