Analytical Data
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Gene name
F8
- Application
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Alternative Names
F8；SIAT8F；Alpha-2.8-sialyltransferase 8F
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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
P61647
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Expression Region
1-398aa
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AA Sequence
MRPGGALLALLASLLLLLLLRLLWCPADAPGRARILVEESREATHGTPAALRTLRSPATAVPRATNSTYLNEKSLQLTEKCKNLQYGIESFSNKTKGYSENDYLQIITDIQSCPWKRQAEEYANFRAKLASCCDAVQNFVVSQNNTPVGTNMSYEVESKKEIPIKKNIFHMFPVSQPFVDYPYNQCAVVGNGGILNKSLCGTEIDKSDFVFRCNLPPTTGDVSKDVGSKTNLVTINPSIITLKYGNLKEKKALFLEDIATYGDAFFLLPAFSFRANTGTSFKVYYTLEESKARQKVLFFHPKYLKDLALFWRTKGVTAYRLSTGLMITSVAVELCKNVKLYGFWPFSKTVEDIPVSHHYYDNKLPKHGFHQMPKEYSQILQLHMKGILKLQFSKCEVA
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Molecular Weight
44.8 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
F8 recombinant protein, also known as recombinant Factor VIII, plays a crucial role in the treatment of hemophilia A, a genetic disorder characterized by the deficiency of clotting factor VIII, leading to excessive bleeding. Traditional treatments for hemophilia involved administering plasma-derived Factor VIII, which posed risks such as viral transmission and fluctuating factor levels. In the 1980s, advancements in biotechnology led to the development of recombinant Factor VIII, produced through genetic engineering techniques, allowing for a safer and more consistent supply. Research has focused on improving the stability, efficacy, and safety of F8 recombinant proteins, leading to the creation of various formulations with longer half-lives and reduced immunogenicity. These innovations have significantly enhanced the quality of life for hemophilia patients, reducing the frequency of infusions and complications associated with antibodies formed against Factor VIII. Ongoing studies aim to explore novel delivery methods, combination therapies, and gene therapy approaches to provide more effective and durable treatment solutions for individuals affected by hemophilia A.
