Analytical Data
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Gene name
Von Willebrand Factor/vWF
- Application
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Alternative Names
von Willebrand antigen II
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Species
Mouse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8CIZ8
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Expression Region
1498-1665aa
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Molecular Weight
23.9 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Von Willebrand Factor (vWF) is a critical multimeric glycoprotein involved in hemostasis, serving as a bridge between platelets and the endothelial collagen during vascular injury. Deficiencies or dysfunctions in vWF lead to von Willebrand disease (vWD), a common hereditary bleeding disorder that affects platelet adhesion and blood clotting. The complexity of vWF structure, which exists in various multimeric forms, is crucial for its biological function and regulation. Researchers have focused on recombinant vWF proteins to better understand the pathophysiology of vWD and to develop therapeutic strategies. Advances in recombinant DNA technology have facilitated the production of these proteins, allowing for the exploration of their physiological properties, including their interaction with platelets and the extracellular matrix. Furthermore, therapeutic applications of recombinant vWF aim to provide effective treatments for patients with vWD, improving their quality of life and reducing bleeding complications. Ongoing studies are investigating the efficacy, dosage, and safety of these recombinant proteins, with the goal of creating more refined and patient-specific treatment options. The research on recombinant vWF not only enhances our understanding of hemostatic mechanisms but also holds promise for innovative therapies in bleeding disorders.
