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Human Fibroblast Growth Factor 23 Recombinant

FGF-23

accession:  Q9GZV9
   Size A     5ug   $ 70
   Size B      20ug  $160
   Size C      1mg  $ 3500
Domain  :  HBGF/IL1
Gene  :  FGF23
Catalog no. :  RKQ9GZV9
Source:
Optimized DNA sequence encoding Human Fibroblast Growth Factor-23 mature chain was expressed in Escherichia Coli.

 
Molecular weight:

Native human FGF23 is generated by the proteolytic removal of the signal peptide
and propeptide, this molecule has a calculated molecular mass of approximately 23 kDa.

Recombinant Fibroblast Growth Factor 23 is a disulfide-linked monomer protein consisting of 228 amino acid residue subunits, and migrates as an approximately 23 kDa protein under non-reducing and reducing conditions in SDS-PAGE.


 
Purity:
>96%, as determined by SDS-PAGE and HPLC

 
Biological Activity:
The ED(50) was determined by the dose-dependent  proliferation of
mouse 3T3 cells expressing FGF receptors, and was found to be
<0.3ug/ml., corresponding to a specific activity of 3.0 x 104 Units/mg.

 
Protein Sequence:
        10         20         30         40         50         60 
MLGARLRLWV CALCSVCSMS VLRAYPNASP LLGSSWGGLI HLYTATARNS YHLQIHKNGH 

        70         80         90        100        110        120 
VDGAPHQTIY SALMIRSEDA GFVVITGVMS RRYLCMDFRG NIFGSHYFDP ENCRFQHQTL 

       130        140        150        160        170        180 
ENGYDVYHSP QYHFLVSLGR AKRAFLPGMN PPPYSQFLSR RNEIPLIHFN TPIPRRHTRS 

       190        200        210        220        230        240 
AEDDSERDPL NVLKPRARMT PAPASCSQEL PSAEDNSPMA SDPLGVVRGG RVNTHAGGTG 

       250 
PEGCRPFAKF I 
(*)Complete precursor sequence shown, expressed chain highlighted
 
Endotoxin:
Endotoxin content was assayed using a LAL gel clot method.
Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).

 
Presentation:
Recombinant Human FGF23 was lyophilized from 0.2 μm filtered PBS solution, pH 7.4 .

 
Reconstitution:
A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.

 
Storage:
The lyophilized protein is stable for at least 2 years from date of receipt at -20° C.
Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8° C for one month, or at -20° C for six months, with a carrier protein without detectable loss of activity.

Avoid repeated freeze/thaw cycles.

 
Usage:
This cytokine product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.

 

 

FGF23

FGF23 is a protein of ∼30 kDa that is proteolytically processed to generate smaller NH2-terminal (18 kDa) and COOH-terminal (12 kDa) fragments. The NH2- terminal fragment of FGF23 contains the FGF receptor (FGFR)-binding domain. In vivo studies using synthetic peptides have indicated that neither of the processed NH2-terminal or COOH- terminal fragments of FGF23 can influence serum phosphate levels. FGF23 can decrease the activity of NaPi-2a and NaPi-2c cotransporters to reduce renal phosphate reabsorption and thereby can increase urinary phosphate excretion. Similarly, FGF23 can suppress the expression of 1-α-hydroxylase to reduce the production of the active vitamin D metabolite 1,25(OH)2D. Moreover, FGF23 can also induce 24- hydroxylase, which degrades 1,25(OH)2D

Related Publications:
increased circulating levels of FGF23: an adaptive response in primary hyperparathyroidism?
Eur. J. Endocrinol., Jan 2012; 166: 55 - 60.
pnas plus: iron deficiency drives an autosomal dominant hypophosphatemic rickets (adhr) phenotype in fibroblast growth factor-23 (FGF23) knock-in mice
PNAS, Nov 2011; 108: E1146 - E1155.
iron modifies plasma FGF23 differently in autosomal dominant hypophosphatemic rickets and healthy humans
J. Clin. Endocrinol. Metab., Nov 2011; 96: 3541 - 3549.
pth ablation ameliorates the anomalies of FGF23-deficient mice by suppressing the elevated vitamin d and calcium levels
Endocrinology, Nov 2011; 152: 4053 - 4061.
lanthanum carbonate reduces FGF23 in chronic kidney disease stage 3 patients
Nephrol. Dial. Transplant., Aug 2011; 26: 2567 - 2571.




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