>90%, 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.
73 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
1. Dilute rhADAMTS13 to 5 µg/mL in Assay Buffer. 2. Dilute Substrate to 8 µM in Assay Buffer. 3. Load 50 µL of dilute rhADAMTS13 into a plate, and start the reactions by adding 50 µL of 8 µM Substrate. Include a Substrate Blank containing 50 µL of Assay Buffer and 50 µL of 8 µM Substrate. 4. Read at excitation and emission wavelengths of 340 nm and 450 nm (top read), respectively, in kinetic mode for 5 minutes. 5. 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 FRETS-25-STD1 (Peptides International, Catalog # STD-3720-V).
rhADAMTS13: 0.25 µg
Substrate: 4 µM
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human ADAMTS13 Protein, CF
A disintegrin and metalloproteinase with thrombospondin motifs 13
a disintegrin-like and metalloprotease (reprolysin type) with thrombospondintype 1 motif, 13
ADAM metallopeptidase with thrombospondin type 1 motif, 13
VWFCPvon Willebrand factor-cleaving protease
ADAMTS13 (a disintegrin and metalloproteinase with thrombospondin motifs 13), also known as von Willebran Factor (vWF) cleaving protease, is a member of the family of secreted zinc proteases with a multi-domain structure (1‑3). The protein precursors consist of a signal peptide and following domains: pro, catalytic, disintegrin-like, TS type 1 motif, cysteine-rich, spacer, a second set of seven TSP1 repeats, and two CUB domins. The only known substrate of ADAMTS13 is vWF, a blood glycoprotein with two homeostatic functions (4). It is required for platelet adhesion to sites of vascular damage and acts as a carrier protein for blood-clotting factor VIII in the circulation. It exists in plasma as multimers, the largest of which effectively mediate platelet adhesion. ADAMTS13 cleaves multimeric vWF in the A2 domain at the position, Tyr1605‑Met1606. A defect in ADAMTS13 activity is a cause of congenital thrombotic thrombocytopenic purpura (TTP), also known as Upshaw‑Schulman syndrome. Lack of ADAMTS13 activity allows unusually large vWF (UlvWF) to occur in plasma (5). These UlvWF multimers have tendency to agglutinate circulating platelets at sites with high levels of shear stress to cause TTP. The purified rhADAMTS13 starts at the N‑terminus of the pro domain and ends in the spacer domain. If desired, the rhvWF‑A2 cleaving activity of rhADAMTS13 can be inhibited by 5 mM 1,10-phenanthroline.
Furlan, M. et al. (1996) Blood. 87:4223.
Porter, S. et al. (2005) Biochem. J. 386:15.
Chung, D. W. and J.E. Saddler (2004) in Handbook of Proteolytic Enzymes, Barret, A. J. et al. eds. pp. 747-751.
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