Recombinant Human ECE2 protein(Gly199-Trp883), hFc-tagged

• Cat.No.: ECE2-690H
• Product Overview: Recombinant Human endothelin converting enzyme 2 isoform A (NP_055508.3) (Gly 199-Trp 883) was expressed in HEK293, fused with the Fc region of Human IgG1 at the N-terminus.

Specification

• Species: Human
• Source: HEK293
• Tag: Fc
• Protein Length: 199-883 a.a.
• Form: Lyophilized from sterile 100mM Glycine, 10mM NaCl, 50mM Tris, pH 7.5. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
• Molecular Mass: The recombinant human Fc/ECE2 is a disulfide-linked homodimeric protein. The reduced monomer consists of 921 amino acids and predicts a molecular mass of 105 kDa. As a result of glycosylation, the apparent molecular mass of rh ECE2/Fc monomer is approximately 120-130 kDa in SDS-PAGE under reducing conditions.
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Purity: > 95 % as determined by SDS-PAGE
• Storage: Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents.

Gene Information

• Gene Name: ECE2 endothelin converting enzyme 2 [ Homo sapiens ]
• Official Symbol: ECE2
• Synonyms: ECE2; endothelin converting enzyme 2; endothelin-converting enzyme 2; KIAA0604; MGC2408; ECE-2; MGC17664; MGC78487
• Gene ID: 9718
• mRNA Refseq: NM_001037324
• Protein Refseq: NP_001032401
• MIM: 610145
• UniProt ID: O60344

Case Study

Case 1: Smith-Anttila CJA, et al. Autoimmunity. 2017

APS1-linked AIRE mutations reveal ECE-2 as a neuroendocrine-specific autoantigen, detected in 46% of patients’ sera but absent in other autoimmune disorders. Despite high pancreatic/pituitary expression, ECE-2 immunoreactivity lacks correlation with hypopituitarism, highlighting its role in APS1 autoimmunity.

Fig1. Tissue mRNA expression of ECE-2 by quantitative PCR.

Fig2. Characterization of the ECE-2 cell population in the pituitary gland from guinea pig.

Case 2: Liao X, et al. JCI Insight. 2020

Study identifies rare ECE2 gene mutations (R186C/F751S) in Alzheimer’s disease pathogenesis, linking impaired amyloid-beta degradation to increased AD risk. Research using AD model mice demonstrates wild-type ECE2 overexpression reduces Aβ plaques and cognitive deficits, while mutations abolish this neuroprotective effect. These findings position ECE2 as a key genetic risk factor in neurodegenerative disorders, suggesting pharmacological activation of Aβ-degrading enzymes could advance AD treatment strategies.

Fig1. Identification of purified proteins by Coomassie staining (upper) and Western blotting.

Fig2. 20E2 cells were transfected with vector, ECE2WT, ECE2R186C, or ECE2F751S plasmids, and cell lysates were blotted.

Application

1. Therapeutic Potential of Recombinant ECE2 Protein in Alzheimer’s Disease Recombinant endothelin-converting enzyme 2 (ECE2) protein has emerged as a promising therapeutic candidate for Alzheimer’s disease (AD) due to its ability to degrade amyloid-beta (Aβ) peptides, a hallmark of AD pathology. Studies demonstrate that ECE2 efficiently cleaves neurotoxic Aβ aggregates, reducing plaque accumulation and mitigating synaptic dysfunction. This enzyme replacement strategy targets impaired Aβ clearance mechanisms, addressing a critical gap in current AD therapeutic strategies. 2. Preclinical Evidence and Mechanisms In AD model mice, administration of recombinant ECE2 protein significantly decreased hippocampal Aβ plaque burden and improved cognitive deficits, mirroring effects observed with ECE2 gene overexpression. The protein’s peptidase activity directly disrupts Aβ aggregation pathways, enhancing neuronal survival and synaptic plasticity. These findings highlight its dual role in both Aβ degradation and neuroprotection, positioning it as a novel disease-modifying therapy for neurodegenerative disorders. 3. Challenges and Future Directions Despite its potential, challenges like limited blood-brain barrier (BBB) penetration and protein stability require optimization. Innovations in delivery systems—such as nanoparticle carriers or fusion proteins—may enhance recombinant ECE2’s bioavailability. Additionally, combining ECE2 activation with anti-inflammatory or tau-targeting agents could amplify therapeutic efficacy. As research advances, recombinant ECE2-based therapies may revolutionize AD treatment, offering hope for halting disease progression through targeted Aβ clearance and enzyme replacement approaches.

Fig1. Schematic diagram of ECE2/ET1 axis-induced NSCLC progression through YAP1/MAGEA3 signaling. (Huaiqing Xiao, 2025)