Analytical Data
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Gene name
FGB
- Application
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Alternative Names
FGB;Fibrinogen beta chain
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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
P02675
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Expression Region
45-491aa
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AA Sequence
GHRPLDKKREEAPSLRPAPPPISGGGYRARPAKAAATQKKVERKAPDAGGCLHADPDLGVLCPTGCQLQEALLQQERPIRNSVDELNNNVEAVSQTSSSSFQYMYLLKDLWQKRQKQVKDNENVVNEYSSELEKHQLYIDETVNSNIPTNLRVLRSILENLRSKIQKLESDVSAQMEYCRTPCTVSCNIPVVSGKECEEIIRKGGETSEMYLIQPDSSVKPYRVYCDMNTENGGWTVIQNRQDGSVDFGRKWDPYKQGFGNVATNTDGKNYCGLPGEYWLGNDKISQLTRMGPTELLIEMEDWKGDKVKAHYGGFTVQNEANKYQISVNKYRGTAGNALMDGASQLMGENRTMTIHNGMFFSTYDRDNDGWLTSDPRKQCSKEDGGGWWYNRCHAANPNGRYYWGGQYTWDMAKHGTDDGVVWMNWKGSWYSMRKMSMKIRPFFPQQ
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Molecular Weight
54.8kDa
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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
FGB, or fibrinogen beta chain, is a crucial protein involved in the blood coagulation process, playing a significant role in wound healing and hemostasis. The study of FGB and its recombinant forms has gained attention due to their potential applications in both therapeutic and diagnostic fields. Abnormalities in fibrinogen levels are associated with various diseases, including cardiovascular disorders, where either elevated or reduced levels can lead to thrombosis or bleeding complications, respectively. The production of recombinant FGB proteins allows for a deeper understanding of its structure-function relationships and facilitates the development of novel therapeutic agents aimed at modulating coagulation. Furthermore, recombinant FGB can serve as a useful tool in platelet aggregation studies, offering insights into platelet function and interactions. The advancement of biotechnological techniques has enabled the efficient expression and purification of FGB, paving the way for extensive studies that could unravel its role in various pathophysiological conditions. As research progresses, the potential for FGB-based therapeutics continues to expand, particularly in the context of personalized medicine and targeted therapies aimed at regenerative medicine and the management of clotting disorders.
