Analytical Data
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Gene name
F8A1
- Application
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Alternative Names
F8A; F8A2; F8A3; HAP40; int22h; Factor VIII intron 22 Protein(intronic transcript); CpG Island Protein
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q00558
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Expression Region
His171~Pro375
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Molecular Weight
26kDa
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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
F8A1 recombinant protein research focuses on the development and application of a synthetic version of a key protein involved in blood coagulation, specifically Factor VIII. Factor VIII is essential for normal blood clotting, and its deficiency or dysfunction leads to hemophilia A, a hereditary bleeding disorder characterized by increased bleeding tendency. Traditional treatments for hemophilia A involved infusions of human-derived Factor VIII, which carried risks such as viral transmission and immune responses. The advent of recombinant DNA technology has allowed for the production of F8A1, a non-modified, highly purified version of Factor VIII, in various expression systems. This innovation aims to provide a safer, more effective treatment option with consistent quality and reduced risks. Researchers are investigating the structure, function, and stability of F8A1 recombinant protein, exploring its efficacy in therapies to restore normal clotting function in hemophilia A patients. Furthermore, studies focus on optimizing production processes and understanding the protein's interactions with other factors in the coagulation cascade, thus enhancing its therapeutic potential and paving the way for improved treatment strategies in hemophilia management.
