Synonyms	ECE2;hCG_2022032;KIAA0604;MGC17664;MGC2408;MGC78487
Species	Human
Expression_host	HEK293 Cells
Sequence	Gly 199-Trp 883
Accession	NP_055508.3
Mol_Mass	80.2 kDa
AP_Mol_Mass	120-125 kDa
Tag	N-His

Properties

Purity	> 93 % as determined by reducing SDS-PAGE.
Endotoxin level	< 1.0 EU per μg of the protein as determined by the LAL method.
Storage	Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
Shipping	This product is provided as lyophilized powder which is shipped with ice packs.
Formulation	Lyophilized from sterile PBS, pH 7.4 Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the printed manual.
Reconstitution	Please refer to the printed manual for detailed information.

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.

Citations

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