Analytical Data
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Gene name
FGA
- Application
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Alternative Names
/
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Species
Human
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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
Q8WW76
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Expression Region
36-218aa
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Molecular Weight
25.1 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
FGA, or fibrinogen alpha chain, is a key component of the fibrinogen protein complex, which plays a crucial role in blood coagulation and wound healing. Research into FGA recombinant proteins has gained significant attention due to their potential applications in medicine, particularly in tissue engineering and the development of hemostatic agents. The recombinant expression of FGA allows for the production of high-purity proteins that can be used to study the structure-function relationships of fibrinogen, its interactions with platelets, and the mechanisms underlying clot formation. Additionally, understanding FGA's role in various pathophysiological conditions, such as thrombosis and cardiovascular diseases, is vital for developing targeted therapies. Advances in genetic engineering and protein production techniques have facilitated the efficient synthesis of FGA, making it feasible to explore its therapeutic potential in treating bleeding disorders and improving surgical outcomes. Overall, the study of FGA recombinant proteins represents a promising area of research that bridges basic science and clinical applications, highlighting the importance of fibrinogen in both hemostasis and pathological states.
