Analytical Data
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Gene name
FGF23
- Application
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Alternative Names
FGF23；HYPF；Fibroblast growth factor 23
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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
Q9GZV9
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Expression Region
25-251aa
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AA Sequence
YPNASPLLGSSWGGLIHLYTATARNSYHLQIHKNGHVDGAPHQTIYSALM IRSEDAGFVVITGVMSRRYLCMDFRGNIFGSHYFDPENCRFQHQTLENGY DVYHSPQYHFLVSLGRAKRAFLPGMNPPPYSQFLSRRNEIPLIHFNTPIP RRHTRSAEDDSERDPLNVLKPRARMTPAPASCSQELPSAEDNSPMASDPL GVVRGGRVNTHAGGTGPEGCRPFAKFI
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Molecular Weight
25 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
Fibroblast growth factor 23 (FGF23) is a key regulatory protein involved in phosphate metabolism and vitamin D homeostasis. It is primarily produced by osteocytes and osteoblasts in response to increased phosphate levels and is crucial for maintaining phosphate balance by promoting renal excretion of phosphate and inhibiting the synthesis of 1,25-dihydroxyvitamin D. Abnormal levels of FGF23 are associated with various metabolic disorders, including chronic kidney disease, where it contributes to dysregulated phosphate and calcium homeostasis. Researchers have focused on recombinant FGF23 for its potential therapeutic applications, particularly in conditions characterized by elevated phosphate levels, such as X-linked hypophosphatemia and tumor-induced osteomalacia. The production and characterization of recombinant FGF23 enables a deeper understanding of its biological functions and interactions within signaling pathways, facilitating the development of FGF23-based therapies. Moreover, studying FGF23 in a recombinant form provides insights into its structure-function relationships and may pave the way for novel treatments targeting phosphate-related disorders. Overall, the investigation of recombinant FGF23 holds promise in advancing our understanding of mineral metabolism and devising innovative therapeutic strategies for diseases associated with phosphate imbalance.
