Description
RP1-Carboxypeptidase-B1 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-B1. The antibody is made to a synthetic peptide based on the propeptide domain of human carboxypeptidase-B1. 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 B1 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 CPB1 and the other forms ranges from 37-49% identity at the amino acid level. CPB1 is 42.8% identical to CPA1, 41.4% with CPA2, 48.8% with CPA3, 41.1% with CPA4, 36.9% with CPA5 and 40.8% with CPA6, by comparing the archetype sequences. The primary sequence identity between CPB1 and CPB2 is 40.1%. Carboxypeptidase B1 is considered a digestive proteinase, produced by the acinar cells of the pancreas. Carboxypeptidase B1 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. Carboxypeptidase B1is secreted in zymogen form as a free monomer, and trypsin activates carboxypeptidase B1 in the duodenum by removing the propeptide domain, cleaving at Arg110-Ala111, the same cleavage site and position as in CPA1. The cleaved propeptide domain is thought to have potent inhibitory activity, in the low nanomolar kI range. The catalytic domain chelates the zinc atom using residues His176, Glu179 and His304, with Glu378 acting as the active nucleophile. The zinc binding site has the GxHxREW motif conserved throughout the CPA and CPB groups. Two forms of CPB1 are reported, a 417 amino acid form and a 247 amino acid form that starts at the second methionine, just before the zinc binding site. The shorter sequence lacks the entire propeptide domain, but contains the entire catalytic domain. The substrate specificity of CPB1 is primarily arginine and lysine carboxyterminal residues, but there is limited activity against carboxyterminal asparagines, glutamine, and some activity against carboxyterminal valine, leucine, isoleucine and glycine. Carboxypeptidase B2, originally listed as the second pancreatic CPB, is thought to be principally a serum proteinase, and the literature is confused by the nomenclature. 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-B1 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-B1. The antibody is made to a synthetic peptide based on the amino end of the catalytic domain of human carboxypeptidase-B1. 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 B1 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 CPB1 and the other forms ranges from 37-49% identity at the amino acid level. CPB1 is 42.8% identical to CPA1, 41.4% with CPA2, 48.8% with CPA3, 41.1% with CPA4, 36.9% with CPA5 and 40.8% with CPA6, by comparing the archetype sequences. The primary sequence identity between CPB1 and CPB2 is 40.1%. Carboxypeptidase B1 is considered a digestive proteinase, produced by the acinar cells of the pancreas. Carboxypeptidase B1 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. Carboxypeptidase B1is secreted in zymogen form as a free monomer, and trypsin activates carboxypeptidase B1 in the duodenum by removing the propeptide domain, cleaving at Arg110-Ala111, the same cleavage site and position as in CPA1. The cleaved propeptide domain is thought to have potent inhibitory activity, in the low nanomolar kI range. The catalytic domain chelates the zinc atom using residues His176, Glu179 and His304, with Glu378 acting as the active nucleophile. The zinc binding site has the GxHxREW motif conserved throughout the CPA and CPB groups. Two forms of CPB1 are reported, a 417 amino acid form and a 247 amino acid form that starts at the second methionine, just before the zinc binding site. The shorter sequence lacks the entire propeptide domain, but contains the entire catalytic domain. The substrate specificity of CPB1 is primarily arginine and lysine carboxyterminal residues, but there is limited activity against carboxyterminal asparagines, glutamine, and some activity against carboxyterminal valine, leucine, isoleucine and glycine. Carboxypeptidase B2, originally listed as the second pancreatic CPB, is thought to be principally a serum proteinase, and the literature is confused by the nomenclature. 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-B1 is a rabbit polyclonal antibody made to the metalloprotease carboxypeptidase-B1. The antibody is made to a synthetic peptide based on the carboxy end of the catalytic domain of human carboxypeptidase-B1. 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 B1 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 CPB1 and the other forms ranges from 37-49% identity at the amino acid level. CPB1 is 42.8% identical to CPA1, 41.4% with CPA2, 48.8% with CPA3, 41.1% with CPA4, 36.9% with CPA5 and 40.8% with CPA6, by comparing the archetype sequences. The primary sequence identity between CPB1 and CPB2 is 40.1%. Carboxypeptidase B1 is considered a digestive proteinase, produced by the acinar cells of the pancreas. Carboxypeptidase B1 domain structure contains a signal sequence, a propeptide domain and a zinc metallopeptidase domain. Carboxypeptidase B1is secreted in zymogen form as a free monomer, and trypsin activates carboxypeptidase B1 in the duodenum by removing the propeptide domain, cleaving at Arg110-Ala111, the same cleavage site and position as in CPA1. The cleaved propeptide domain is thought to have potent inhibitory activity, in the low nanomolar kI range. The catalytic domain chelates the zinc atom using residues His176, Glu179 and His304, with Glu378 acting as the active nucleophile. The zinc binding site has the GxHxREW motif conserved throughout the CPA and CPB groups. Two forms of CPB1 are reported, a 417 amino acid form and a 247 amino acid form that starts at the second methionine, just before the zinc binding site. The shorter sequence lacks the entire propeptide domain, but contains the entire catalytic domain. The substrate specificity of CPB1 is primarily arginine and lysine carboxyterminal residues, but there is limited activity against carboxyterminal asparagines, glutamine, and some activity against carboxyterminal valine, leucine, isoleucine and glycine. Carboxypeptidase B2, originally listed as the second pancreatic CPB, is thought to be principally a serum proteinase, and the literature is confused by the nomenclature. 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.
