Recombinant Human ADAMTS13 (Full Length) Protein, CF

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

ADAMTS13 (a disintegrin and metalloproteinase with thrombospondin motifs 13), also known as von Willebrand Factor (vWF) cleaving protease, is a member of the family of secreted zinc proteases with a multidomain structure (1-3). The protein precursors consist of a signal peptide and following domains: pro, catalytic, disintegrin-like, thromobspondin type 1 (TSP1) motif, a cysteine-rich domain, a spacer region, 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 between Tyr1605 and 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 high concentrations vWF (UlvWF) to accumulate in plasma (5). These UlvWF multimers have a tendency to agglutinate circulating platelets at sites with high levels of shear stress to cause TTP. The recombinant human vWFA2 cleaving activity of recombinant human ADAMTS13 can be inhibited by 5 mM 1,10‑phenanthroline.

We have publications tested in 2 confirmed species: Human, Mouse.

We have publications tested in 5 applications: Bioassay, ELISA Capture, ELISA Standard, In Vivo, Surface Plasmon Resonance.

Showing Publications 1 - 7 of 7.

Publications using 6156-AD	Applications	Species
Madarati, H;DeYoung, V;Singh, K;Sparring, T;Kwong, AC;Fredenburgh, JC;Teney, C;Koschinsky, ML;Boffa, MB;Weitz, JI;Kretz, CA; Optimization of plasma-based BioID identifies plasminogen as a ligand of ADAMTS13 Scientific reports 2024-04-20 [PMID: 38643218] (Bioassay, Human)	Bioassay	Human
L Kong, Y Zhang, J Ning, C Xu, Z Wang, J Yang, L Yang CaMKII orchestrates endoplasmic reticulum stress and apoptosis in doxorubicin-induced cardiotoxicity by regulating the IRE1alpha/XBP1s pathway Journal of Cellular and Molecular Medicine, 2022-09-16;0(0):. 2022-09-16 [PMID: 36111515] (Bioassay, Mouse)	Bioassay	Mouse
Y Bi, J Su, S Zhou, Y Zhao, Y Zhang, H Zhang, M Liu, A Zhou, J Xu, M Pan, Y Zhao, F Li Distinct impact of IgG subclass on autoantibody pathogenicity in different IgG4-mediated diseases Elife, 2022-08-03;11(0):. 2022-08-03 [PMID: 35920621] (ELISA Standard, Mouse)	ELISA Standard	Mouse
T Ito, T Minamitani, M Hayakawa, R Otsubo, H Akiba, K Tsumoto, M Matsumoto, T Yasui Optimization of anti-ADAMTS13 antibodies for the treatment of ADAMTS13-related bleeding disorder in patients receiving circulatory assist device support Scientific Reports, 2021-11-16;11(1):22341. 2021-11-16 [PMID: 34785706] (ELISA Capture, Surface Plasmon Resonance, Human)	ELISA Capture, Surface Plasmon Resonance	Human
CA Kretz, K Tomberg, A Van Esbroe, A Yee, D Ginsburg High throughput protease profiling comprehensively defines active site specificity for thrombin and ADAMTS13 Sci Rep, 2018-02-12;8(1):2788. 2018-02-12 [PMID: 29434246] (Bioassay)	Bioassay
Lee , Manfai, Keener , Justin, Xiao , Juan, Long Zheng , X, Rodgers , George M ADAMTS13 and its variants promote angiogenesis via upregulation of VEGF and VEGFR2. Cell Mol Life Sci, 2014-06-21;72(2):349-56. 2014-06-21 [PMID: 24950743] (Bioassay, Human)	Bioassay	Human
Muroi C, Fujioka M, Mishima K, Irie K, Fujimura Y, Nakano T, Fandino J, Keller E, Iwasaki K, Fujiwara M Effect of ADAMTS-13 on cerebrovascular microthrombosis and neuronal injury after experimental subarachnoid hemorrhage. J Thromb Haemost, 2014-04-01;12(4):505-14. 2014-04-01 [PMID: 24476338] (In Vivo, Mouse)	In Vivo	Mouse

Array 6156-AD

• ADAMTS13 Antibodies
• ADAMTS13 ELISA Kit
• ADAMTS13 Lysate
• ADAMTS13 Proteins
• ADAMTS13 ELISAs
• ADAMTS13 Proteins and Enzymes