Description
RP1- Elastase-2 is a polyclonal antibody made to the serine protease elastase-2. The antibody is made to a synthetic peptide based on the aminoterminal end of mature human elastase-2. 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
Elastase-2, also known as Leukocyte Elastase, Neutrophil Elastase, NE, PMN Elastase, Bone Marrow Serine Proteinase, Medullasin, Human Leukocyte Elastase and HLE is a member of the serine proteinase family, most closely related to proteinase-3 and azurocidin (sharing 55 and 44% identity at the amino acid level respectively). Elastase-2 is produced by neutrophils and stored in azurophil granules along with proteinase-3, azurocidin and cathepsin-G (the Seprocidins), as well as the defensin oligopeptides. The name elastase is confusing: it applies to the metalloproteinase HME (Human Metallo Elastase, MMP-12), to the pancreatic elastases-I and II, as well as elastase-2. The MMP-12 elastase is structurally dissimilar to elastase-2, but the pancreatic elastases 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 and the pancreatic elastases have pH optima near neutral, but the pancreatic elastases are much more efficient as elastases. Elastase-2 also cleaves fibronectin, laminin, and collagens I, II, III, IV, VIII, IX, and XI, cleaves and inactivates Protein-C, alpha2-antiplasmin, alpha1-antichymotrypsin, TIMP-1, and cleaves and activates Factor V. Elastase-2 is mainly found in polymorphonuclear leukocytes, where it can amount to as much a 3 ug/106 cells. The combined inhibition of proteinase inhibitors, activation of other proteinases, and cleavage of elastin and collagens explains the destructive potential of elastase-2 in diseases such as emphasema, as well as the beneficial effects of the enzyme in killing bacteria. Much lower amounts are found in monocytes. Mature leukocytes stop producing elastse-2 but can dump granules containing elastase-2 rapidly on stimulus. Monocytes start out making elastase-2, but when they differentiate into macrophages they switch to MMP-12 as the dominant elastase. The 267 amino acid elastase-2 sequence encodes a protein with predicted mass of 28.5 kDa and a pI of 12.2. Glycosylation increases the apparent molecular weight to 32 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-Elastase-2 is a polyclonal antibody made to the serine protease elastase-2. The antibody is made to a synthetic peptide based on the catalytic domain of human elastase-2. 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
Elastase-2, also known as Leukocyte Elastase, Neutrophil Elastase, NE, PMN Elastase, Bone Marrow Serine Proteinase, Medullasin, Human Leukocyte Elastase and HLE is a member of the serine proteinase family, most closely related to proteinase-3 and azurocidin (sharing 55 and 44% identity at the amino acid level respectively). Elastase-2 is produced by neutrophils and stored in azurophil granules along with proteinase-3, azurocidin and cathepsin-G (the Seprocidins), as well as the defensin oligopeptides. The name elastase is confusing: it applies to the metalloproteinase HME (Human Metallo Elastase, MMP-12), to the pancreatic elastases-I and II, as well as elastase-2. The MMP-12 elastase is structurally dissimilar to elastase-2, but the pancreatic elastases 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 and the pancreatic elastases have pH optima near neutral, but the pancreatic elastases are much more efficient as elastases. Elastase-2 also cleaves fibronectin, laminin, and collagens I, II, III, IV, VIII, IX, and XI, cleaves and inactivates Protein-C, alpha2-antiplasmin, alpha1-antichymotrypsin, TIMP-1, and cleaves and activates Factor V. Elastase-2 is mainly found in polymorphonuclear leukocytes, where it can amount to as much a 3 ug/106 cells. The combined inhibition of proteinase inhibitors, activation of other proteinases, and cleavage of elastin and collagens explains the destructive potential of elastase-2 in diseases such as emphasema, as well as the beneficial effects of the enzyme in killing bacteria. Much lower amounts are found in monocytes. Mature leukocytes stop producing elastse-2 but can dump granules containing elastase-2 rapidly on stimulus. Monocytes start out making elastase-2, but when they differentiate into macrophages they switch to MMP-12 as the dominant elastase. The 267 amino acid elastase-2 sequence encodes a protein with predicted mass of 28.5 kDa and a pI of 12.2. Glycosylation increases the apparent molecular weight to 32 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-Elastase-2 is a polyclonal antibody made to the serine protease elastase-2. The antibody is made to a synthetic peptide based on the carboxyterminal end of human elastase-2. 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
Elastase-2, also known as Leukocyte Elastase, Neutrophil Elastase, NE, PMN Elastase, Bone Marrow Serine Proteinase, Medullasin, Human Leukocyte Elastase and HLE is a member of the serine proteinase family, most closely related to proteinase-3 and azurocidin (sharing 55 and 44% identity at the amino acid level respectively). Elastase-2 is produced by neutrophils and stored in azurophil granules along with proteinase-3, azurocidin and cathepsin-G (the Seprocidins), as well as the defensin oligopeptides. The name elastase is confusing: it applies to the metalloproteinase HME (Human Metallo Elastase, MMP-12), to the pancreatic elastases-I and II, as well as elastase-2. The MMP-12 elastase is structurally dissimilar to elastase-2, but the pancreatic elastases 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 and the pancreatic elastases have pH optima near neutral, but the pancreatic elastases are much more efficient as elastases. Elastase-2 also cleaves fibronectin, laminin, and collagens I, II, III, IV, VIII, IX, and XI, cleaves and inactivates Protein-C, alpha2-antiplasmin, alpha1-antichymotrypsin, TIMP-1, and cleaves and activates Factor V. Elastase-2 is mainly found in polymorphonuclear leukocytes, where it can amount to as much a 3 ug/106 cells. The combined inhibition of proteinase inhibitors, activation of other proteinases, and cleavage of elastin and collagens explains the destructive potential of elastase-2 in diseases such as emphasema, as well as the beneficial effects of the enzyme in killing bacteria. Much lower amounts are found in monocytes. Mature leukocytes stop producing elastse-2 but can dump granules containing elastase-2 rapidly on stimulus. Monocytes start out making elastase-2, but when they differentiate into macrophages they switch to MMP-12 as the dominant elastase. The 267 amino acid elastase-2 sequence encodes a protein with predicted mass of 28.5 kDa and a pI of 12.2. Glycosylation increases the apparent molecular weight to 32 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.
