Recombinant Human Neurolysin Protein, CF
R&D Systems, part of Bio-Techne | Catalog # 3814-ZN
Key Product Details
Product Specifications
Source
E. coli-derived human Neurolysin protein
Ser38-Pro704, with an N-terminal Met and 6-His tag
Ser38-Pro704, with an N-terminal Met and 6-His tag
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
N-terminal Sequence Analysis
Met
Predicted Molecular Mass
77 kDa
SDS-PAGE
73 kDa, reducing conditions
Activity
Measured by its ability to cleave a fluorogenic peptide substrate, (7-methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Pro-D-Lys(2,4-dinitrophenyl)-OH or Mca-PLGPK(Dnp)-OH.
The specific activity is >70 pmol/min/µg, as measured under the described conditions.
The specific activity is >70 pmol/min/µg, as measured under the described conditions.
Formulation, Preparation and Storage
3814-ZN
| Formulation | Supplied as a 0.2 μm filtered solution in Tris, NaCl and Glycerol. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
|
Background: Neurolysin
Neurolysin, also known as Oligopeptidase M (mitochondrial peptidase), soluble angiotensin II-binding protein and endopeptidase EC 3.4.24.16 (1, 2), is a homologue of Thimet Ologopeptidase (THOP1), a zinc peptidase of the M3 family that also includes mitochondrial intermediate peptidase. Neurolysin expresses in two forms with the difference of an N-terminal transit peptide that targets the localization to mitochondria (1). The shorter form exists in cytosol. The recombinant human Neurolysin is expressed without the transit peptide and is isolated from the cytosol. Like THOP1, Neurolysin is capable of cleaving a number of vasoactive peptides such as bradykinin and neurotensin (3). All known substrates of THOP1 and Neurolysin contain 17 or fewer amino acids.
References
- Serizawa, A. et al. (1995) J. Biol. Chem. 270:2092.
- Barett, A.J. and J.M. Chen (2004) in Handbook of Proteolytic Enzymes (ed. Barrett, A.J. et al.) pp. 356, Elsevier Academic Press, San Diego.
- Norman, M.U. et al. (2003) Am. J. Physiol. Heart Circ. Physiol. 284:H1978.
Alternate Names
AGTBP, Neurotensin Endopeptidase, NLN, Oligopeptidase M
Gene Symbol
NLN
UniProt
Additional Neurolysin Products
Product Documents for Recombinant Human Neurolysin Protein, CF
Product Specific Notices for Recombinant Human Neurolysin Protein, CF
For research use only
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