>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<1.0 EU per 1 μg of the protein by the LAL method.
69 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 Component 1: Phenylalanine (Sigma, Catalog # P2126), 100 mM stock in diH2O
Substrate Component 2: Amplex Ultra Red (AUR) (Molecular Probes, Catalog # A36006), 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 rmIL-4I1 to 2 ng/µL in Assay Buffer.
Prepare the Substrate mixture including 2 mM Phenylalanine, 2 units/mL HRP and 100 µM AUR in Assay Buffer.
Load in a black well plate 50 µL of 2 ng/µL of rmIL-4I1, and start the reaction by adding 50 µL of the Substrate mixture (step 2). Include a Substrate Blank containing 50 µL of the Assay Buffer and 50 µL of the Substrate mixture.
Read at excitation and emission wavelengths of 544 nm and 590 nm (top read), respectively in kinetic mode for 5 minutes. Note: A wavelength cutoff of 570 nm should be manually specified.
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 a fluorescent standard prepared by incubating 50 µM AUR, 1 unit/mL HRP, 1 mM Phenylalanine, and a range of Hydrogen Peroxide (0-500 pmol) (Sigma, Catalog # H1009) in Assay Buffer at room temperature. Use the resulting amounts of oxidized AUR to determine the conversion factor.
rmIL-4I1: 0.1 µg
Phenylalanine: 1 mM
HRP: 1 unit/mL
AUR: 50 µM
Caution: The rmIL-4I1 enzymatic reaction may significantly be interfered with organic buffer such as MES.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse IL-4I1 Protein, CF
IL4-induced protein 1
interleukin 4 induced 1
interleukin four induced 1
Interleukin four-induced gene 1 (IL-4I1) was first identified in mouse B cells as part of the response to IL-4, a key regulator of the immune response (1). Later, the enzyme was shown to be a member of the flavin-containing amino acid oxidase family and closely related to L-amino acid oxidases (2, 3). Enzymological characterization reveals that IL-4I1 has L-amino acid oxidase activity with preference toward aromatic amino acids (4). Its limited expression in immune tissues, dendritic cells, and macrophages indicates that it may play an important function in the immune system (5, 6).
Chu, C.C. and W.E. Paul (1997) Proc. Natl. Acad. Sci. USA 94:2507.
Raibekas, A.A. and V. Massey (1998) Biochem. Biophys. Res. Comm. 248:476.
Chavan, S.S. et al. (2002) Biochim. Biophys. Acta 1576:70.
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PRODUCT AVAILABILITY: Update Regarding the Evolving COVID-19 Situation
Bio-Techne appreciates the critical role that you and our products and services play in research efforts to further scientific innovation and discovery. We are continually assessing our manufacturing and supplier capabilities during the COVID-19 situation and are implementing precautionary measures to ensure uninterrupted supply of products and services. Currently, and as we abide by local shelter in place orders across the world, we are fully operational and do not anticipate any material supply disruptions across our Bio-Techne brands and product lines. As the situation evolves, our goal is to utilize preventive measures to reduce the threat that COVID-19 poses to our ability to meet the needs of our customers globally.