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Conditions of optimal THOP1 Enzyme performance should be determined experimentally by the investigator.
Price/availability/specifications subject to change without notice. Unless otherwise indicated, our catalog and customized products are for research use only and not intended for human or animal diagnostic or therapeutic use.
Phone: 1-617-401-8149
Fax: 1-617-606-5019
Email: message@sydlabs.com
Or leave a message with a formal purchase
order (PO) Or credit card.
Introduction
Thimet oligopeptidase (THOP1), also known as Endopeptidase 24.15 and MP78, belongs to the peptidase M3 family which includes neurolysin and mitochondrial intermediate peptidase. THOP1 is located in Cytoplasm. THOP1 is widely expressed in human tissues and can detected in different subcellular locations. THOP1 is preferential cleavage for bonds with hydrophobic residues at P1, P2 and P3' and a small residue at P1' in substrates of 5 to 15 residues. THOP1 is involved in the metabolism of neuropeptides under 20 amino acid residues and degradation of cytoplasmic peptide. In addition, THOP1 also can degrade the beta-amyloid precursor protein and generate amyloidogenic fragments.
BP001069-C179: Recombinant Human Thimet oligopeptidase (THOP1) Enzyme
Source: E. coli-derived.
Recombinant Human Thimet oligopeptidase (THOP1) Enzyme is expressed with sequence (Lys2-Cys689) of Human THOP1.
Purity: > 95% by SEC-HPLC and reducing SDS-PAGE.
Endotoxin: < 0.1 ng/ug (1 IEU/ug).
Formulation: 0.2 um filtered solution of 20 mM PB, 100 mM NaCl, 10% Glycerol, pH 7.0.
Shipping: The product is shipped with ice pack. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70°C as supplied.
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