Description
RP1-ECE-1 is a rabbit polyclonal antibody made to the type-II membrane metalloproteinase ECE-1. The antibody is made to a synthetic peptide based on the cytoplasmic domain of human ECE-1. 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
ECE-1 was discovered as one of several enzymes that make the final processing cleavage of the endothelins (ET-1, ET-2, ET-3), and release the active forms of these potent vasoconstrictors. The initial processing of the precursor is via the proprotein convertases, and ECE-1 cleaves the endothelins at Trp21-Val/Ile22. ECE-1 also functions like ACE and Neprilysin as a carboxypeptidase, cleaving neurotensin, substance P and bradykinin, but does not appear to work as well on shorter sequences, and the carboxypeptidase activity is thought to be significantly weaker than the cleavage of the endothelins. The cleavage of substance P is thought to re-sensitize the substance P neurokinin-1 receptor, resulting in the pro-inflammatory effects of substance P. The specific activity of ECE-1 is thought to be more pH dependant than the cousin enzymes ACE and Neprilysin, and different splice variants of ECE-1 have been postulated to have different specificities and localization. The endothelins are also important in directing neural crest cell migration in development, and mutations in ECE-1 are part of a group of mutations affecting the endothelin system thought to yield familial Hirschprung disease. A mutation in ECE-1 (C338A) has been implicated in a number of disorders, such as Alzheimer's disease and gastric cancer, and is thought to increase susceptibility to carotoid atherosclerosis. Activation of the endothelin system is implicated in retinal ischemia, as well as in prostate cancer. ECE-1 is a type-II transmembrane metalloproteinase, with an aminoterminal cytoplasmic domain, a transmembrane domain, and a metalloproteinase domain of the M13 class. The different splice variants of ECE-1 reported thus far contain modifications to the cytoplasmic domain, and the rest of the molecules are identical. The full-length human ECE-1 is 770 amino acids in length, with predicted mass of 87.2 kDa, and pI of 5.2. Glycosylation and other posttranslational modifications make human ECE-1 run around 120-130 kDa on reduced Western blots. 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-ECE-1 is a rabbit polyclonal antibody made to the type-II membrane metalloproteinase ECE-1. The antibody is made to a synthetic peptide based on the stem region just extracellular from the transmembrane domain of human ECE-1. 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
ECE-1 was discovered as one of several enzymes that make the final processing cleavage of the endothelins (ET-1, ET-2, ET-3), and release the active forms of these potent vasoconstrictors. The initial processing of the precursor is via the proprotein convertases, and ECE-1 cleaves the endothelins at Trp21-Val/Ile22. ECE-1 also functions like ACE and Neprilysin as a carboxypeptidase, cleaving neurotensin, substance P and bradykinin, but does not appear to work as well on shorter sequences, and the carboxypeptidase activity is thought to be significantly weaker than the cleavage of the endothelins. The cleavage of substance P is thought to re-sensitize the substance P neurokinin-1 receptor, resulting in the pro-inflammatory effects of substance P. The specific activity of ECE-1 is thought to be more pH dependant than the cousin enzymes ACE and Neprilysin, and different splice variants of ECE-1 have been postulated to have different specificities and localization. The endothelins are also important in directing neural crest cell migration in development, and mutations in ECE-1 are part of a group of mutations affecting the endothelin system thought to yield familial Hirschprung disease. A mutation in ECE-1 (C338A) has been implicated in a number of disorders, such as Alzheimer's disease and gastric cancer, and is thought to increase susceptibility to carotoid atherosclerosis. Activation of the endothelin system is implicated in retinal ischemia, as well as in prostate cancer. ECE-1 is a type-II transmembrane metalloproteinase, with an aminoterminal cytoplasmic domain, a transmembrane domain, and a metalloproteinase domain of the M13 class. The different splice variants of ECE-1 reported thus far contain modifications to the cytoplasmic domain, and the rest of the molecules are identical. The full-length human ECE-1 is 770 amino acids in length, with predicted mass of 87.2 kDa, and pI of 5.2. Glycosylation and other posttranslational modifications make human ECE-1 run around 120-130 kDa on reduced Western blots. 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-ECE-1 is a rabbit polyclonal antibody made to the type-II membrane metalloproteinase ECE-1. The antibody is made to a synthetic peptide based on the catalytic domain of human ECE-1. 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
ECE-1 was discovered as one of several enzymes that make the final processing cleavage of the endothelins (ET-1, ET-2, ET-3), and release the active forms of these potent vasoconstrictors. The initial processing of the precursor is via the proprotein convertases, and ECE-1 cleaves the endothelins at Trp21-Val/Ile22. ECE-1 also functions like ACE and Neprilysin as a carboxypeptidase, cleaving neurotensin, substance P and bradykinin, but does not appear to work as well on shorter sequences, and the carboxypeptidase activity is thought to be significantly weaker than the cleavage of the endothelins. The cleavage of substance P is thought to re-sensitize the substance P neurokinin-1 receptor, resulting in the pro-inflammatory effects of substance P. The specific activity of ECE-1 is thought to be more pH dependant than the cousin enzymes ACE and Neprilysin, and different splice variants of ECE-1 have been postulated to have different specificities and localization. The endothelins are also important in directing neural crest cell migration in development, and mutations in ECE-1 are part of a group of mutations affecting the endothelin system thought to yield familial Hirschprung disease. A mutation in ECE-1 (C338A) has been implicated in a number of disorders, such as Alzheimer's disease and gastric cancer, and is thought to increase susceptibility to carotoid atherosclerosis. Activation of the endothelin system is implicated in retinal ischemia, as well as in prostate cancer. ECE-1 is a type-II transmembrane metalloproteinase, with an aminoterminal cytoplasmic domain, a transmembrane domain, and a metalloproteinase domain of the M13 class. The different splice variants of ECE-1 reported thus far contain modifications to the cytoplasmic domain, and the rest of the molecules are identical. The full-length human ECE-1 is 770 amino acids in length, with predicted mass of 87.2 kDa, and pI of 5.2. Glycosylation and other posttranslational modifications make human ECE-1 run around 120-130 kDa on reduced Western blots. 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-ECE-1 is a rabbit polyclonal antibody made to the type-II membrane metalloproteinase ECE-1. The antibody is made to a synthetic peptide based on the carboxyterminal end of human ECE-1. 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
ECE-1 was discovered as one of several enzymes that make the final processing cleavage of the endothelins (ET-1, ET-2, ET-3), and release the active forms of these potent vasoconstrictors. The initial processing of the precursor is via the proprotein convertases, and ECE-1 cleaves the endothelins at Trp21-Val/Ile22. ECE-1 also functions like ACE and Neprilysin as a carboxypeptidase, cleaving neurotensin, substance P and bradykinin, but does not appear to work as well on shorter sequences, and the carboxypeptidase activity is thought to be significantly weaker than the cleavage of the endothelins. The cleavage of substance P is thought to re-sensitize the substance P neurokinin-1 receptor, resulting in the pro-inflammatory effects of substance P. The specific activity of ECE-1 is thought to be more pH dependant than the cousin enzymes ACE and Neprilysin, and different splice variants of ECE-1 have been postulated to have different specificities and localization. The endothelins are also important in directing neural crest cell migration in development, and mutations in ECE-1 are part of a group of mutations affecting the endothelin system thought to yield familial Hirschprung disease. A mutation in ECE-1 (C338A) has been implicated in a number of disorders, such as Alzheimer's disease and gastric cancer, and is thought to increase susceptibility to carotoid atherosclerosis. Activation of the endothelin system is implicated in retinal ischemia, as well as in prostate cancer. ECE-1 is a type-II transmembrane metalloproteinase, with an aminoterminal cytoplasmic domain, a transmembrane domain, and a metalloproteinase domain of the M13 class. The different splice variants of ECE-1 reported thus far contain modifications to the cytoplasmic domain, and the rest of the molecules are identical. The full-length human ECE-1 is 770 amino acids in length, with predicted mass of 87.2 kDa, and pI of 5.2. Glycosylation and other posttranslational modifications make human ECE-1 run around 120-130 kDa on reduced Western blots. 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.
