Analytical Data
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Gene name
FIGF
- Application
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Alternative Names
c-Fos-induced growth factor ;FIGF
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43915
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Expression Region
89-205aa
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Protein Length
Partial
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Molecular Weight
40.1 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
FIGF (Fibroblast Growth Factor Inducible Angiogenic Factor) is a member of the fibroblast growth factor (FGF) family, which plays a crucial role in angiogenesis, tissue repair, and various physiological processes. The study of FIGF is driven by its significant implications in both normal and pathological conditions, such as wound healing, cancer development, and cardiovascular diseases. The understanding of FIGF's mechanisms can provide insights into how angiogenesis is regulated, potentially leading to novel therapeutic strategies for conditions characterized by inadequate blood supply or excessive angiogenesis, like tumors. Recent research has focused on the recombinant expression of FIGF, enabling researchers to examine its biological activity, structural properties, and interactions with other angiogenic factors. This recombinant protein production is essential for various applications, including drug development and the establishment of in vitro models for studying vascular biology. As the demand for targeted therapies increases, the characterization of FIGF as a potential therapeutic target continues to gain attention, forging a pathway for innovative interventions in disease management through modulating angiogenic processes.
