Analytical Data
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Gene name
FIGF
- Application
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Alternative Names
FIGF；FIGF；Vascular endothelial growth factor D
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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
O43915
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Expression Region
93-201aa
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AA Sequence
FYDIETLKVI DEEWQRTQCS PRETCVEVAS ELGKSTNTFF KPPCVNVFRC GGCCNEESLI CMNTSTSYIS KQLFEISVPL TSVPELVPVK VANHTGCKCL PTAPRHPYS
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Molecular Weight
14 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 (FMS-like tyrosine kinase 4-induced gene) is an important protein implicated in various physiological processes, particularly in angiogenesis and lymphangiogenesis. Identified primarily for its roles in the development of blood and lymphatic vessels, FIGF acts as a ligand for receptor kinases such as VEGFR-3 and VEGFR-2, activating downstream signaling pathways that promote endothelial cell proliferation and migration. Research into the recombinant expression of FIGF has gained traction due to its potential therapeutic applications in treating diseases characterized by pathological angiogenesis, such as cancer and age-related macular degeneration. Additionally, understanding the precise molecular mechanisms of FIGF can provide insights into cardiovascular and lymphatic system disorders. The generation of FIGF recombinant proteins allows for the exploration of its biological functions and interactions, which are crucial for advancing knowledge in vascular biology and developing novel therapeutic strategies. Enhanced production techniques, such as the use of engineered expression systems, have enabled researchers to obtain higher yields of active FIGF, facilitating detailed functional assays and structural studies. This growing body of work aims to leverage FIGF's biological properties for innovative therapeutic applications, aiming to harness its angiogenic potential while minimizing adverse effects. Thus, ongoing research into FIGF recombinant proteins is vital for uncovering new avenues for drug development and understanding the intricate networks regulating vascular health.
