Description
RP1-Carboxypeptidase-O is a rabbit polyclonal antibody made to the metallopeptidase carboxypeptidase-O. The antibody is made to a synthetic peptide based on the aminoterminal end of human carboxypeptidase-O. 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 O is a zinc metalloproteinase of the MC clan, in the M14B family of MEROPS designations. Carboxypeptidase O was discovered in a search for enzymes that compensate for carboxypeptidase E in CPE null mutant mice. The fat/fat mouse lacks CPE, but still processes some of the substrates assumed to be CPE targets. The first carboxypeptidase that compensated for such activity was named carboxypeptidase D, and carboxypeptidase O was later discovered by cloning. Based on sequence homology, carboxypeptidase O is a member of the CPB group of carboxypeptidases, which show a preference for basic residues on the carboxyterminus, versus the CPA group, which prefers aliphatic residues. No information is available yet as to native substrates for CPO. The catalytic domain of carboxypeptidase O is most similar to the other CPB type carboxypeptidases, with His108, Glu111, His233 chelating the catalytic zinc, and the Glu310 acting as the active nucleophile. The domain structure contains a 20 residue signal sequence, a relatively short propeptide domain (relative to the other metallocarboxypeptidases) of 28 residues, and a catalytic domain of 282 residues. Carboxypeptidase O is a reported to encode a protein of 374 amino acid protein, with a predicted mass of 45.5 kDa and a pI of 6.7. A 428 amino acid form is reported that has a predicted mass of 48.6 kDa and a pI of 6.5. The longer form has a longer carboxyterminal end, but both forms contain intact catalytic domains. Little is known about relative production levels, activity or distribution of carboxypeptidase O at this time. The acidic pI of the carboxypeptidase O isoforms gives some clues to activity; the other metallocarboxypeptidases have acidic pI, and function in acidic environments. The exceptions are carboxypeptidases U, which has a pI of 7.54, and is found in circulation, and carboxypeptidase Z. It seems reasonable that carboxypeptidase O might function best in the slightly acidic environment of the trans-golgi network, but that is mere speculation. 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-O is a rabbit polyclonal antibody made to the metallopeptidase carboxypeptidase-O. The antibody is made to a synthetic peptide based on the aminoterminal end of the catalytic domain of human carboxypeptidase-O. 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 O is a zinc metalloproteinase of the MC clan, in the M14B family of MEROPS designations. Carboxypeptidase O was discovered in a search for enzymes that compensate for carboxypeptidase E in CPE null mutant mice. The fat/fat mouse lacks CPE, but still processes some of the substrates assumed to be CPE targets. The first carboxypeptidase that compensated for such activity was named carboxypeptidase D, and carboxypeptidase O was later discovered by cloning. Based on sequence homology, carboxypeptidase O is a member of the CPB group of carboxypeptidases, which show a preference for basic residues on the carboxyterminus, versus the CPA group, which prefers aliphatic residues. No information is available yet as to native substrates for CPO. The catalytic domain of carboxypeptidase O is most similar to the other CPB type carboxypeptidases, with His108, Glu111, His233 chelating the catalytic zinc, and the Glu310 acting as the active nucleophile. The domain structure contains a 20 residue signal sequence, a relatively short propeptide domain (relative to the other metallocarboxypeptidases) of 28 residues, and a catalytic domain of 282 residues. Carboxypeptidase O is a reported to encode a protein of 374 amino acid protein, with a predicted mass of 45.5 kDa and a pI of 6.7. A 428 amino acid form is reported that has a predicted mass of 48.6 kDa and a pI of 6.5. The longer form has a longer carboxyterminal end, but both forms contain intact catalytic domains. Little is known about relative production levels, activity or distribution of carboxypeptidase O at this time. The acidic pI of the carboxypeptidase O isoforms gives some clues to activity; the other metallocarboxypeptidases have acidic pI, and function in acidic environments. The exceptions are carboxypeptidases U, which has a pI of 7.54, and is found in circulation, and carboxypeptidase Z. It seems reasonable that carboxypeptidase O might function best in the slightly acidic environment of the trans-golgi network, but that is mere speculation. 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-O is a rabbit polyclonal antibody made to the metallopeptidase carboxypeptidase-O. The antibody is made to a synthetic peptide based on the carboxyterminal end of the catalytic domain of human carboxypeptidase-O. 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 O is a zinc metalloproteinase of the MC clan, in the M14B family of MEROPS designations. Carboxypeptidase O was discovered in a search for enzymes that compensate for carboxypeptidase E in CPE null mutant mice. The fat/fat mouse lacks CPE, but still processes some of the substrates assumed to be CPE targets. The first carboxypeptidase that compensated for such activity was named carboxypeptidase D, and carboxypeptidase O was later discovered by cloning. Based on sequence homology, carboxypeptidase O is a member of the CPB group of carboxypeptidases, which show a preference for basic residues on the carboxyterminus, versus the CPA group, which prefers aliphatic residues. No information is available yet as to native substrates for CPO. The catalytic domain of carboxypeptidase O is most similar to the other CPB type carboxypeptidases, with His108, Glu111, His233 chelating the catalytic zinc, and the Glu310 acting as the active nucleophile. The domain structure contains a 20 residue signal sequence, a relatively short propeptide domain (relative to the other metallocarboxypeptidases) of 28 residues, and a catalytic domain of 282 residues. Carboxypeptidase O is a reported to encode a protein of 374 amino acid protein, with a predicted mass of 45.5 kDa and a pI of 6.7. A 428 amino acid form is reported that has a predicted mass of 48.6 kDa and a pI of 6.5. The longer form has a longer carboxyterminal end, but both forms contain intact catalytic domains. Little is known about relative production levels, activity or distribution of carboxypeptidase O at this time. The acidic pI of the carboxypeptidase O isoforms gives some clues to activity; the other metallocarboxypeptidases have acidic pI, and function in acidic environments. The exceptions are carboxypeptidases U, which has a pI of 7.54, and is found in circulation, and carboxypeptidase Z. It seems reasonable that carboxypeptidase O might function best in the slightly acidic environment of the trans-golgi network, but that is mere speculation. 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.