Description
RP1-Carboxypeptidase-X2 is a rabbit polyclonal antibody made to the metallopeptidase carboxypeptidase-X2. The antibody is made to a synthetic peptide based on the propeptide domain of human carboxypeptidase-X2. 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 X2 is a zinc metalloproteinase of the MC clan, in the M14B family of MEROPS designations. Carboxypeptidase X2 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 X1 and X2 were later discovered by cloning. Carboxypeptidase X2 shares 57% overall identity at the amino acid level with carboxypeptidase X1, and 59% identity with AEBP1. All three proteins contain atypical structure to their catalytic domains. AEBP1 was not thought to be an active proteinase, although there are reports of activity on some substrates, rather it is thought to fulfill roles in development and differentiation. Carboxypeptidase X1 and X2 share a similar feature with AEBP1, a discoidin-like/Factor 5/8-like domain, located between the propeptide domain and the putative catalytic domain. The catalytic domain of carboxypeptidase X2 contains a noncannonical sequence for the zinc binding site; GxHxxE, where the other CPB-like metallocarboxypeptidases have the GxHxREW motif. The positions of the other chelating histidine and the nucleophilic glutamic acid are also not in good alignment with the CPB group. That said, it is possible that CPX1 and CPX2 are active carboxypeptidases, although initial experiments showed no activity on a range of substrates. Full length CPX2 is a 756 amino acid protein, with a predicted mass of 85.9 kDa and a pI of 6.5. A 647 amino acid form is reported that starts at the second methionine, 110 residues downstream from the longer form, near the end of the propeptide domain, and has a predicted mass of 74 kDa and a pI of 6.2. A 511 amino acid long form is also reported, which starts at the fourth methionine, 246 residues after the long form, near the end of the discoidin-like domain. All three forms contain the complete catalytic domain. Little is known about relative production levels, activity or distribution of the shorter forms, and there is no information yet about the substrates or functions for the carboxypeptidase X2 protein. 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-X2 is a rabbit polyclonal antibody made to the metallopeptidase carboxypeptidase-X2. The antibody is made to a synthetic peptide based on the amino end of the catalytic domain of human carboxypeptidase-X2. 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 X2 is a zinc metalloproteinase of the MC clan, in the M14B family of MEROPS designations. Carboxypeptidase X2 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 X1 and X2 were later discovered by cloning. Carboxypeptidase X2 shares 57% overall identity at the amino acid level with carboxypeptidase X1, and 59% identity with AEBP1. All three proteins contain atypical structure to their catalytic domains. AEBP1 was not thought to be an active proteinase, although there are reports of activity on some substrates, rather it is thought to fulfill roles in development and differentiation. Carboxypeptidase X1 and X2 share a similar feature with AEBP1, a discoidin-like/Factor 5/8-like domain, located between the propeptide domain and the putative catalytic domain. The catalytic domain of carboxypeptidase X2 contains a noncannonical sequence for the zinc binding site; GxHxxE, where the other CPB-like metallocarboxypeptidases have the GxHxREW motif. The positions of the other chelating histidine and the nucleophilic glutamic acid are also not in good alignment with the CPB group. That said, it is possible that CPX1 and CPX2 are active carboxypeptidases, although initial experiments showed no activity on a range of substrates. Full length CPX2 is a 756 amino acid protein, with a predicted mass of 85.9 kDa and a pI of 6.5. A 647 amino acid form is reported that starts at the second methionine, 110 residues downstream from the longer form, near the end of the propeptide domain, and has a predicted mass of 74 kDa and a pI of 6.2. A 511 amino acid long form is also reported, which starts at the fourth methionine, 246 residues after the long form, near the end of the discoidin-like domain. All three forms contain the complete catalytic domain. Little is known about relative production levels, activity or distribution of the shorter forms, and there is no information yet about the substrates or functions for the carboxypeptidase X2 protein. 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-X2 is a rabbit polyclonal antibody made to the metallopeptidase carboxypeptidase-X2. The antibody is made to a synthetic peptide based on the carboxyterminal end of human carboxypeptidase-X2. 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 X2 is a zinc metalloproteinase of the MC clan, in the M14B family of MEROPS designations. Carboxypeptidase X2 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 X1 and X2 were later discovered by cloning. Carboxypeptidase X2 shares 57% overall identity at the amino acid level with carboxypeptidase X1, and 59% identity with AEBP1. All three proteins contain atypical structure to their catalytic domains. AEBP1 was not thought to be an active proteinase, although there are reports of activity on some substrates, rather it is thought to fulfill roles in development and differentiation. Carboxypeptidase X1 and X2 share a similar feature with AEBP1, a discoidin-like/Factor 5/8-like domain, located between the propeptide domain and the putative catalytic domain. The catalytic domain of carboxypeptidase X2 contains a noncannonical sequence for the zinc binding site; GxHxxE, where the other CPB-like metallocarboxypeptidases have the GxHxREW motif. The positions of the other chelating histidine and the nucleophilic glutamic acid are also not in good alignment with the CPB group. That said, it is possible that CPX1 and CPX2 are active carboxypeptidases, although initial experiments showed no activity on a range of substrates. Full length CPX2 is a 756 amino acid protein, with a predicted mass of 85.9 kDa and a pI of 6.5. A 647 amino acid form is reported that starts at the second methionine, 110 residues downstream from the longer form, near the end of the propeptide domain, and has a predicted mass of 74 kDa and a pI of 6.2. A 511 amino acid long form is also reported, which starts at the fourth methionine, 246 residues after the long form, near the end of the discoidin-like domain. All three forms contain the complete catalytic domain. Little is known about relative production levels, activity or distribution of the shorter forms, and there is no information yet about the substrates or functions for the carboxypeptidase X2 protein. 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.
