Recombinant Mouse Neprilysin Protein, CF
Recombinant Mouse Neprilysin Protein, CF Summary
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Supplied as a 0.2 μm filtered solution in Tris and NaCl.|
|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.
- Assay Buffer: 0.1 M MES, pH 6.5
- Recombinant Mouse Neprilysin/CD10 (rmNeprilysin) (Catalog # 1126-ZN)
- Substrate: MCA-Arg-Pro-Pro-Gly-Phe-Ser-Ala-Phe-Lys(DNP)-OH (Catalog # ES005)
- F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
- Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
- Dilute rmNeprilysin to 0.2 µg/mL in Assay Buffer.
- Dilute Substrate to 20 µM in Assay Buffer.
- Load 50 µL of 0.2 µg/mL of rmNeprilysin in a plate, and start the reaction by adding 50 µL of 20 µM Substrate. As a Substrate Blank, load 50 µL of Assay Buffer and 50 µL of Substrate.
- Read at excitation and emission wavelengths of 320 nm and 405 nm (top read), respectively, in kinetic mode for 5 minutes.
- Calculate specific activity:
Specific Activity (pmol/min/µg) =
|Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)|
|amount of enzyme (µg)|
*Adjusted for Substrate Blank
**Derived using calibration standard MCA-Pro-Leu-OH (Bachem, Catalog # M-1975).Per Well:
- rmNeprilysin: 0.010 µg
- Substrate: 10 µM
Neprilysin (NEP, neutral endopeptidase 24.11, EC 18.104.22.168) is a zinc metallopeptidase expressed at the cell surface of a variety of cells. The enzyme functions both as an endopeptidase with a thermolysin-like specificity and as a dipeptidylcarboxypeptidase. NEP has been shown to be involved in the degradation of enkephalins in the mammalian brain and the inactivation of circulating atrial natriuretic peptide (1, 2). NEP has also been identified as the common acute lymphoblastic leukemia antigen (CALLA), and to be expressed on the surface of lymphocytes in some disease states (3). These and other observations have resulted in considerable clinical interest in NEP as a potential target for analgesics and antihypertensive drugs. NEP is also a major degrading enzyme of amyloid beta peptide (A beta ) in the brain, indicating that down-regulation of NEP activity, which could be caused by aging, can contribute to the development of Alzheimer’s disease by promoting A beta accumulation (4).
- Malfroy, B. et al. (1978) Nature 276:523.
- Kenny, A.J. and S.L. Stephenson (1988) FEBS Lett. 232:1.
- LeTarte, M. et al. (1988) J. Exp. Med. 168:1247.
- Itwata, N. et al. (2001) Science 292:1550.
Citation for Recombinant Mouse Neprilysin Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Successive action of meprin A and neprilysin catabolizes B-type natriuretic peptide.
Authors: Pankow K, Wang Y, Gembardt F, Krause E, Sun X, Krause G, Schultheiss HP, Siems WE, Walther T
Circ. Res., 2007;101(9):875-82.
Sample Types: Peptide
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