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Creative Biolabs

NoGeneST™ Anti-VWF Aptamer, aVWF aptamer-1 sodium

[CAT#: NRYF-0625-HZ10]

A pegylated RNA aptamer that acts as a potent and specific inhibitor of von Willebrand Factor (VWF), designed to modulate hemostasis and treat thrombotic disorders.

Target:
VWF
Type:
RNA

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Product Overview

Description

Egaptivon pegol sodium is a cutting-edge therapeutic agent composed of a synthetic single-stranded RNA aptamer covalently linked to a polyethylene glycol (PEG) polymer. This pegylation process is designed to enhance the molecule's stability and extend its circulatory half-life. The aptamer's specific three-dimensional structure allows it to bind with high affinity to the A1 domain of von Willebrand Factor (VWF). This targeted interaction sterically hinders the binding of VWF to its primary platelet receptor, GPIb, thereby blocking the initial step of platelet adhesion and aggregation at sites of vascular injury. As a targeted modulator of the VWF axis, this compound is being investigated for use as an anticoagulant and antiplatelet agent in various hematologic and cardiovascular disorders.

Type

RNA
Properties

Size

1 mg; 5 mg; 10 mg

Appearance

Supplied as a lyophilized white to off-white solid.

Purity

>90%

Shipping

Room temperature

Storage

Powder Form: Stable for 3 years when stored at -20°C.
In Solvent: Stable for 6 months when aliquoted and stored at -80°C

Research Use Only

For Research Use Only
Target Details

Target

VWF

Full Name

Von Willebrand Factor

Alternative Names

Factor VIII related antigen

Gene ID

7450

Uniprot ID

P04275

Target Overview

Von Willebrand Factor (VWF) is a large, multimeric glycoprotein that plays a central and critical role in hemostasis (the cessation of bleeding). It performs two primary functions in the bloodstream: first, it acts as a molecular bridge, mediating the adhesion of platelets to exposed subendothelial collagen at sites of vascular injury, a crucial initial step in forming a platelet plug. Second, it serves as a carrier protein for Coagulation Factor VIII, binding to it and protecting it from premature degradation in the circulation. The size and adhesive activity of VWF multimers are tightly regulated, and dysregulation of VWF function can lead to either bleeding disorders (like von Willebrand disease) or pathological thrombosis.
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