Measured by its ability to inhibit active Cathepsin V cleavage of a fluorogenic peptide substrate Z-LR-AMC (Catalog # ES008). The IC50 value is <400 nM, as measured under the described conditions.
Source
Mouse myeloma cell line, NS0-derived human Lipocalin-1 protein His19-Asp176, with a C-terminal 10-His tag
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Theoretical MW
19 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.
SDS-PAGE
20-22 kDa, reducing conditions
Publications
Read Publication using 1708-PI in the following applications:
Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
Prepare a curve of rhLipocalin-1 (MW: 18,805 Da) in Assay Buffer. Make the following serial dilutions: 40,000, 10,000, 4000, 1000, 500, 250, 125, 50, 12.5, and 6.25 nM.
Dilute rhCathepsin V to 2 µg/mL in Cathepsin Buffer.
Mix equal volumes of the rhLipocalin-1 curve dilutions and the 2 µg/mL rhCathepsin V. Include a Cathepsin Control (in duplicate) containing Assay Buffer in place of rhLipocalin-1.
Incubate mixtures at room temperature for 30 minutes.
Dilute Substrate to 40 µM in Substrate Buffer.
Load into a black well plate 50 µL of the incubated mixtures, and start the reaction by adding 50 µL of 40 µM Substrate.
Read at excitation and emission wavelengths of 380 nm and 460 nm (top read), respectively, in kinetic mode for 5 minutes.
Derive the 50 % inhibiting concentration (IC50) of rhLipocalin-1 by plotting RFU/min (or specific activity) vs. concentration with 4‑PL fitting.
The specific activity for rhCathepsin V at each point may be determined using the following formula (if needed):
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 Coumarin (Sigma, Catalog # A-9891).
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Lipocalin-1 Protein, CF
LCN1
lipocalin 1 (tear prealbumin)
lipocalin 1-like 2
Lipocalin1
Lipocalin-1
MGC71975
PMFA
Tear lipocalin
Tear Prealbumin
TLC
TPVon Ebner gland protein
VEG protein
VEGP
VEGPlipocalin 1 (protein migrating faster than albumin, tear prealbumin)
Background
Lipocalin-1, also known as tear prealbumin or von Ebner’s gland protein (VEGP), is encoded by the LCN1 gene (1-3). It is a member of the Lipocalin superfamily that binds many different classes of lipophylic chemicals (4). Lipocalin-1 contains three sequence motifs similar to the cystatins, a superfamily of cysteine protease inhibitors (5). In fact, it has been suggested that Lipocalin-1 is a physiological inhibitor of cysteine proteases and plays a role in the control of inflammatory processes in oral and ocular tissues (5). Recombinant Human Lipocalin-1 corresponds to the mature and secreted protein. It is a weak inhibitor of cysteine proteases such as cathepsin V, which is similar to recombinant human Cystatin S (Catalog # 1296-PI).
Redl, B. et al. (1992) J. Biol. Chem. 267:20282.
Blaker, M. et al. (1993) Biochim. Biophys. Acta 1172:131.
Lassagne, H. and A.M. Gachon (1993) Exp. Eye Res. 56:605.
Redl, B. et al. (2000) Biochim. Biophys. Acta 1482:241.
van’t Hof, W. et al. (1997) J. Biol. Chem. 272:1837.
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