Analytical Data
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Gene name
vWFCP
- Application
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Alternative Names
vWFCP；
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q76LX8
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Expression Region
1328-1427aa
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AA Sequence
FINVAPHARIAIHALATNMGAGTEGANASYILIRDTHSLRTTAFHGQQVL YWESESSQAEMEFSEGFLKAQASLRGQYWTLQSWVPEMQDPQSWKGKEGT
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Molecular Weight
37 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-C (vWFCP) is a critical component of the von Willebrand factor (vWF) protein, which plays a vital role in hemostasis, the process of blood clotting. It is known for mediating platelet adhesion to damaged vascular surfaces, thereby facilitating the creation of a stable clot. Abnormalities or deficiencies in vWF can lead to bleeding disorders, such as von Willebrand disease, which affects millions globally. The exploration of recombinant vWFCP has garnered attention due to its potential therapeutic applications, particularly for patients with bleeding disorders. Traditional treatment options, such as plasma-derived concentrates, may pose risks of infection and variability in efficacy. Consequently, the development of recombinant forms of vWFCP aims to provide a safer, more consistent, and effective treatment modality. Recent advances in genetic engineering and biotechnology have enabled the production of recombinant vWFCP, allowing for better characterization and understanding of its structure-function relationship. This research is crucial for optimizing the therapeutic properties of vWFCP, improving patient outcomes, and offering novel strategies for managing bleeding disorders. Researchers are actively investigating the stability, functionality, and bioactivity of recombinant vWFCP, paving the way for potential innovations in hemophilia and related conditions. The ongoing studies highlight the importance of vWFCP in both basic science and clinical applications, marking a significant advancement in our understanding of coagulation biology and therapeutic development.
