>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.
33 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.
Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
Activate rhCathepsin X/Z/P.
Dilute rhCathepsin X/Z/P to 20 µg/mL in Activation Buffer.
Dilute DTT stock to 10 mM in Activation Buffer.
Mix equal volumes of 20 µg/mL rhCathepsin X/Z/P and 10 mM DTT.
Incubate at room temperature for 5 minutes.
Dilute activated rhCathepsin X/Z/P to 0.4 ng/µL in Assay Buffer.
Dilute Substrate to 20 µM in Assay Buffer.
Load 50 µL of the 0.4 ng/µL rhCathepsin X/Z/P in a black well plate, and start the reaction by adding 50 µL of 20 µM Substrate. Include a Substrate Blank containing 50 µL of Assay Buffer and 50 µL of 20 µM Substrate without any rhCathepsin X/Z/P.
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).
rhCathepsin X/Z/P: 0.02 µg
Substrate: 10 µM
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human Cathepsin X/Z/P Protein, CF
Cathepsin X (also known as Cathepsin Z and P) is a cysteine protease of the papain family (1-5). Compared to other members of the papain family, Cathepsin X has a short proregion and unique insertions. The cysteine residue in the proregion forms a covalent and reversible bond with the active site cysteine residue (6). Acting as a carboxypeptidase, Cathepsin X displays a unique specificity (7-10). It is ubiquitously expressed in human tissues and conserved in other species such as mouse, nematode and echiuran. The nematode enzyme is apparently involved in molting of third stage larvae (11).
Nagler, D.K. and R. Menard (1998) FEBS Lett. 434:135.
Santamaria, I. et al. (1998) J. Biol. Chem. 273:16816.
Deussing, J. et al. (2000) Biochim. Biophys. Acta 1491:93.
Pungercar, J. and G. Ivanovski (2000) Pflugers Arch. Eur. J. Physiol. 439:R116.
Pungercar, J. et al. (2000) Pflugers Arch. Eur. J. Physiol. 439:R119.
Sivaraman, J. et al. (2000) J. Mol. Biol. 295:935.
Menard, R. et al. (2001) Biol. Chem. 382:839.
Therrien, C. et al. (2001) Biochemistry 40:2702.
Klemencic, I. et al. (2000) Eur. J. Biochem. 267:5404.
Guncar, G. et al. (2000) Structure Fold Des. 8:305.
Lustigman, S. et al. (1996) J. Biol. Chem. 271:30181.
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