Description
RP1-Carboxypeptidase-A1 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A1. The antibody is made to a synthetic peptide based on the propeptide domain of human carboxypeptidase-A1. 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
Carboxypeptidase A1 is a zinc metalloproteinase of the MC clan, in the M14A family of MEROPS designations. 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 CPA1 and the other forms ranges from 34-63% identity at the amino acid level. CPA1 is 62.8% identical to CPA2, 34.1% with CPA3, 53.5% with CPA4, 60.1% with CPA5 and 34% with CPA6, by comparing the archetype sequences. Some splice variants within the group increase the diversity amongst the CPA group. The identity between CPA1 and the CPB group is 40.4% for CPB1 and 34.4 for CPB2. Carboxypeptidase A1 is considered a digestive proteinase, produced by the acinar cells of the pancreas. Carboxypeptidase A1is secreted in zymogen form as a free monomer, or bound in a dimer with either Proproteinase E (PPE, Elastase-3) or Chymotrypsinogen C, and also as a heterotrimeric complex. Carboxypeptidase A1 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. Trypsin activates carboxypeptidase A1 in the duodenum by removing the propeptide domain, cleaving at Arg110-Ala111. The cleaved propeptide domain is thought to have potent inhibitory activity, in the low nanomolar kI range. The ternary complex acts as a reservoir, inhibiting the trypsin activation. The catalytic domain chelates the zinc atom using residues His179, Glu182 and His306, with Glu380 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-A1 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A1. The antibody is made to a synthetic peptide based on the amino end of the catalytic domain of human carboxypeptidase-A1. 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
Carboxypeptidase A1 is a zinc metalloproteinase of the MC clan, in the M14A family of MEROPS designations. 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 CPA1 and the other forms ranges from 34-63% identity at the amino acid level. CPA1 is 62.8% identical to CPA2, 34.1% with CPA3, 53.5% with CPA4, 60.1% with CPA5 and 34% with CPA6, by comparing the archetype sequences. Some splice variants within the group increase the diversity amongst the CPA group. The identity between CPA1 and the CPB group is 40.4% for CPB1 and 34.4 for CPB2. Carboxypeptidase A1 is considered a digestive proteinase, produced by the acinar cells of the pancreas. Carboxypeptidase A1is secreted in zymogen form as a free monomer, or bound in a dimer with either Proproteinase E (PPE, Elastase-3) or Chymotrypsinogen C, and also as a heterotrimeric complex. Carboxypeptidase A1 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. Trypsin activates carboxypeptidase A1 in the duodenum by removing the propeptide domain, cleaving at Arg110-Ala111. The cleaved propeptide domain is thought to have potent inhibitory activity, in the low nanomolar kI range. The ternary complex acts as a reservoir, inhibiting the trypsin activation. The catalytic domain chelates the zinc atom using residues His179, Glu182 and His306, with Glu380 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-A1 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A1. The antibody is made to a synthetic peptide based on the carboxy end of the catalytic domain of human carboxypeptidase-A1. 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
Carboxypeptidase A1 is a zinc metalloproteinase of the MC clan, in the M14A family of MEROPS designations. 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 CPA1 and the other forms ranges from 34-63% identity at the amino acid level. CPA1 is 62.8% identical to CPA2, 34.1% with CPA3, 53.5% with CPA4, 60.1% with CPA5 and 34% with CPA6, by comparing the archetype sequences. Some splice variants within the group increase the diversity amongst the CPA group. The identity between CPA1 and the CPB group is 40.4% for CPB1 and 34.4 for CPB2. Carboxypeptidase A1 is considered a digestive proteinase, produced by the acinar cells of the pancreas. Carboxypeptidase A1is secreted in zymogen form as a free monomer, or bound in a dimer with either Proproteinase E (PPE, Elastase-3) or Chymotrypsinogen C, and also as a heterotrimeric complex. Carboxypeptidase A1 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. Trypsin activates carboxypeptidase A1 in the duodenum by removing the propeptide domain, cleaving at Arg110-Ala111. The cleaved propeptide domain is thought to have potent inhibitory activity, in the low nanomolar kI range. The ternary complex acts as a reservoir, inhibiting the trypsin activation. The catalytic domain chelates the zinc atom using residues His179, Glu182 and His306, with Glu380 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.
