Description
RP1-Carboxypeptidase-Z is a rabbit polyclonal antibody made to the metallopeptidase carboxypeptidase-Z. The antibody is made to a synthetic peptide based on the frizzled domain of human carboxypeptidase-Z. 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 Z is a zinc metalloproteinase of the MC clan, in the M14B family of MEROPS designations. Carboxypeptidase Z 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 Z was later discovered by cloning. Carboxypeptidase Z 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. Carboxypeptidase Z is unusual relative to the other carboxypeptidases in having a 'Frizzled' like domain in the propeptide region. The frizzled domain is involved in Wnt signaling, and the 133 residue frizzled domain follows a 19 residue signal sequence. It has been proposed that carboxypeptidase Z cleaves the Wnt precursors at the carboxytermuinal end, and it has been observed that carboxypeptidase Z is expressed in high levels in the developing placenta. The catalytic domain of carboxypeptidase Z is most similar to the other CPB type carboxypeptidases, with His248, Glu251, His 380 chelating the catalytic zinc, and the Glu472 acting as the active nucleophile. Full length CPZ is a 652 amino acid protein, with a predicted mass of 73.6 kDa and a pI of 8.8. A 641 amino acid form is reported that has a 11 residue deletion at the beginning of the frizzled domain, and has a predicted mass of 7.5 kDa and a pI of 8.9. A shorter form of 611 amino acids, truncated at the carboxyterminal end, with a predicted mass of 68.7 and a pI of 8.7 is also reported. All three forms contain the complete catalytic domain. Little is known about relative production levels, activity or distribution of the shorter forms. The basic pI of the carboxypeptidase Z isoforms gives some clues to activity; the other metallocarboxypeptidases have much more acidic pI, and function in acidic environments. The exception is carboxypeptidase U, which has a pI of 7.54, and is found in circulation, which has a pH range closer to the pI of carboxypeptidase Z. 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-Z is a rabbit polyclonal antibody made to the metallopeptidase carboxypeptidase-Z. The antibody is made to a synthetic peptide based on the amino end of the catalytic domain of human carboxypeptidase-Z. 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 Z is a zinc metalloproteinase of the MC clan, in the M14B family of MEROPS designations. Carboxypeptidase Z 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 Z was later discovered by cloning. Carboxypeptidase Z 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. Carboxypeptidase Z is unusual relative to the other carboxypeptidases in having a 'Frizzled' like domain in the propeptide region. The frizzled domain is involved in Wnt signaling, and the 133 residue frizzled domain follows a 19 residue signal sequence. It has been proposed that carboxypeptidase Z cleaves the Wnt precursors at the carboxytermuinal end, and it has been observed that carboxypeptidase Z is expressed in high levels in the developing placenta. The catalytic domain of carboxypeptidase Z is most similar to the other CPB type carboxypeptidases, with His248, Glu251, His 380 chelating the catalytic zinc, and the Glu472 acting as the active nucleophile. Full length CPZ is a 652 amino acid protein, with a predicted mass of 73.6 kDa and a pI of 8.8. A 641 amino acid form is reported that has a 11 residue deletion at the beginning of the frizzled domain, and has a predicted mass of 7.5 kDa and a pI of 8.9. A shorter form of 611 amino acids, truncated at the carboxyterminal end, with a predicted mass of 68.7 and a pI of 8.7 is also reported. All three forms contain the complete catalytic domain. Little is known about relative production levels, activity or distribution of the shorter forms. The basic pI of the carboxypeptidase Z isoforms gives some clues to activity; the other metallocarboxypeptidases have much more acidic pI, and function in acidic environments. The exception is carboxypeptidase U, which has a pI of 7.54, and is found in circulation, which has a pH range closer to the pI of carboxypeptidase Z. 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-Z is a rabbit polyclonal antibody made to the metallopeptidase carboxypeptidase-Z. The antibody is made to a synthetic peptide based on the carboxyterminal end of full length human carboxypeptidase-Z. 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 Z is a zinc metalloproteinase of the MC clan, in the M14B family of MEROPS designations. Carboxypeptidase Z 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 Z was later discovered by cloning. Carboxypeptidase Z 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. Carboxypeptidase Z is unusual relative to the other carboxypeptidases in having a 'Frizzled' like domain in the propeptide region. The frizzled domain is involved in Wnt signaling, and the 133 residue frizzled domain follows a 19 residue signal sequence. It has been proposed that carboxypeptidase Z cleaves the Wnt precursors at the carboxytermuinal end, and it has been observed that carboxypeptidase Z is expressed in high levels in the developing placenta. The catalytic domain of carboxypeptidase Z is most similar to the other CPB type carboxypeptidases, with His248, Glu251, His 380 chelating the catalytic zinc, and the Glu472 acting as the active nucleophile. Full length CPZ is a 652 amino acid protein, with a predicted mass of 73.6 kDa and a pI of 8.8. A 641 amino acid form is reported that has a 11 residue deletion at the beginning of the frizzled domain, and has a predicted mass of 7.5 kDa and a pI of 8.9. A shorter form of 611 amino acids, truncated at the carboxyterminal end, with a predicted mass of 68.7 and a pI of 8.7 is also reported. All three forms contain the complete catalytic domain. Little is known about relative production levels, activity or distribution of the shorter forms. The basic pI of the carboxypeptidase Z isoforms gives some clues to activity; the other metallocarboxypeptidases have much more acidic pI, and function in acidic environments. The exception is carboxypeptidase U, which has a pI of 7.54, and is found in circulation, which has a pH range closer to the pI of carboxypeptidase Z. 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.
