Description
RP1-Carboxypeptidase-D is a rabbit polyclonal antibody made to the metallopeptidase carboxypeptidase-D. The antibody is made to a synthetic peptide based on the first catalytic domain of human carboxypeptidase-D. 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 D is a zinc metalloproteinase of the MC clan, in the M14A family of MEROPS designations. Serine carboxypeptiase D has historically shared the same name, and the name metallopcarboxypeptidase D was proposed to limit confusion, but the serine proteinase seems to be limited to plants. Carboxypeptidase D was discovered independently as a hepatitis B virus-binding protein in duck liver cells, and a carboxypeptidase that partially compensated for carbopxypeptidase E in CPE null mutant mice. In addition to the mammalian and avian carboxypeptidase D, the drosophila mutant silver was identified as a CPD family mutation. Null mutations of CPD in drosophila are lethal, but those that decrease CPD activity are viable, and have altered wing morphology and pigmentation. Carboxypeptidase D is unique amongst the metallocarboxypeptidase family in having a mosaic catalytic domain, comprised of 2 active metallocarboxypeptidase domains, and a third catalytic domain that does not contain the classical catalytic zinc binding site. The third domain is not thought to be an active enzyme, but is proposed to take on some of the propeptide domain functions of the other metallocarboxypeptidases. The two functional catalytic domains are thought to have different pH optima, allowing CPD to work over a wider pH or substrate range. The carboxyterminal end of CPD contains a transmembrane domain, followed by a cytoplasmic domain. The TM domain localizes the CPD to the trans-golgi membrane, and the cytoplasmic domain contains several different phosphorylation sites that help direct the trafficking and cycling of CPD to the cell surface. 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). Carboxypeptidase D is a CPB group enzyme, mainly cleaving arginine and lysine carboxyterminal residues. In the secretory pathway proprotein convertases such as furin cleave at paired basic sequences, leaving a carboxyterminal arginine or two that must be removed to produce the mature protein. The arginine removed by CPD is implicated in nitric oxide production. Full length CPD is a 1380 amino acid protein, with a 30 residue signal sequence. A shorter form is reported of 1079 amino acids, starting at a methionine 302 residues downstream from the long form, near the end of the first catalytic domain, but little is known about relative production levels or distribution. 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-D is a rabbit polyclonal antibody made to the metallopeptidase carboxypeptidase-D. The antibody is made to a synthetic peptide based on the first linker region, between catalytic domains 1 and 2 of human carboxypeptidase-D. 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 D is a zinc metalloproteinase of the MC clan, in the M14A family of MEROPS designations. Serine carboxypeptiase D has historically shared the same name, and the name metallopcarboxypeptidase D was proposed to limit confusion, but the serine proteinase seems to be limited to plants. Carboxypeptidase D was discovered independently as a hepatitis B virus-binding protein in duck liver cells, and a carboxypeptidase that partially compensated for carbopxypeptidase E in CPE null mutant mice. In addition to the mammalian and avian carboxypeptidase D, the drosophila mutant silver was identified as a CPD family mutation. Null mutations of CPD in drosophila are lethal, but those that decrease CPD activity are viable, and have altered wing morphology and pigmentation. Carboxypeptidase D is unique amongst the metallocarboxypeptidase family in having a mosaic catalytic domain, comprised of 2 active metallocarboxypeptidase domains, and a third catalytic domain that does not contain the classical catalytic zinc binding site. The third domain is not thought to be an active enzyme, but is proposed to take on some of the propeptide domain functions of the other metallocarboxypeptidases. The two functional catalytic domains are thought to have different pH optima, allowing CPD to work over a wider pH or substrate range. The carboxyterminal end of CPD contains a transmembrane domain, followed by a cytoplasmic domain. The TM domain localizes the CPD to the trans-golgi membrane, and the cytoplasmic domain contains several different phosphorylation sites that help direct the trafficking and cycling of CPD to the cell surface. 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). Carboxypeptidase D is a CPB group enzyme, mainly cleaving arginine and lysine carboxyterminal residues. In the secretory pathway proprotein convertases such as furin cleave at paired basic sequences, leaving a carboxyterminal arginine or two that must be removed to produce the mature protein. The arginine removed by CPD is implicated in nitric oxide production. Full length CPD is a 1380 amino acid protein, with a 30 residue signal sequence. A shorter form is reported of 1079 amino acids, starting at a methionine 302 residues downstream from the long form, near the end of the first catalytic domain, but little is known about relative production levels or distribution. 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-D is a rabbit polyclonal antibody made to the metallopeptidase carboxypeptidase-D. The antibody is made to a synthetic peptide based on the second linker region, between catalytic domains 2 and 3 of human carboxypeptidase-D. 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 D is a zinc metalloproteinase of the MC clan, in the M14A family of MEROPS designations. Serine carboxypeptiase D has historically shared the same name, and the name metallopcarboxypeptidase D was proposed to limit confusion, but the serine proteinase seems to be limited to plants. Carboxypeptidase D was discovered independently as a hepatitis B virus-binding protein in duck liver cells, and a carboxypeptidase that partially compensated for carbopxypeptidase E in CPE null mutant mice. In addition to the mammalian and avian carboxypeptidase D, the drosophila mutant silver was identified as a CPD family mutation. Null mutations of CPD in drosophila are lethal, but those that decrease CPD activity are viable, and have altered wing morphology and pigmentation. Carboxypeptidase D is unique amongst the metallocarboxypeptidase family in having a mosaic catalytic domain, comprised of 2 active metallocarboxypeptidase domains, and a third catalytic domain that does not contain the classical catalytic zinc binding site. The third domain is not thought to be an active enzyme, but is proposed to take on some of the propeptide domain functions of the other metallocarboxypeptidases. The two functional catalytic domains are thought to have different pH optima, allowing CPD to work over a wider pH or substrate range. The carboxyterminal end of CPD contains a transmembrane domain, followed by a cytoplasmic domain. The TM domain localizes the CPD to the trans-golgi membrane, and the cytoplasmic domain contains several different phosphorylation sites that help direct the trafficking and cycling of CPD to the cell surface. 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). Carboxypeptidase D is a CPB group enzyme, mainly cleaving arginine and lysine carboxyterminal residues. In the secretory pathway proprotein convertases such as furin cleave at paired basic sequences, leaving a carboxyterminal arginine or two that must be removed to produce the mature protein. The arginine removed by CPD is implicated in nitric oxide production. Full length CPD is a 1380 amino acid protein, with a 30 residue signal sequence. A shorter form is reported of 1079 amino acids, starting at a methionine 302 residues downstream from the long form, near the end of the first catalytic domain, but little is known about relative production levels or distribution. 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
RP4-Carboxypeptidase-D is a rabbit polyclonal antibody made to the metallopeptidase carboxypeptidase-D. The antibody is made to a synthetic peptide based on the cytoplasmic domain of human carboxypeptidase-D. 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 D is a zinc metalloproteinase of the MC clan, in the M14A family of MEROPS designations. Serine carboxypeptiase D has historically shared the same name, and the name metallopcarboxypeptidase D was proposed to limit confusion, but the serine proteinase seems to be limited to plants. Carboxypeptidase D was discovered independently as a hepatitis B virus-binding protein in duck liver cells, and a carboxypeptidase that partially compensated for carbopxypeptidase E in CPE null mutant mice. In addition to the mammalian and avian carboxypeptidase D, the drosophila mutant silver was identified as a CPD family mutation. Null mutations of CPD in drosophila are lethal, but those that decrease CPD activity are viable, and have altered wing morphology and pigmentation. Carboxypeptidase D is unique amongst the metallocarboxypeptidase family in having a mosaic catalytic domain, comprised of 2 active metallocarboxypeptidase domains, and a third catalytic domain that does not contain the classical catalytic zinc binding site. The third domain is not thought to be an active enzyme, but is proposed to take on some of the propeptide domain functions of the other metallocarboxypeptidases. The two functional catalytic domains are thought to have different pH optima, allowing CPD to work over a wider pH or substrate range. The carboxyterminal end of CPD contains a transmembrane domain, followed by a cytoplasmic domain. The TM domain localizes the CPD to the trans-golgi membrane, and the cytoplasmic domain contains several different phosphorylation sites that help direct the trafficking and cycling of CPD to the cell surface. 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). Carboxypeptidase D is a CPB group enzyme, mainly cleaving arginine and lysine carboxyterminal residues. In the secretory pathway proprotein convertases such as furin cleave at paired basic sequences, leaving a carboxyterminal arginine or two that must be removed to produce the mature protein. The arginine removed by CPD is implicated in nitric oxide production. Full length CPD is a 1380 amino acid protein, with a 30 residue signal sequence. A shorter form is reported of 1079 amino acids, starting at a methionine 302 residues downstream from the long form, near the end of the first catalytic domain, but little is known about relative production levels or distribution. 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.
