Description
RP1-Carboxypeptidase-A6 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A6. The antibody is made to a synthetic peptide based on the propeptide domain of human carboxypeptidase-A6. 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 A6 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 CPA6 and the other forms ranges from 36-41% identity at the amino acid level. CPA6 is 37.5% identical to CPA1, 39.2% with CPA2, 41% with CPA3, 38.6% with CPA4 and 36.5% with CPA5, by comparing the archetype sequences. Some splice variants within the group increase the diversity amongst the CPA group. The identity between CPA6 and the CPB group is 40.5% for CPB1 and 38.3% for CPB2. Thus CPA6 would seem most similar to CPA3 by sequence homology, but the overall homology is relatively low compared to the more closely related CPA proteins. Carboxypeptidase A6 is not considered a pancreatic proteinase, such as carboxypeptidase A1. CPA6 messsage has been reported to be produced in the olfactory bulb and the epididymus in mice, and in very low levels in the human tissues examined thus far. Mutations in the human CPA6 gene are reportedly linked to Duane syndrome, in which occulomotor control is lessened, thought to be due in incomplete innervations of the orbital muscles of the eye. Expression of recombinant carboxypeptidase A6 in HEK cells led to secretion and of the protein in the cell culture media, and accumulation in the ECM, as might be expected for a protein with a predicted pI of 9.8. Carboxypeptidase A6 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. In recombinant CPA6 cells cotransfected with a proprotein convertase inhibitor the CPA6 failed to be cleaved, and it was postulated that PCs play a role in CPA6 cleavage and activation. Cleavage of CPA6 is thought to occur at Arg129-Ser130. The catalytic domain chelates the zinc atom using residues His196, Glu199 and His324, with Glu398 acting as the active nucleophile. The zinc binding site has the GHxHxREW motif conserved throughout the CPA and CPB groups. 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-A6 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A6. The antibody is made to a synthetic peptide based on the amino end of the catalytic domain of human carboxypeptidase-A6. 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 A6 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 CPA6 and the other forms ranges from 36-41% identity at the amino acid level. CPA6 is 37.5% identical to CPA1, 39.2% with CPA2, 41% with CPA3, 38.6% with CPA4 and 36.5% with CPA5, by comparing the archetype sequences. Some splice variants within the group increase the diversity amongst the CPA group. The identity between CPA6 and the CPB group is 40.5% for CPB1 and 38.3% for CPB2. Thus CPA6 would seem most similar to CPA3 by sequence homology, but the overall homology is relatively low compared to the more closely related CPA proteins. Carboxypeptidase A6 is not considered a pancreatic proteinase, such as carboxypeptidase A1. CPA6 messsage has been reported to be produced in the olfactory bulb and the epididymus in mice, and in very low levels in the human tissues examined thus far. Mutations in the human CPA6 gene are reportedly linked to Duane syndrome, in which occulomotor control is lessened, thought to be due in incomplete innervations of the orbital muscles of the eye. Expression of recombinant carboxypeptidase A6 in HEK cells led to secretion and of the protein in the cell culture media, and accumulation in the ECM, as might be expected for a protein with a predicted pI of 9.8. Carboxypeptidase A6 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. In recombinant CPA6 cells cotransfected with a proprotein convertase inhibitor the CPA6 failed to be cleaved, and it was postulated that PCs play a role in CPA6 cleavage and activation. Cleavage of CPA6 is thought to occur at Arg129-Ser130. The catalytic domain chelates the zinc atom using residues His196, Glu199 and His324, with Glu398 acting as the active nucleophile. The zinc binding site has the GHxHxREW motif conserved throughout the CPA and CPB groups. 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-A6 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A6. The antibody is made to a synthetic peptide based on the carboxy end of the catalytic domain of human carboxypeptidase-A6. 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 A6 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 CPA6 and the other forms ranges from 36-41% identity at the amino acid level. CPA6 is 37.5% identical to CPA1, 39.2% with CPA2, 41% with CPA3, 38.6% with CPA4 and 36.5% with CPA5, by comparing the archetype sequences. Some splice variants within the group increase the diversity amongst the CPA group. The identity between CPA6 and the CPB group is 40.5% for CPB1 and 38.3% for CPB2. Thus CPA6 would seem most similar to CPA3 by sequence homology, but the overall homology is relatively low compared to the more closely related CPA proteins. Carboxypeptidase A6 is not considered a pancreatic proteinase, such as carboxypeptidase A1. CPA6 messsage has been reported to be produced in the olfactory bulb and the epididymus in mice, and in very low levels in the human tissues examined thus far. Mutations in the human CPA6 gene are reportedly linked to Duane syndrome, in which occulomotor control is lessened, thought to be due in incomplete innervations of the orbital muscles of the eye. Expression of recombinant carboxypeptidase A6 in HEK cells led to secretion and of the protein in the cell culture media, and accumulation in the ECM, as might be expected for a protein with a predicted pI of 9.8. Carboxypeptidase A6 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. In recombinant CPA6 cells cotransfected with a proprotein convertase inhibitor the CPA6 failed to be cleaved, and it was postulated that PCs play a role in CPA6 cleavage and activation. Cleavage of CPA6 is thought to occur at Arg129-Ser130. The catalytic domain chelates the zinc atom using residues His196, Glu199 and His324, with Glu398 acting as the active nucleophile. The zinc binding site has the GHxHxREW motif conserved throughout the CPA and CPB groups. 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.
