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Human ECE-2 Protein (His Tag)

ECE2, hCG_2022032, KIAA0604, MGC17664, MGC2408, MGC78487

Catalog Number P10207-H07H
Organism Species Human
Host Human Cells
Synonyms ECE2, hCG_2022032, KIAA0604, MGC17664, MGC2408, MGC78487
Molecular Weight The recombinant human ECE2 consists of 700 amino acids with the predicted molecular mass of 80.2 kDa. As a result of glycosylation, rhECE2 migrates as an approximately 120-125 kDa band in SDS-PAGE under reducing conditions.
predicted N His
SDS-PAGE
Purity > 93 % as determined by SDS-PAGE
Protein Construction A DNA sequence encoding the ectodomain of human endothelin converting enzyme 2 isoform A (NP_055508.3) (Gly 199-Trp 883) was fused with a polyhistidine tag at the N-terminus.
Bio-activity
Research Area Cancer |Oncoprotein & suppressor & biomarker |Oncoprotein |Growth Factor & Receptor |Hormones
Formulation Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
Background Endothelin-converting enzyme 2, also known as ECE-2, is a metalloprotease that possesses many properties consistent with it being a neuropeptide-processing enzyme. Endothelin-converting enzymes (ECEs) are the key enzymes in the endothelin (ET) biosynthesis that catalyze the conversion of big ET, the biologically inactive precursor of mature ET. Two enzymes, termed ECE-1 and ECE-2, have been molecularly identified. ECE-2 is found primarily in neural tissues, with high levels of expression in midbrain, cerebellum, hypothalamus, frontal cortex and spinal cord and moderate levels in hippocampus and striatum. ECE-2 is strongly down-regulated in inferior parietal lobe from Alzheimer disease patients (at protein level). ECE-2 converts big endothelin-1 to endothelin-1. It is involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides. ECE-2 may limit beta-amyloid peptide accumulation in brain. It may also have methyltransferase activity. A comparison of residues around the cleavage site revealed that ECE-2 exhibits a unique cleavage site selectivity that is related to but distinct from that of ECE-1.
Reference