Description
RP1-CPVL is a rabbit polyclonal antibody made to the serine proteinase CPVL. The antibody is made to a synthetic peptide based on the propeptide domain of human CPVL. 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
CPVL, also known as Carboxypeptidase, Vitellogenic-Like, HVLP, Vitellogenic Carboxypeptidase-Like Protein, VCP-Like Protein and BM031, is a serine proteinase first identified in insects as a vitellogen cleaving proteinase. Vitellogenin is a glycolipoprotein that is a yolk protein in fish, amphibians and insects, used as a food reservoir. In humans CPVL was discovered in bone marrow, and given the name BM031, with unknown function. Also cloned by differential display from human macrophages, CPVL was named after the vitellogenic carboxypeptidase found in mosquito ovaries, based on the 43% identity at the amino acid level. CPVL orthologues are found in many insects and vertebrates, and is reasonably well conserved structurally. In humans CPVL message was found in the spleen, leukocytes, placenta, heart and kidney. CPVL is induced in monocytes as they are converted to macrophages, and is postulated to be involved in antigen processing. To date substrates are unknown for CPVL, nor are the roles in heart, kidney and other tissues. Structural homology to the other human serine carboxypeptidases Serine Carboxypeptidase-1, Retinoid-Inducible Serine Carboxypeptidase and Cathepsin A is low. The domain structure of CPVL indicates a signal sequence, followed by a propeptide domain and a serine protease domain. Several different splice variants are published, which encode proteins of 476, 385, 298, 233 and 105 amino acids in length, with predicted mass of 54.2, 43.5, 34.5, 26.9 and 11.6 kDa and pI of 5.3, 5.8, 5.5, 4.4 and 9.7 respectively. The 2 shortest sequences lack one or more of the catalytic residues, but the other forms are thought to have a competent catalytic triad. Relative abundance and distribution for the splice variants is unknown at this time. CPVL is thought to be glycosylated, increasing the apparent mass by several kDa on SDS PAGE gels. The catalytic triad of HDS found in trypsin and chymotrypsin-like serine proteinases is reversed in CPVL, with Ser204-Asp388-His448 thought to be the active residues. 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 approximately 12 months at -20C.
Description
RP2-CPVL is a rabbit polyclonal antibody made to the serine proteinase CPVL. The antibody is made to a synthetic peptide based on the catalytic domain of human CPVL. 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
CPVL, also known as Carboxypeptidase, Vitellogenic-Like, HVLP, Vitellogenic Carboxypeptidase-Like Protein, VCP-Like Protein and BM031, is a serine proteinase first identified in insects as a vitellogen cleaving proteinase. Vitellogenin is a glycolipoprotein that is a yolk protein in fish, amphibians and insects, used as a food reservoir. In humans CPVL was discovered in bone marrow, and given the name BM031, with unknown function. Also cloned by differential display from human macrophages, CPVL was named after the vitellogenic carboxypeptidase found in mosquito ovaries, based on the 43% identity at the amino acid level. CPVL orthologues are found in many insects and vertebrates, and is reasonably well conserved structurally. In humans CPVL message was found in the spleen, leukocytes, placenta, heart and kidney. CPVL is induced in monocytes as they are converted to macrophages, and is postulated to be involved in antigen processing. To date substrates are unknown for CPVL, nor are the roles in heart, kidney and other tissues. Structural homology to the other human serine carboxypeptidases Serine Carboxypeptidase-1, Retinoid-Inducible Serine Carboxypeptidase and Cathepsin A is low. The domain structure of CPVL indicates a signal sequence, followed by a propeptide domain and a serine protease domain. Several different splice variants are published, which encode proteins of 476, 385, 298, 233 and 105 amino acids in length, with predicted mass of 54.2, 43.5, 34.5, 26.9 and 11.6 kDa and pI of 5.3, 5.8, 5.5, 4.4 and 9.7 respectively. The 2 shortest sequences lack one or more of the catalytic residues, but the other forms are thought to have a competent catalytic triad. Relative abundance and distribution for the splice variants is unknown at this time. CPVL is thought to be glycosylated, increasing the apparent mass by several kDa on SDS PAGE gels. The catalytic triad of HDS found in trypsin and chymotrypsin-like serine proteinases is reversed in CPVL, with Ser204-Asp388-His448 thought to be the active residues. 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 approximately 12 months at -20C.
Description
RP3-CPVL is a rabbit polyclonal antibody made to the serine proteinase CPVL. The antibody is made to a synthetic peptide based on the carboxyterminal end of full length human CPVL. 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
CPVL, also known as Carboxypeptidase, Vitellogenic-Like, HVLP, Vitellogenic Carboxypeptidase-Like Protein, VCP-Like Protein and BM031, is a serine proteinase first identified in insects as a vitellogen cleaving proteinase. Vitellogenin is a glycolipoprotein that is a yolk protein in fish, amphibians and insects, used as a food reservoir. In humans CPVL was discovered in bone marrow, and given the name BM031, with unknown function. Also cloned by differential display from human macrophages, CPVL was named after the vitellogenic carboxypeptidase found in mosquito ovaries, based on the 43% identity at the amino acid level. CPVL orthologues are found in many insects and vertebrates, and is reasonably well conserved structurally. In humans CPVL message was found in the spleen, leukocytes, placenta, heart and kidney. CPVL is induced in monocytes as they are converted to macrophages, and is postulated to be involved in antigen processing. To date substrates are unknown for CPVL, nor are the roles in heart, kidney and other tissues. Structural homology to the other human serine carboxypeptidases Serine Carboxypeptidase-1, Retinoid-Inducible Serine Carboxypeptidase and Cathepsin A is low. The domain structure of CPVL indicates a signal sequence, followed by a propeptide domain and a serine protease domain. Several different splice variants are published, which encode proteins of 476, 385, 298, 233 and 105 amino acids in length, with predicted mass of 54.2, 43.5, 34.5, 26.9 and 11.6 kDa and pI of 5.3, 5.8, 5.5, 4.4 and 9.7 respectively. The 2 shortest sequences lack one or more of the catalytic residues, but the other forms are thought to have a competent catalytic triad. Relative abundance and distribution for the splice variants is unknown at this time. CPVL is thought to be glycosylated, increasing the apparent mass by several kDa on SDS PAGE gels. The catalytic triad of HDS found in trypsin and chymotrypsin-like serine proteinases is reversed in CPVL, with Ser204-Asp388-His448 thought to be the active residues. 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 approximately 12 months at -20C.
