Description
RP1-Proteinase-3 is a polyclonal antibody made to the serine protease proteinase-3. The antibody is made to a synthetic peptide based on the aminoterminal end of mature human proteinase-3. 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
Proteinase-3, also known as Myeloblastin, Leukocyte proteinase-3, PR-3, AGP-7, Azurophilic Granule Protein-7, P29, Neutrophil Proteinase-4, NP-4 and Wegener Autoantigen is a member of the serine proteinase family, most closely related to and elastase-2 and azurocidin (sharing 55 and 43% identity at the amino acid level respectively). Proteinase-3 is produced by neutrophils and stored in azurophil granules along with azurocidin, elastase-2 and cathepsin-G (the Seprocidins), as well as the defensin oligopeptides. The pancreatic elastases, proteinase-3 and cathepsin-G are also members of the chymotrypsin-like PA clade, using the MEROPS terminology, and are in the S1A family. These serine proteinases all share a similar catalytic domain topology, with a canonical HDS catalytic triad in the catalytic domain. Elastase-2, proteinase-3 and the pancreatic elastases have pH optima near neutral, but the pancreatic elastases are much more efficient as elastases. Proteinase-3 also cleaves fibronectin, laminin, vitronectin, and collagen IV, but not collagens I, II, III, IV, VIII, IX. Proteinase-3 is not inhibited by the endiogenous serine proteinase inhibitor SLPI, which is a potent inhibitor of elastase-2. Proteinase-3 is mainly found in polymorphonuclear leukocytes, but at much lower levels than elastase-2. Auto-antibodies to proteinase-3 are thought to cause Wegener's granulomatosis (WG), and are referred to as ANCA (anti-neutrophil cytoplasmic antibodies). The 256 amino acid proteinase-3sequence encodes a protein with predicted mass of 27.8 kDa and a pI of 9.9. Glycosylation increases the apparent molecular weight to 32 kDa, and the basic pI is still much less basic than that of azurocidin or elastase-2, suggesting weaker interactions with heparin and HS gags and differential localization. Like elastase-2, proteinase-3 is activated by a cleavage of the animoterminal end, as well as removal of the carboxyterminal tail. 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-Proteinase-3 is a polyclonal antibody made to the serine protease proteinase-3. The antibody is made to a synthetic peptide based on the catalytic domain human proteinase-3, following the catalytic aspartic acid. 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
Proteinase-3, also known as Myeloblastin, Leukocyte proteinase-3, PR-3, AGP-7, Azurophilic Granule Protein-7, P29, Neutrophil Proteinase-4, NP-4 and Wegener Autoantigen is a member of the serine proteinase family, most closely related to and elastase-2 and azurocidin (sharing 55 and 43% identity at the amino acid level respectively). Proteinase-3 is produced by neutrophils and stored in azurophil granules along with azurocidin, elastase-2 and cathepsin-G (the Seprocidins), as well as the defensin oligopeptides. The pancreatic elastases, proteinase-3 and cathepsin-G are also members of the chymotrypsin-like PA clade, using the MEROPS terminology, and are in the S1A family. These serine proteinases all share a similar catalytic domain topology, with a canonical HDS catalytic triad in the catalytic domain. Elastase-2, proteinase-3 and the pancreatic elastases have pH optima near neutral, but the pancreatic elastases are much more efficient as elastases. Proteinase-3 also cleaves fibronectin, laminin, vitronectin, and collagen IV, but not collagens I, II, III, IV, VIII, IX. Proteinase-3 is not inhibited by the endiogenous serine proteinase inhibitor SLPI, which is a potent inhibitor of elastase-2. Proteinase-3 is mainly found in polymorphonuclear leukocytes, but at much lower levels than elastase-2. Auto-antibodies to proteinase-3 are thought to cause Wegener's granulomatosis (WG), and are referred to as ANCA (anti-neutrophil cytoplasmic antibodies). The 256 amino acid proteinase-3sequence encodes a protein with predicted mass of 27.8 kDa and a pI of 9.9. Glycosylation increases the apparent molecular weight to 32 kDa, and the basic pI is still much less basic than that of azurocidin or elastase-2, suggesting weaker interactions with heparin and HS gags and differential localization. Like elastase-2, proteinase-3 is activated by a cleavage of the animoterminal end, as well as removal of the carboxyterminal tail. 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-Proteinase-3 is a polyclonal antibody made to the serine protease proteinase-3. The antibody is made to a synthetic peptide based on the catalytic domain human proteinase-3, before the catalytic serine acid. 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
Proteinase-3, also known as Myeloblastin, Leukocyte proteinase-3, PR-3, AGP-7, Azurophilic Granule Protein-7, P29, Neutrophil Proteinase-4, NP-4 and Wegener Autoantigen is a member of the serine proteinase family, most closely related to and elastase-2 and azurocidin (sharing 55 and 43% identity at the amino acid level respectively). Proteinase-3 is produced by neutrophils and stored in azurophil granules along with azurocidin, elastase-2 and cathepsin-G (the Seprocidins), as well as the defensin oligopeptides. The pancreatic elastases, proteinase-3 and cathepsin-G are also members of the chymotrypsin-like PA clade, using the MEROPS terminology, and are in the S1A family. These serine proteinases all share a similar catalytic domain topology, with a canonical HDS catalytic triad in the catalytic domain. Elastase-2, proteinase-3 and the pancreatic elastases have pH optima near neutral, but the pancreatic elastases are much more efficient as elastases. Proteinase-3 also cleaves fibronectin, laminin, vitronectin, and collagen IV, but not collagens I, II, III, IV, VIII, IX. Proteinase-3 is not inhibited by the endiogenous serine proteinase inhibitor SLPI, which is a potent inhibitor of elastase-2. Proteinase-3 is mainly found in polymorphonuclear leukocytes, but at much lower levels than elastase-2. Auto-antibodies to proteinase-3 are thought to cause Wegener's granulomatosis (WG), and are referred to as ANCA (anti-neutrophil cytoplasmic antibodies). The 256 amino acid proteinase-3sequence encodes a protein with predicted mass of 27.8 kDa and a pI of 9.9. Glycosylation increases the apparent molecular weight to 32 kDa, and the basic pI is still much less basic than that of azurocidin or elastase-2, suggesting weaker interactions with heparin and HS gags and differential localization. Like elastase-2, proteinase-3 is activated by a cleavage of the animoterminal end, as well as removal of the carboxyterminal tail. 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
RP4-Proteinase-3 is a polyclonal antibody made to the serine protease proteinase-3. The antibody is made to a synthetic peptide based on the catalytic domain human proteinase-3, following the catalytic histidine. 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
Proteinase-3, also known as Myeloblastin, Leukocyte proteinase-3, PR-3, AGP-7, Azurophilic Granule Protein-7, P29, Neutrophil Proteinase-4, NP-4 and Wegener Autoantigen is a member of the serine proteinase family, most closely related to and elastase-2 and azurocidin (sharing 55 and 43% identity at the amino acid level respectively). Proteinase-3 is produced by neutrophils and stored in azurophil granules along with azurocidin, elastase-2 and cathepsin-G (the Seprocidins), as well as the defensin oligopeptides. The pancreatic elastases, proteinase-3 and cathepsin-G are also members of the chymotrypsin-like PA clade, using the MEROPS terminology, and are in the S1A family. These serine proteinases all share a similar catalytic domain topology, with a canonical HDS catalytic triad in the catalytic domain. Elastase-2, proteinase-3 and the pancreatic elastases have pH optima near neutral, but the pancreatic elastases are much more efficient as elastases. Proteinase-3 also cleaves fibronectin, laminin, vitronectin, and collagen IV, but not collagens I, II, III, IV, VIII, IX. Proteinase-3 is not inhibited by the endiogenous serine proteinase inhibitor SLPI, which is a potent inhibitor of elastase-2. Proteinase-3 is mainly found in polymorphonuclear leukocytes, but at much lower levels than elastase-2. Auto-antibodies to proteinase-3 are thought to cause Wegener's granulomatosis (WG), and are referred to as ANCA (anti-neutrophil cytoplasmic antibodies). The 256 amino acid proteinase-3sequence encodes a protein with predicted mass of 27.8 kDa and a pI of 9.9. Glycosylation increases the apparent molecular weight to 32 kDa, and the basic pI is still much less basic than that of azurocidin or elastase-2, suggesting weaker interactions with heparin and HS gags and differential localization. Like elastase-2, proteinase-3 is activated by a cleavage of the animoterminal end, as well as removal of the carboxyterminal tail. 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
RP5-Proteinase-3 is a polyclonal antibody made to the serine protease proteinase-3. The antibody is made to a synthetic peptide based on the carboxyterminal end of human proteinase-3. 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
Proteinase-3, also known as Myeloblastin, Leukocyte proteinase-3, PR-3, AGP-7, Azurophilic Granule Protein-7, P29, Neutrophil Proteinase-4, NP-4 and Wegener Autoantigen is a member of the serine proteinase family, most closely related to and elastase-2 and azurocidin (sharing 55 and 43% identity at the amino acid level respectively). Proteinase-3 is produced by neutrophils and stored in azurophil granules along with azurocidin, elastase-2 and cathepsin-G (the Seprocidins), as well as the defensin oligopeptides. The pancreatic elastases, proteinase-3 and cathepsin-G are also members of the chymotrypsin-like PA clade, using the MEROPS terminology, and are in the S1A family. These serine proteinases all share a similar catalytic domain topology, with a canonical HDS catalytic triad in the catalytic domain. Elastase-2, proteinase-3 and the pancreatic elastases have pH optima near neutral, but the pancreatic elastases are much more efficient as elastases. Proteinase-3 also cleaves fibronectin, laminin, vitronectin, and collagen IV, but not collagens I, II, III, IV, VIII, IX. Proteinase-3 is not inhibited by the endiogenous serine proteinase inhibitor SLPI, which is a potent inhibitor of elastase-2. Proteinase-3 is mainly found in polymorphonuclear leukocytes, but at much lower levels than elastase-2. Auto-antibodies to proteinase-3 are thought to cause Wegener's granulomatosis (WG), and are referred to as ANCA (anti-neutrophil cytoplasmic antibodies). The 256 amino acid proteinase-3sequence encodes a protein with predicted mass of 27.8 kDa and a pI of 9.9. Glycosylation increases the apparent molecular weight to 32 kDa, and the basic pI is still much less basic than that of azurocidin or elastase-2, suggesting weaker interactions with heparin and HS gags and differential localization. Like elastase-2, proteinase-3 is activated by a cleavage of the animoterminal end, as well as removal of the carboxyterminal tail. 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.