Description
RP1-Carboxypeptidase-A3 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A3. The antibody is made to a synthetic peptide based on the propeptide domain of human carboxypeptidase-A3. 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
Human mast cells produce a battery of defensive proteinases that are released upon degranulation. The MC(TC) mast cells contain the serine proteinases mast-cell tryptase , cathepsin G, chymase and carboxypeptidase A3 (MCP), while the MCT mast cells are thought to contain mainly the tryptases. Null mutant mice lacking carboxypeptidase A3 have mast cells that fail to mature competent mast cells, thus carboxypeptidsase A3 plays an important role in the development of mast cells. Carboxypeptidase A3 (CPA3) is a zinc metalloproteinase of the MC clan, in the M14A family of MEROPS designations. Also known as mast cell carboxypeptidase, understanding of CPA3 is hampered by the confusion in the literature with carboxypeptidase A1. In addition, comparative studies with other species are often applied to human CPA3, but it is clear that there are significant differences amongst mammalian species in their carboxypeptidases. The zinc carboxypeptidase family is divided into those enzymes with substrate preferences for an aliphatic residues in the P1' position (the CPA group) and those that prefer basic P1' residues (the CPB group). In humans the CPA group contains 6 members, CPA1-6, and the CPB group 2 members, CPB1-2. The sequence homology between CPA3 and the other forms ranges from 36-48% identity at the amino acid level. CPA3 is 36.9% identical to CPA1, 38.2% with CPA2, 38.1% with CPA4, 36.6% with CPA5 and 41% with CPA6, by comparing the archetype sequences. Some splice variants within the group increase the diversity amongst the CPA group. The identity between CPA3and the CPB group is 48.8% for CPB1 and 40.5% for CPB2, thus CPA3 more closely resembles the CPB enzymes than the CPA group. Carboxypeptidase A3 is produced by the mast cells as a zymogen, and the pI of 9.16 drives an interaction with proteoglycans in the storage granules. The propeptide domain is presumed to be removed before storage in the granules, and cathepsin E is thought to be involved, since null mutant mice lacking cathepsin E accumulate pro-CPA3 in their mast cells. Carboxypeptidase A3 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. The catalytic domain chelates the zinc atom using residues His176, Glu179 and His304, with Glu378 acting as the active nucleophile. The zinc binding site has the GHxHxREW motif conserved throughout the CPA and CPB groups. An endogenous inhibitor of CPA, latexin, is produced by neuronal tissues and mast cells, and is known to form polymeric complexes. 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 12 months at -20C.
Description
RP2-Carboxypeptidase-A3 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A3. The antibody is made to a synthetic peptide based on the amino end of the catalytic domain of human carboxypeptidase-A3. 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
Human mast cells produce a battery of defensive proteinases that are released upon degranulation. The MC(TC) mast cells contain the serine proteinases mast-cell tryptase , cathepsin G, chymase and carboxypeptidase A3 (MCP), while the MCT mast cells are thought to contain mainly the tryptases. Null mutant mice lacking carboxypeptidase A3 have mast cells that fail to mature competent mast cells, thus carboxypeptidsase A3 plays an important role in the development of mast cells. Carboxypeptidase A3 (CPA3) is a zinc metalloproteinase of the MC clan, in the M14A family of MEROPS designations. Also known as mast cell carboxypeptidase, understanding of CPA3 is hampered by the confusion in the literature with carboxypeptidase A1. In addition, comparative studies with other species are often applied to human CPA3, but it is clear that there are significant differences amongst mammalian species in their carboxypeptidases. The zinc carboxypeptidase family is divided into those enzymes with substrate preferences for an aliphatic residues in the P1' position (the CPA group) and those that prefer basic P1' residues (the CPB group). In humans the CPA group contains 6 members, CPA1-6, and the CPB group 2 members, CPB1-2. The sequence homology between CPA3 and the other forms ranges from 36-48% identity at the amino acid level. CPA3 is 36.9% identical to CPA1, 38.2% with CPA2, 38.1% with CPA4, 36.6% with CPA5 and 41% with CPA6, by comparing the archetype sequences. Some splice variants within the group increase the diversity amongst the CPA group. The identity between CPA3and the CPB group is 48.8% for CPB1 and 40.5% for CPB2, thus CPA3 more closely resembles the CPB enzymes than the CPA group. Carboxypeptidase A3 is produced by the mast cells as a zymogen, and the pI of 9.16 drives an interaction with proteoglycans in the storage granules. The propeptide domain is presumed to be removed before storage in the granules, and cathepsin E is thought to be involved, since null mutant mice lacking cathepsin E accumulate pro-CPA3 in their mast cells. Carboxypeptidase A3 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. The catalytic domain chelates the zinc atom using residues His176, Glu179 and His304, with Glu378 acting as the active nucleophile. The zinc binding site has the GHxHxREW motif conserved throughout the CPA and CPB groups. An endogenous inhibitor of CPA, latexin, is produced by neuronal tissues and mast cells, and is known to form polymeric complexes. 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 12 months at -20C.
Description
RP3-Carboxypeptidase-A3 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A3. The antibody is made to a synthetic peptide based on the carboxy end of the catalytic domain of human carboxypeptidase-A3. 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
Human mast cells produce a battery of defensive proteinases that are released upon degranulation. The MC(TC) mast cells contain the serine proteinases mast-cell tryptase , cathepsin G, chymase and carboxypeptidase A3 (MCP), while the MCT mast cells are thought to contain mainly the tryptases. Null mutant mice lacking carboxypeptidase A3 have mast cells that fail to mature competent mast cells, thus carboxypeptidsase A3 plays an important role in the development of mast cells. Carboxypeptidase A3 (CPA3) is a zinc metalloproteinase of the MC clan, in the M14A family of MEROPS designations. Also known as mast cell carboxypeptidase, understanding of CPA3 is hampered by the confusion in the literature with carboxypeptidase A1. In addition, comparative studies with other species are often applied to human CPA3, but it is clear that there are significant differences amongst mammalian species in their carboxypeptidases. The zinc carboxypeptidase family is divided into those enzymes with substrate preferences for an aliphatic residues in the P1' position (the CPA group) and those that prefer basic P1' residues (the CPB group). In humans the CPA group contains 6 members, CPA1-6, and the CPB group 2 members, CPB1-2. The sequence homology between CPA3 and the other forms ranges from 36-48% identity at the amino acid level. CPA3 is 36.9% identical to CPA1, 38.2% with CPA2, 38.1% with CPA4, 36.6% with CPA5 and 41% with CPA6, by comparing the archetype sequences. Some splice variants within the group increase the diversity amongst the CPA group. The identity between CPA3and the CPB group is 48.8% for CPB1 and 40.5% for CPB2, thus CPA3 more closely resembles the CPB enzymes than the CPA group. Carboxypeptidase A3 is produced by the mast cells as a zymogen, and the pI of 9.16 drives an interaction with proteoglycans in the storage granules. The propeptide domain is presumed to be removed before storage in the granules, and cathepsin E is thought to be involved, since null mutant mice lacking cathepsin E accumulate pro-CPA3 in their mast cells. Carboxypeptidase A3 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. The catalytic domain chelates the zinc atom using residues His176, Glu179 and His304, with Glu378 acting as the active nucleophile. The zinc binding site has the GHxHxREW motif conserved throughout the CPA and CPB groups. An endogenous inhibitor of CPA, latexin, is produced by neuronal tissues and mast cells, and is known to form polymeric complexes. 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 12 months at -20C.
