>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<1.0 EU per 1 μg of the protein by the LAL method.
104 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Substrate: H-Ala-AMC (Bachem, Catalog # I-1410), 10 mM stock in DMSO
F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
Dilute rmCD13 to 1 µg/mL in Assay Buffer.
Incubate at 37 °C for one hour (fully activates enzyme).
Dilute rmCD13 to 0.2 ng/µL in Assay Buffer.
Dilute Substrate to 200 µM in Assay Buffer.
Load 50 µL of 0.2 ng/µL rmCD13 in a plate, and start the reaction by adding 50 µL of 200 µM Substrate. Include a Substrate Blank containing 50 µL of Assay Buffer and 50 µL of 200 µM Substrate.
Read at excitation and emission wavelengths of 380 nm and 460 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 7-Amino-4-Methyl-Courmarin (AMC) (Sigma, Catalog # A-9891).
rmCD13 0.010 µg
Substrate: 100 µM
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse Aminopeptidase N/CD13 Protein, CF
alanyl (membrane) aminopeptidase
Myeloid plasma membrane glycoprotein CD13
The mouse ANPEP gene encodes Aminopeptidase N (APN), which is also known as microsomal aminopeptiase, alanyl aminopeptidase, Aminopeptidase M, CD13, or membrane protein p161 (1-3). The deduced amino acid sequence of mouse APN consists of a short cytoplasmic tail (residues 2 to 8), a transmembrane region (residue 9 to 32), a Ser/Thr rich region and a zinc metalloprotease domain (residues 69 to 966). Widely expressed in many cells, tissues and species, APN cleaves the N-terminal amino acids from bioactive peptides, leading to their inactivation or degradation. The roles of APN in many fields, such as neuroscience, hematopoeitic cells, immune system, angiogenesis, cancer and viral infection, have been reviewed (4).
Chen, H. et al. (1996) J. Immunol. 157:2593.
Larsen, S.L. et al. (1996) J. Exp. Med. 184:183.
Hansen, A.S. et al. (1993) Eur. J. Immunol. 23:2358.
Turner, A.J. (2004) in Handbook of Proteolytic Enzymes (ed. Barrett, et al.) p. 289 Academic Press, San Diego.
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