Description
Key facts
Detection method:Colorimetric,
Sample types:Cell culture supernatant, Citrate plasma, EDTA Plasma, Heparin Plasma, Serum,
Reacts with:Human,
Assay type:Sandwich (quantitative),
Sensitivity:< 20 pg/mL,
Range:0.78 - 50 ng/mL,
Assay time:3h 30m,
Assay Platform:Pre-coated microplate (12 x 8 well strips)
Product details:
Human ADAMTS13 ELISA kit (ab213752) is designed for the quantitative measurement of Human ADAMTS13 in cell culture supernatants, serum and plasma (heparin, EDTA, citrate).
The ELISA kit is based on standard sandwich enzyme-linked immunosorbent assay technology. A monoclonal antibody from mouse specific for ADAMTS13 has been pre-coated onto 96-well plates. Standards (CHO, Q34-W688) and test samples are added to the wells, a biotinylated detection polyclonal antibody from goat specific for ADAMTS13 is added subsequently and then followed by washing with PBS or TBS buffer. Avidin-Biotin-Peroxidase Complex is added and unbound conjugates are washed away with PBS or TBS buffer. HRP substrate TMB is used to visualize HRP enzymatic reaction. TMB is catalyzed by HRP to produce a blue color product that changed into yellow after adding acidic stop solution. The density of yellow is proportional to the Human ADAMTS13 amount of sample captured in plate.
ADAMTS13 is a zinc-containing metalloprotease enzyme. The ADAMTS13 gene is mapped to chromosome 9q34 by genomic sequence analysis. It is reported that a metal-containing proteolytic enzyme (metalloprotease) in normal plasma cleaves the peptide bond between tyrosine at position 842 and methionine at position 843 in monomeric subunits of von Willebrand factor, thereby degrading the large multimers. It is confirmed that the ADAMTS13 gene encodes the von Willebrand factor-cleaving protease (VWFCP). ADAMTS13 is secreted in blood and degrades large vWf multimers, decreasing their activity.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information--20°C
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
ADAMTS13 also known as von Willebrand factor-cleaving protease (VWFCP) is a zinc-containing metalloprotease with a molecular mass of approximately 190 kDa. This protein belongs to the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) family and exhibits a complex structure with specific domains including a metalloprotease and a disintegrin-like domain. ADAMTS13 is produced mainly in the liver and circulates in the blood plasma. Research shows that it primarily facilitates the cleavage of von Willebrand factor (vWF) a large multimeric protein essential for blood clotting.
Biological function summary
ADAMTS13 plays a role in regulating the size and function of von Willebrand factor (vWF) ensuring proper hemostatic balance. The enzyme prevents the accumulation of ultra-large vWF multimers which can lead to spontaneous platelet aggregation and thrombus formation. Although ADAMTS13 acts independently its function is closely linked to the dynamics of vWF in response to vascular injury. Properly functioning ADAMTS13 aids in maintaining normal blood flow by preventing unnecessary clot formation in the bloodstream.
Pathways
ADAMTS13 is critical in the coagulation and hemostatic pathways. It operates by modulating the activity of vWF which plays an essential role in platelet adhesion and aggregation forming part of the coagulation cascade. A significant relationship exists between ADAMTS13 and vWF in these pathways as the protease controls vWF multimer size directly impacting clot formation. In the context of hemostatic balance ADAMTS13 intersects with factors like thrombin and fibrinogen which further contribute to clotting processes.
ADAMTS13 deficiency or dysfunction is associated with thrombotic thrombocytopenic purpura (TTP) a rare but severe blood disorder. In TTP the reduced activity of ADAMTS13 leads to an over-accumulation of ultra-large vWF multimers resulting in excessive platelet aggregation and microvascular thrombosis. Another related condition is atypical hemolytic uremic syndrome (aHUS) where abnormal ADAMTS13 activity might exacerbate the disease pathology. Both disorders highlight the critical need for balanced ADAMTS13 function in maintaining vascular health and highlight its potential as a therapeutic target.
