Analytical Data
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Gene name
FBP
- Application
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Alternative Names
FBP；C1orf39；TOCA1；Formin-binding Protein 1-like
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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
P09467
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Expression Region
2-338aa
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AA Sequence
ADQAPFDTDVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHSAQ
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Molecular Weight
56.7 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
FBP (Fructose-1,6-bisphosphatase) is a key regulatory enzyme in the gluconeogenesis pathway, which plays a crucial role in glucose metabolism. Its primary function is to catalyze the conversion of fructose-1,6-bisphosphate to fructose-6-phosphate, thereby facilitating the synthesis of glucose from non-carbohydrate sources, particularly during fasting or low-carbohydrate intake. Imbalances in FBP activity can lead to metabolic disorders, such as diabetes and obesity, making it a target for therapeutic intervention. The study of FBP has gained traction in recent years due to the increasing prevalence of metabolic diseases globally. Research has focused on understanding the enzyme's structure, function, and regulation, as well as its interactions with other metabolic pathways. Advancements in recombinant protein technology enable the production of FBP in heterologous systems, allowing for detailed studies of its enzymatic properties and potential inhibitors. This research is crucial for developing strategies that could improve metabolic health and provide insights into how altered FBP activity contributes to disease states. As a result, FBP not only serves as an essential component in metabolic regulation but also represents a promising area of research for therapeutic development aimed at treating metabolic disorders.
