Description
RP1- Azurocidin is a polyclonal antibody made to the protelytically inactive serine protease Azurocidin. The antibody is made to a synthetic peptide based on the aminoterminal end of mature human Azurocidin. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
Azurocidin, also known as Cationic Antimicrobial Protein, CAP37, Heparin-Binding Protein and HBP is a catalytically inactive member of the serine proteinase family, most closely related to proteinase-3 and elastase-2 (sharing 44 and 42% identity at the amino acid level respectively). Azurocidin is produced by neutrophils and stored in azurophil granules along with proteinase-3, elastase and cathepsin-G (the Seprocidins), as well as the defensin oligopeptides. It is not clear how much of the antimicrobial and antifungal activity should be ascribed to the defensins, but azurocidin was shown to increase vascular permeability of endothelial cells, to stimulate epithelial cell growth, and to stimulate cell migration. The proposed antimicrobial activity, along with the propensity of the granules to stain blue gave azurocidin its name, as did parallel observations that the protein binds to heparin. The vascular permeability mechanism is thought in involve binding of neutrophils to activated endothelial cells via integrin-ICAM interactions. The stimulis triggers in a release of azurocidin from the neutrophil granules, and a calcium-sensitive rearrangement of the endothelial cell cytoskeleton, resulting in intracellular gap formation. Azurocidin is also produced by HL-60 cells, and by a wider range of cells when stimulated by agonists such as TNF-alpha, and is thought to be a pro-inflammatory molecule. The released azurocidin is also thought to attract more mononuclear cells and neutrophils to wound areas. Azurocidin is structurally most similar to proteinase-3 and elastase-2, but lacks the catalytic histidine and serine residues. Mutation of the azurocidin structure to contain the classical HDS triad of the related serine proteinases yields an active enzyme. Interestingly, many of the functions of azurocidin can be blocked with the proteinase inhibitor aprotinin. The 251 amino acid azurocidin sequence encodes a protein with predicted mass of 26.9 kDa and a pI of 11.9. Glycosylation increases the apparent molecular weight to 29 kDa, and the quite basic pI explains much of the binding to heparin and to HS gags. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 months at -20C.
Description
RP2- Azurocidin is a polyclonal antibody made to the protelytically inactive serine protease Azurocidin. The antibody is made to a synthetic peptide based on the catalytic domain of human Azurocidin. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
Azurocidin, also known as Cationic Antimicrobial Protein, CAP37, Heparin-Binding Protein and HBP is a catalytically inactive member of the serine proteinase family, most closely related to proteinase-3 and elastase-2 (sharing 44 and 42% identity at the amino acid level respectively). Azurocidin is produced by neutrophils and stored in azurophil granules along with proteinase-3, elastase and cathepsin-G (the Seprocidins), as well as the defensin oligopeptides. It is not clear how much of the antimicrobial and antifungal activity should be ascribed to the defensins, but azurocidin was shown to increase vascular permeability of endothelial cells, to stimulate epithelial cell growth, and to stimulate cell migration. The proposed antimicrobial activity, along with the propensity of the granules to stain blue gave azurocidin its name, as did parallel observations that the protein binds to heparin. The vascular permeability mechanism is thought in involve binding of neutrophils to activated endothelial cells via integrin-ICAM interactions. The stimulis triggers in a release of azurocidin from the neutrophil granules, and a calcium-sensitive rearrangement of the endothelial cell cytoskeleton, resulting in intracellular gap formation. Azurocidin is also produced by HL-60 cells, and by a wider range of cells when stimulated by agonists such as TNF-alpha, and is thought to be a pro-inflammatory molecule. The released azurocidin is also thought to attract more mononuclear cells and neutrophils to wound areas. Azurocidin is structurally most similar to proteinase-3 and elastase-2, but lacks the catalytic histidine and serine residues. Mutation of the azurocidin structure to contain the classical HDS triad of the related serine proteinases yields an active enzyme. Interestingly, many of the functions of azurocidin can be blocked with the proteinase inhibitor aprotinin. The 251 amino acid azurocidin sequence encodes a protein with predicted mass of 26.9 kDa and a pI of 11.9. Glycosylation increases the apparent molecular weight to 29 kDa, and the quite basic pI explains much of the binding to heparin and to HS gags. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 months at -20C.
Description
RP3- Azurocidin is a polyclonal antibody made to the protelytically inactive serine protease Azurocidin. The antibody is made to a synthetic peptide based on the carboxyterminal end of human Azurocidin. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.
Use
Azurocidin, also known as Cationic Antimicrobial Protein, CAP37, Heparin-Binding Protein and HBP is a catalytically inactive member of the serine proteinase family, most closely related to proteinase-3 and elastase-2 (sharing 44 and 42% identity at the amino acid level respectively). Azurocidin is produced by neutrophils and stored in azurophil granules along with proteinase-3, elastase and cathepsin-G (the Seprocidins), as well as the defensin oligopeptides. It is not clear how much of the antimicrobial and antifungal activity should be ascribed to the defensins, but azurocidin was shown to increase vascular permeability of endothelial cells, to stimulate epithelial cell growth, and to stimulate cell migration. The proposed antimicrobial activity, along with the propensity of the granules to stain blue gave azurocidin its name, as did parallel observations that the protein binds to heparin. The vascular permeability mechanism is thought in involve binding of neutrophils to activated endothelial cells via integrin-ICAM interactions. The stimulis triggers in a release of azurocidin from the neutrophil granules, and a calcium-sensitive rearrangement of the endothelial cell cytoskeleton, resulting in intracellular gap formation. Azurocidin is also produced by HL-60 cells, and by a wider range of cells when stimulated by agonists such as TNF-alpha, and is thought to be a pro-inflammatory molecule. The released azurocidin is also thought to attract more mononuclear cells and neutrophils to wound areas. Azurocidin is structurally most similar to proteinase-3 and elastase-2, but lacks the catalytic histidine and serine residues. Mutation of the azurocidin structure to contain the classical HDS triad of the related serine proteinases yields an active enzyme. Interestingly, many of the functions of azurocidin can be blocked with the proteinase inhibitor aprotinin. The 251 amino acid azurocidin sequence encodes a protein with predicted mass of 26.9 kDa and a pI of 11.9. Glycosylation increases the apparent molecular weight to 29 kDa, and the quite basic pI explains much of the binding to heparin and to HS gags. A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates. Higher concentrations of antibody may be needed for samples from more distantly related species. FOR RESEARCH USE ONLY; NOT FOR USE IN HUMANS.
Storage
The undiluted antibody solution is stable for approximately 12 months at -20C.
