Description
RP1-Carboxypeptidase-A4 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A4. The antibody is made to a synthetic peptide based on the propeptide domain of human carboxypeptidase-A4. 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 A4 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 CPA4 and the other forms ranges from 35-63% identity at the amino acid level. CPA4 is 54.4% identical to CPA1, 63.8% with CPA2, 38.1% with CPA3, 51.1% with CPA5 and 38.6% 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 41.7% for CPB1 and 35.9 for CPB2. Thus CPA4 would seem most similar to CPA2 by sequence homology, but relatively little is known about the substrate specificity or distribution of CPA4. Although Carboxypeptidase A2 is considered a digestive proteinase, produced by the acinar cells of the pancreas, Carboxypeptidase A4 is not considered a pancreatic proteinase. CPA4 has been reported to be produced in the prostate, and may be involved in prostate cancer, since expression levels of CPA4 are reported to be low in normal tissues, and elevated in transformed tissues. CPA4 is also a candidate for imprinting, and has been localized to a gene cluster involved in imprinting offspring with parental gene expression patterns. Carboxypeptidase A4 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. Trypsin activates carboxypeptidase A2 in the duodenum by removing the propeptide domain, cleaving at Arg110-Glu111, but it is still unclear which enzyme activates CPA4. Cleavage of CPA4 occurs at Arg113-Ser114, and the sequence for CPA4 predicts an acidic pI of 6.2. The catalytic domain chelates the zinc atom using residues His181, Glu184 and His308, with Glu382 acting as the active nucleophile. The zinc binding site has the GHxHxREW motif conserved throughout the CPA and CPB groups. An endogenous inhibitor of CPA4, latexin, is produced by neuronal tissues and mast cells, and is known to form polymeric complexes. A crystal structure of CPA4 with latexin shows that latexin acts like a cystatin, which might give some clues to CPA4 function. 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-A4 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A4. The antibody is made to a synthetic peptide based on the amino end of the catalytic domain of human carboxypeptidase-A4. 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 A4 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 CPA4 and the other forms ranges from 35-63% identity at the amino acid level. CPA4 is 54.4% identical to CPA1, 63.8% with CPA2, 38.1% with CPA3, 51.1% with CPA5 and 38.6% 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 41.7% for CPB1 and 35.9 for CPB2. Thus CPA4 would seem most similar to CPA2 by sequence homology, but relatively little is known about the substrate specificity or distribution of CPA4. Although Carboxypeptidase A2 is considered a digestive proteinase, produced by the acinar cells of the pancreas, Carboxypeptidase A4 is not considered a pancreatic proteinase. CPA4 has been reported to be produced in the prostate, and may be involved in prostate cancer, since expression levels of CPA4 are reported to be low in normal tissues, and elevated in transformed tissues. CPA4 is also a candidate for imprinting, and has been localized to a gene cluster involved in imprinting offspring with parental gene expression patterns. Carboxypeptidase A4 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. Trypsin activates carboxypeptidase A2 in the duodenum by removing the propeptide domain, cleaving at Arg110-Glu111, but it is still unclear which enzyme activates CPA4. Cleavage of CPA4 occurs at Arg113-Ser114, and the sequence for CPA4 predicts an acidic pI of 6.2. The catalytic domain chelates the zinc atom using residues His181, Glu184 and His308, with Glu382 acting as the active nucleophile. The zinc binding site has the GHxHxREW motif conserved throughout the CPA and CPB groups. An endogenous inhibitor of CPA4, latexin, is produced by neuronal tissues and mast cells, and is known to form polymeric complexes. A crystal structure of CPA4 with latexin shows that latexin acts like a cystatin, which might give some clues to CPA4 function. 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-A4 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-A4. The antibody is made to a synthetic peptide based on the carboxy end of the catalytic domain of human carboxypeptidase-A4. 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 A4 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 CPA4 and the other forms ranges from 35-63% identity at the amino acid level. CPA4 is 54.4% identical to CPA1, 63.8% with CPA2, 38.1% with CPA3, 51.1% with CPA5 and 38.6% 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 41.7% for CPB1 and 35.9 for CPB2. Thus CPA4 would seem most similar to CPA2 by sequence homology, but relatively little is known about the substrate specificity or distribution of CPA4. Although Carboxypeptidase A2 is considered a digestive proteinase, produced by the acinar cells of the pancreas, Carboxypeptidase A4 is not considered a pancreatic proteinase. CPA4 has been reported to be produced in the prostate, and may be involved in prostate cancer, since expression levels of CPA4 are reported to be low in normal tissues, and elevated in transformed tissues. CPA4 is also a candidate for imprinting, and has been localized to a gene cluster involved in imprinting offspring with parental gene expression patterns. Carboxypeptidase A4 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. Trypsin activates carboxypeptidase A2 in the duodenum by removing the propeptide domain, cleaving at Arg110-Glu111, but it is still unclear which enzyme activates CPA4. Cleavage of CPA4 occurs at Arg113-Ser114, and the sequence for CPA4 predicts an acidic pI of 6.2. The catalytic domain chelates the zinc atom using residues His181, Glu184 and His308, with Glu382 acting as the active nucleophile. The zinc binding site has the GHxHxREW motif conserved throughout the CPA and CPB groups. An endogenous inhibitor of CPA4, latexin, is produced by neuronal tissues and mast cells, and is known to form polymeric complexes. A crystal structure of CPA4 with latexin shows that latexin acts like a cystatin, which might give some clues to CPA4 function. 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.
