Description
RP1-ECE-2 is a rabbit polyclonal antibody made to the type-II membrane metalloproteinase ECE-2. The antibody is made to a synthetic peptide based on the cytoplasmic domain of human ECE-2. 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-2 was discovered as one of several enzymes that make the final processing cleavage of the endothelins (ET-1, ET-2, ET-3), and releases the active forms of these potent vasoconstrictors. The initial processing of the precursor is via the proprotein convertases, and ECE-2 cleaves the endothelins at Trp21-Val/Ile22. ECE-2 has a more acidic pH optimum (around 5.5 on ET-1) than ECE-1, and is considered a poor enzyme at neutral pH. The overall homology between ECE-1 and ECE-2 is approximately 59% at the amino acid level, and both enzymes share the same domain structure. ECE-2 is also more restricted in expression than the more ubiquitous ECE-1, with the highest concentrations found in neuronal tissues and the adrenal medulla, although the overall expression levels of ECE-2 are lower than ECE-1. Microarray analysis of Alzheimer's patients' tissues showed a marked decrease in ECE-2 message levels, and intracranial injections of ECE-1 have been shown to clear some of the amyloid beta protein in mouse models of Alzheimer's disease. ECE-2 is also thought to play a role in generating neuropeptides. ECE-2 is a type-II transmembrane metalloproteinase, with an aminoterminal cytoplasmic domain, a transmembrane domain, and a metalloproteinase domain of the M13 class. The cytoplasmic domain is longer in ECE-2 than in ECE-1, and is reported to have similarity to methyytransferases, although little is known about the function in ECE-2. A number of different splice variants of ECE-2 have been reported thus far, mostly containing modifications to the cytoplasmic domain, and the rest of the molecules are identical. Two splice variants of 255 amino acids length are reported that diverge and terminate after the transmembrane domain. Full-length variants of ECE-2 are reported of 883, 811, 787, 765, 737 and 736, amino acids in length, with predicted mass of 99.8, 91.2, 89.2, 86.5, 83.4 and 83.3 kDa, and pI of 4.77, 5.1, 4.9, 4.8, 4.9 and 4.9 respectively. Glycosylation and other posttranslational modifications make human ECE-2 run around 120-130 kDa on reduced Western blots. The RP1-ECE-2 antibody recognizes the 883, 787, and 255 amino acid forms of ECE-2. 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-2 is a rabbit polyclonal antibody made to the type-II membrane metalloproteinase ECE-2. The antibody is made to a synthetic peptide based on the stalk region between the TM domain and the catalytic domain of human ECE-2. 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-2 was discovered as one of several enzymes that make the final processing cleavage of the endothelins (ET-1, ET-2, ET-3), and releases the active forms of these potent vasoconstrictors. The initial processing of the precursor is via the proprotein convertases, and ECE-2 cleaves the endothelins at Trp21-Val/Ile22. ECE-2 has a more acidic pH optimum (around 5.5 on ET-1) than ECE-1, and is considered a poor enzyme at neutral pH. The overall homology between ECE-1 and ECE-2 is approximately 59% at the amino acid level, and both enzymes share the same domain structure. ECE-2 is also more restricted in expression than the more ubiquitous ECE-1, with the highest concentrations found in neuronal tissues and the adrenal medulla, although the overall expression levels of ECE-2 are lower than ECE-1. Microarray analysis of Alzheimer's patients' tissues showed a marked decrease in ECE-2 message levels, and intracranial injections of ECE-1 have been shown to clear some of the amyloid beta protein in mouse models of Alzheimer's disease. ECE-2 is also thought to play a role in generating neuropeptides. ECE-2 is a type-II transmembrane metalloproteinase, with an aminoterminal cytoplasmic domain, a transmembrane domain, and a metalloproteinase domain of the M13 class. The cytoplasmic domain is longer in ECE-2 than in ECE-1, and is reported to have similarity to methyytransferases, although little is known about the function in ECE-2. A number of different splice variants of ECE-2 have been reported thus far, mostly containing modifications to the cytoplasmic domain, and the rest of the molecules are identical. Two splice variants of 255 amino acids length are reported that diverge and terminate after the transmembrane domain. Full-length variants of ECE-2 are reported of 883, 811, 787, 765, 737 and 736, amino acids in length, with predicted mass of 99.8, 91.2, 89.2, 86.5, 83.4 and 83.3 kDa, and pI of 4.77, 5.1, 4.9, 4.8, 4.9 and 4.9 respectively. Glycosylation and other posttranslational modifications make human ECE-2 run around 120-130 kDa on reduced Western blots. The RP2-ECE-2 antibody recognizes all but the 255 amino acid form of ECE-2. 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-2 is a rabbit polyclonal antibody made to the type-II membrane metalloproteinase ECE-2. The antibody is made to a synthetic peptide based on the catalytic domain of human ECE-2. 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-2 was discovered as one of several enzymes that make the final processing cleavage of the endothelins (ET-1, ET-2, ET-3), and releases the active forms of these potent vasoconstrictors. The initial processing of the precursor is via the proprotein convertases, and ECE-2 cleaves the endothelins at Trp21-Val/Ile22. ECE-2 has a more acidic pH optimum (around 5.5 on ET-1) than ECE-1, and is considered a poor enzyme at neutral pH. The overall homology between ECE-1 and ECE-2 is approximately 59% at the amino acid level, and both enzymes share the same domain structure. ECE-2 is also more restricted in expression than the more ubiquitous ECE-1, with the highest concentrations found in neuronal tissues and the adrenal medulla, although the overall expression levels of ECE-2 are lower than ECE-1. Microarray analysis of Alzheimer's patients' tissues showed a marked decrease in ECE-2 message levels, and intracranial injections of ECE-1 have been shown to clear some of the amyloid beta protein in mouse models of Alzheimer's disease. ECE-2 is also thought to play a role in generating neuropeptides. ECE-2 is a type-II transmembrane metalloproteinase, with an aminoterminal cytoplasmic domain, a transmembrane domain, and a metalloproteinase domain of the M13 class. The cytoplasmic domain is longer in ECE-2 than in ECE-1, and is reported to have similarity to methyytransferases, although little is known about the function in ECE-2. A number of different splice variants of ECE-2 have been reported thus far, mostly containing modifications to the cytoplasmic domain, and the rest of the molecules are identical. Two splice variants of 255 amino acids length are reported that diverge and terminate after the transmembrane domain. Full-length variants of ECE-2 are reported of 883, 811, 787, 765, 737 and 736, amino acids in length, with predicted mass of 99.8, 91.2, 89.2, 86.5, 83.4 and 83.3 kDa, and pI of 4.77, 5.1, 4.9, 4.8, 4.9 and 4.9 respectively. Glycosylation and other posttranslational modifications make human ECE-2 run around 120-130 kDa on reduced Western blots. The RP3-ECE-2 antibody recognizes all but the 255 amino acid form of ECE-2. 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-2 is a rabbit polyclonal antibody made to the type-II membrane metalloproteinase ECE-2. The antibody is made to a synthetic peptide based on the carboxyterminal end of human ECE-2. 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-2 was discovered as one of several enzymes that make the final processing cleavage of the endothelins (ET-1, ET-2, ET-3), and releases the active forms of these potent vasoconstrictors. The initial processing of the precursor is via the proprotein convertases, and ECE-2 cleaves the endothelins at Trp21-Val/Ile22. ECE-2 has a more acidic pH optimum (around 5.5 on ET-1) than ECE-1, and is considered a poor enzyme at neutral pH. The overall homology between ECE-1 and ECE-2 is approximately 59% at the amino acid level, and both enzymes share the same domain structure. ECE-2 is also more restricted in expression than the more ubiquitous ECE-1, with the highest concentrations found in neuronal tissues and the adrenal medulla, although the overall expression levels of ECE-2 are lower than ECE-1. Microarray analysis of Alzheimer's patients' tissues showed a marked decrease in ECE-2 message levels, and intracranial injections of ECE-1 have been shown to clear some of the amyloid beta protein in mouse models of Alzheimer's disease. ECE-2 is also thought to play a role in generating neuropeptides. ECE-2 is a type-II transmembrane metalloproteinase, with an aminoterminal cytoplasmic domain, a transmembrane domain, and a metalloproteinase domain of the M13 class. The cytoplasmic domain is longer in ECE-2 than in ECE-1, and is reported to have similarity to methyytransferases, although little is known about the function in ECE-2. A number of different splice variants of ECE-2 have been reported thus far, mostly containing modifications to the cytoplasmic domain, and the rest of the molecules are identical. Two splice variants of 255 amino acids length are reported that diverge and terminate after the transmembrane domain. Full-length variants of ECE-2 are reported of 883, 811, 787, 765, 737 and 736, amino acids in length, with predicted mass of 99.8, 91.2, 89.2, 86.5, 83.4 and 83.3 kDa, and pI of 4.77, 5.1, 4.9, 4.8, 4.9 and 4.9 respectively. Glycosylation and other posttranslational modifications make human ECE-2 run around 120-130 kDa on reduced Western blots. The RP4-ECE-2 antibody recognizes all but the 255 amino acid form of ECE-2. 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.
