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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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ADAMTS13 Polyclonal Antibody recognizes ADAMTS13, a secreted zinc-dependent metalloprotease that regulates von Willebrand factor (VWF) multimer size and platelet adhesion. Also known as von Willebrand factor cleaving protease (VWFCP), ADAMTS13 belongs to the ADAMTS family of extracellular metalloproteinases. Its principal function is to cleave unusually large VWF multimers, limiting excessive platelet aggregation and preventing inappropriate microvascular thrombus formation. This enzymatic activity is essential for maintaining normal hemostasis and vascular homeostasis.
The human ADAMTS13 gene is located on chromosome 9q34 and encodes a protein of approximately 1427 amino acids. ADAMTS13 contains a metalloproteinase domain, disintegrin-like domain, thrombospondin type 1 repeats, cysteine-rich region, spacer domain, and two CUB domains. These structural elements contribute to enzymatic activity, substrate recognition, and interactions with VWF. The protein is extensively glycosylated, which influences its apparent molecular weight, secretion, and stability. ADAMTS13 is produced primarily in the liver and circulates in plasma as an active protease.
ADAMTS13 cleaves VWF at the Tyr1605-Met1606 bond within its A2 domain. Under elevated vascular shear stress, VWF undergoes conformational changes that expose this cleavage site, allowing ADAMTS13 to regulate multimer size. This process limits platelet adhesion to the vascular endothelium and helps maintain balanced clot formation. The von Willebrand Factor Cleaving Protease Antibody is relevant to research investigating these mechanisms of coagulation, endothelial function, and vascular regulation.
Severe ADAMTS13 deficiency is associated with thrombotic thrombocytopenic purpura (TTP), a disorder characterized by widespread microvascular platelet thrombi. Acquired TTP commonly results from inhibitory autoantibodies against ADAMTS13, while congenital TTP arises from pathogenic variants in the ADAMTS13 gene. Reduced protease activity permits accumulation of ultra-large VWF multimers, increasing platelet aggregation and microvascular obstruction. ADAMTS13 has also been investigated in ischemic stroke, systemic inflammation, and other disorders involving abnormal thrombosis.
Research into ADAMTS13 focuses on the balance between VWF processing, platelet function, and vascular integrity. Its activity influences thrombotic risk and contributes to the regulation of normal blood flow. NSJ Bioreagents offers antibodies targeting ADAMTS13 for research into hemostasis and cardiovascular biology. An ADAMTS13 Polyclonal Antibody provides a tool for examining VWF cleaving protease expression and its involvement in coagulation, thrombotic disorders, and vascular homeostasis.
For an alternative antibody targeting the same metalloprotease, see our ADAMTS13 Antibody.
Titration of the ADAMTS13 Polyclonal Antibody / von Willebrand Factor Cleaving Protease Antibody may be required due to differences in protocols and secondary/substrate sensitivity.
A portion of amino acids 829-858 from the human protein was used as the immunogen for this ADAMTS13 Polyclonal Antibody.
Aliquot the ADAMTS13 Polyclonal Antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
VWF Cleaving Protease antibody, VWFCP antibody, von Willebrand Factor Protease antibody, ADAMTS-13 antibody, ADAM-TS13 antibody, ADAMTS13 Metalloprotease antibody
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