assay
≥95% (HPLC)
form
lyophilized
specific activity
≥850 units/mg protein
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
solubility
physiological buffer, pH 7.4: 1 mg/mL (e.g., Tris-buffered saline)
shipped in
ambient
storage temp.
−20°C
Disclaimer
Toxicity: Standard Handling (A)
General description
Native, neutral endopeptidase from porcine kidney. A cell surface zinc-containing proteinase that is abundant in the brush border membranes of the kidney proximal tubules. Also present in the brain, endothelial cells, liver, and the lung tissue. Peptidase activity is specifically directed towards the cleavage on the amino side of hydrophobic amino acid residues. Contains an arginine in the active site that can interact with the C-terminal carboxylate of substrates.
Native, neutral endopeptidase from porcine kidney. A cell surface, zinc containing metallopeptidase that is abundant in the brush border membrane of the kidney proximal tubules. Also present in brain, endothelial cells, liver, and lung. Peptidase activity is specifically directed toward the cleavage on the amino side of hydrophobic residues. Contains an arginine in the active site that can interact with the C-terminal carboxylate of substrates.
Other Notes
Barnes, K., et al. 1995. J. Neurochem. 64, 1826.
Gafford, J.T., et al. 1983. Biochemistry 22, 3265.
Gafford, J.T., et al. 1983. Biochemistry 22, 3265.
One unit of enzyme will liberate 1.0 µmol pNA per min from Glutaryl-(Ala)₂-Phe-pNA at 25°C, pH 7.4.
Physical form
Lyophilized from 150 mM NaCl, 25 mM Tris-HCl, 5 mM CaCl₂, TRITON™ X-100 Detergent, pH 7.4.
Preparation Note
Following reconstitution, refrigerate (4°C). Stock solutions are stable for up to 3 days at 4°C.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Triton is a trademark of The Dow Chemical Company or an affiliated company of Dow
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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