Recombinant Rat Fibroblast Growth Factor 23 (FGF23) Protein (His)

Name: Recombinant Rat Fibroblast Growth Factor 23 (FGF23) Protein (His)
Brand: Beta LifeScience
SKU: BLC-04551P
Price: 549.6 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Cytokines, Cytokines and growth factors, Enzymes, Featured enzyme molecules, Growth factors and receptors, Kinase, Recombinant proteins

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Product Overview

Description	Recombinant Rat Fibroblast Growth Factor 23 (FGF23) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q8VI82
Target Symbol	FGF23
Synonyms	Fgf23Fibroblast growth factor 23; FGF-23
Species	Rattus norvegicus (Rat)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	YSDTSPLLGSNWGSLTHLYTATARNSYHLQIHRDGHVDGTPHQTIYSALMITSEDAGSVVIIGAMTRRFLCMDLRGNIFGSYHFSPENCRFRQWTLENGYDVYLSPKHHYLVSLGRSKRIFQPGTNPPPFSQFLARRNEVPLLHFYTARPRRHTRSAEDPPERDPLNVLKPRPRATPIPVSCSRELPSAEEGGPAASDPLGVLRRGRGDARRGAGGTDRCRPFPRFV
Expression Range	25-251aa
Protein Length	Full Length of Mature Protein
Mol. Weight	29.5kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Regulator of phosphate homeostasis. Inhibits renal tubular phosphate transport by reducing SLC34A1 levels. Regulator of vitamin-D metabolism. Negatively regulates osteoblasts differentiation and matrix mineralization. Acts directly on the parathyroid to decrease PTH secretion. Upregulates EGR1 expression in the presence of KL.
Subcellular Location	Secreted.
Protein Families	Heparin-binding growth factors family
Database References	KEGG: rno:170583 STRING: 10116.ENSRNOP00000026888 UniGene: Rn.154421
Tissue Specificity	Expressed in the parathyroid.

Gene Functions References

Increases in plasma erythropoietin and erythropoietin receptor activation are mechanisms implicated in the increase of plasma FGF23 in acute kidney injury. PMID: 29395333
In chronic kidney disease (CKD) rat models, FGF23 mRNA is expressed in the kidney, and the FGF23 protein is expressed at high levels in osteopontin-positive renal tubule epithelium cells likely via TGFbeta1 stimulation. FGF23 produced in the kidney might contribute to P metabolism in subjects with CKD. PMID: 29518087
High FGF23 expression is associated with cardiac hypertrophy. PMID: 28339837
The only direct contribution of the injured kidney to circulating FGF23 levels in uremia appears to be reduced renal extraction of bone-derived FGF23. PMID: 28341272
Osteoblast Fgf23 transcription is upregulated by increase in the cytosolic Ca(2+) activity. Fgf23 transcription is decreased by Orai inhibitors and Orai1 silencing. Fgf23 transcription is lowered by NFkappaB inhibitors. PMID: 26631141
EPO dependent regulation pathway of FGF23 gene expression PMID: 29073196
can directly stimulate hepatic secretion of inflammatory cytokines PMID: 27457912
dietary Mg deficiency causes a rapid increase in circulating levels of FGF23 and renal 24(OH)ase mRNA levels PMID: 27624533
phosphate directly enhances Fgf23 transcription without affecting the stability of Fgf23 messenger RNA. PMID: 25792238
Fgf23 gene transcription was abolished by the actin microfilament-disrupting agent cytochalasin B, as well as by the inhibition of actin-regulating Rac1/PAK1 signaling. PMID: 26878191
Although the molecular link between the cardiac lesion and circulating Fgf23 concentrations remains to be identified, our study has uncovered a novel heart-bone-kidney axis PMID: 25858796
In conclusion, PRL was responsible for the lactation-induced mucosal adaptations, which were associated with compensatory increase in FGF-23 expression probably to prevent calcium hyperabsorption. PMID: 26657069
Data indicate that serum fibroblast growth factor 23 (FGF-23) levels independently correlated with bone volume parameters in rats with experimentally induced chronic kidney disease (CKD). PMID: 26186634
fibroblast growth factor 23 is increased by intravenous phosphate loading in uremic rats PMID: 24625659
The polycystic kidney produces FGF23 but is resistant to its action. PMID: 24402093
FGF23 enhances phosphate-induced vascular calcification by promoting osteoblastic differentiation involving the ERK1/2 pathway in the absence of Klotho deficiency. PMID: 24088960
Ca is not a regulator of acute changes in FGF23 secretion. PMID: 24801007
data suggest that inhibition of FGFR signaling following administration of either pan-FGFR inhibitor or MEK inhibitor interferes with the FGF23 pathway, predisposing animals to hyperphosphatemia PMID: 23872713
In non-iron depleted normal and uremic rats a single high dose of either of two intravenous iron preparations, iron isomaltoside 1000, and ferric carboxymaltose, had no effect on plasma levels of iFGF23 and phosphate for up to seven days. PMID: 24373521
Mg deficiency increases serum FGF-23 levels. PMID: 23608165
a direct and an indirect effect of parathyroid hormone on FGF23 secretion, the latter through changes in calcitriol concentrations PMID: 21525854
late-onset ADHR is the product of gene-environment interactions whereby the combined presence of an Fgf23-stabilizing mutation and iron deficiency can lead to ADHR PMID: 22006328
FGF23 normalizes serum phosphate and decreases 1,25-dihydroxyvitamin D levels in early-stage chronic kidney disease. PMID: 20844473
Serum FGF23 increased in uremic rats treated with paricalcitol but not those treated with cinacalcet. PMID: 20200094
because of a downregulation of the Klotho-FGFR1c receptor complex, an increase of circulating FGF23 does not decrease parathyroid hormone levels in established chronic kidney disease. PMID: 20016468
Data indicate that cleavage at the RXXR motif abrogates FGF23 activity by removing the binding site for the binary FGFR-Klotho complex in the C-terminal region of FGF23, and by generating an endogenous inhibitor of FGF23. PMID: 19966287
a feedback loop exists among serum phosphorus, 1alpha,25(OH)(2)D(3), and FGF-23, in which the novel phosphate-regulating bone-kidney axis integrated with the parathyroid hormone-vitamin D(3) axis in regulating phosphate homeostasis PMID: 15531762
rat UMR-106 osteoblast-like cells were treated with 1,25(OH)(2)D(3) resulted in a dose- and time-dependent stimulation of FGF23 mRNA concentrations. PMID: 16020653
Mineralized tissue cells are a principal source of Fgf23. PMID: 17350357
FGF23 suppressed both parathyroid hormone (PTH) secretion and PTH gene expression PMID: 17992255
These results suggest that the N- and C-terminal domains of FGF23 are responsible for association with cognate FGF receptors and Klotho, respectively, and that these interactions are indispensable for FGF23 activity. PMID: 18442315
Results show that the elevated plasma FGF23 levels in uremic rats reflect the increased expression of FGF23 in bone. PMID: 19339809
estrogens regulate PTH indirectly, possibly through FGF23 PMID: 19628670

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.