Description
RP1-Carboxypeptidase-A5 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A5. The antibody is made to a synthetic peptide based on the propeptide domain of human carboxypeptidase-A5. 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 A5 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 CPA5 and the other forms ranges from 36-60% identity at the amino acid level. CPA5 is 60.4% identical to CPA1, 54% with CPA2, 36.6% with CPA3, 51.1% with CPA4 and 36.5% 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 37.3% for CPB1 and 37% for CPB2. Thus CPA5 would seem most similar to CPA1 by sequence homology, but relatively little is known about the substrate specificity or distribution of CPA5. Although Carboxypeptidase A1 is considered a digestive proteinase, produced by the acinar cells of the pancreas, Carboxypeptidase A5 is not considered a pancreatic proteinase. CPA5 has been reported to be produced in the testis and pituitary in mice, and in very low levels in the human tissues examined thus far. The human CPA5 gene is also a candidate for imprinting, and has been localized to a gene cluster involved in imprinting offspring with parental gene expression patterns. Carboxypeptidase A5 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, but it is still unclear which enzyme activates CPA5. Cleavage of CPA5 is thought to occur at Arg126-Leu127, and the recombinant CPA5 was successfully activated by the proprotein convertase PC4. The catalytic domain chelates the zinc atom using residues His196, Glu199 and His323, with Glu397 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-A5 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A5. The antibody is made to a synthetic peptide based on the amino end of the catalytic domain of human carboxypeptidase-A5. 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 A5 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 CPA5 and the other forms ranges from 36-60% identity at the amino acid level. CPA5 is 60.4% identical to CPA1, 54% with CPA2, 36.6% with CPA3, 51.1% with CPA4 and 36.5% 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 37.3% for CPB1 and 37% for CPB2. Thus CPA5 would seem most similar to CPA1 by sequence homology, but relatively little is known about the substrate specificity or distribution of CPA5. Although Carboxypeptidase A1 is considered a digestive proteinase, produced by the acinar cells of the pancreas, Carboxypeptidase A5 is not considered a pancreatic proteinase. CPA5 has been reported to be produced in the testis and pituitary in mice, and in very low levels in the human tissues examined thus far. The human CPA5 gene is also a candidate for imprinting, and has been localized to a gene cluster involved in imprinting offspring with parental gene expression patterns. Carboxypeptidase A5 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, but it is still unclear which enzyme activates CPA5. Cleavage of CPA5 is thought to occur at Arg126-Leu127, and the recombinant CPA5 was successfully activated by the proprotein convertase PC4. The catalytic domain chelates the zinc atom using residues His196, Glu199 and His323, with Glu397 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-A5 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A5. The antibody is made to a synthetic peptide based on the carboxy end of the catalytic domain of human carboxypeptidase-A5. 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 A5 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 CPA5 and the other forms ranges from 36-60% identity at the amino acid level. CPA5 is 60.4% identical to CPA1, 54% with CPA2, 36.6% with CPA3, 51.1% with CPA4 and 36.5% 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 37.3% for CPB1 and 37% for CPB2. Thus CPA5 would seem most similar to CPA1 by sequence homology, but relatively little is known about the substrate specificity or distribution of CPA5. Although Carboxypeptidase A1 is considered a digestive proteinase, produced by the acinar cells of the pancreas, Carboxypeptidase A5 is not considered a pancreatic proteinase. CPA5 has been reported to be produced in the testis and pituitary in mice, and in very low levels in the human tissues examined thus far. The human CPA5 gene is also a candidate for imprinting, and has been localized to a gene cluster involved in imprinting offspring with parental gene expression patterns. Carboxypeptidase A5 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, but it is still unclear which enzyme activates CPA5. Cleavage of CPA5 is thought to occur at Arg126-Leu127, and the recombinant CPA5 was successfully activated by the proprotein convertase PC4. The catalytic domain chelates the zinc atom using residues His196, Glu199 and His323, with Glu397 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.
