Recombinant Human Fibroblast Growth Factor 9 Protein (FGF9), Active

Name: Recombinant Human Fibroblast Growth Factor 9 Protein (FGF9), Active
Brand: Beta LifeScience
SKU: BLC-05986P
Availability: InStock

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 Human Fibroblast Growth Factor 9 Protein (FGF9), Active is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 95% as determined by SDS-PAGE and HPLC.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	Fully biologically active when compared to standard. The ED50 as determined by thymidine uptake assay using FGF-receptors transfected BaF3 cells is less than 0.5 ng/ml, corresponding to a specific activity of >2.0x10 6 IU/mg.
Uniprotkb	P31371
Target Symbol	FGF9
Synonyms	FGF 9; FGF-9; FGF9; FGF9_HUMAN; Fibroblast growth factor 9; GAF (Glia-activafibroblast growth factor 9 (glia-activating factor); GAF; Glia Activating Factor; Glia-activating factor; HBFG 9; HBFG9; HBGF-9; Heparin-binding growth factor 9; MGC119914; MGC119915; SYNS3
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Complete Sequence	APLGEVGNYF GVQDAVPFGN VPVLPVDSPV LLSDHLGQSE AGGLPRGPAV TDLDHLKGIL RRRQLYCRTG FHLEIFPNGT IQGTRKDHSR FGILEFISIA VGLVSIRGVD SGLYLGMNEK GELYGSEKLT QECVFREQFE ENWYNTYSSN LYKHVDTGRR YYVALNKDGT PREGTRTKRH QKFTHFLPRP VDPDKVPELY KDILSQS
Expression Range	2-208aa
Protein Length	Partial
Mol. Weight	23.3 kDa
Research Area	Cancer
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 µm filtered PBS, pH 7.4
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	Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. May have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.
Subcellular Location	Secreted.
Protein Families	Heparin-binding growth factors family
Database References	HGNC: 3687 OMIM: 600921 KEGG: hsa:2254 STRING: 9606.ENSP00000371790 UniGene: Hs.111
Associated Diseases	Multiple synostoses syndrome 3 (SYNS3)
Tissue Specificity	Glial cells.

Gene Functions References

Our results indicate that miR-4317 can reduce Non-small cell lung cancer (NSCLC) cell growth and metastasis by targeting FGF9 and CCND2. These findings provide new evidence of miR-4317 as a potential non-invasive biomarker and therapeutic target for NSCLC. PMID: 30227870
We have demonstrated for the first time that mutations in FGF9 cause craniosynostosis in humans and confirm that FGF9 mutations cause multiple synostoses. PMID: 28730625
Forced expression of miR-187 inhibited the subcutaneous growth of cervical cancer cells in nude mice. Furthermore, FGF9 was found to be the downstream target of miR-187 in cervical cancer cells. PMID: 28849071
Results show compelling data that homodimerization controls receptor binding specificity of FGF9 by keeping the concentration of active FGF9 monomers at a level, which is sufficient for a normal FGFR "c" isoform binding/signaling, but is insufficient for an illegitimate FGFR "b" isoform. Mutation in FGF9 N or C-terminus skews the ligand equilibrium toward active monomers causing off-target binding and activation of FGFb. PMID: 28757146
The upregulation of FGF9 or the downregulation of miR-372-3p substantially retarded lung squamous cell carcinoma (LSCC) cell growth, mitosis, and invasion. MiR-372-3p enhanced LSCC cell proliferation and invasion through inhibiting FGF9. PMID: 28440022
Data suggest that fibroblast growth factor 9 (FGF9) may provide the anti-apoptotic function and be useful as a novel independent marker for evaluating gastric cancer (GC) prognosis. PMID: 27166269
CCND1 mRNA expression is increased by FGF9 in bovine theca cells and granulosa cells. PMID: 27816766
The present data indicate that non-natural FGFR2 ligands, such as FGF10 and FGF19, are important factors in the pathophysiology of Aspert syndrome. PMID: 27339175
In FGF9-overexpressing colorectal cancer cell lines, FGF9 overexpression induced strong resistance to anti-EGFR therapies via the enforced FGFR signal, and this resistance was cancelled by the application of an FGFR inhibitor. PMID: 26916220
FGF9 and FGF18 increased the migratory capacities of human lung fibroblasts, and FGF9 actively modulated matrix metalloproteinase activity in idiopathic pulmonary fibrosis. PMID: 26773067
we conclude that the S99N mutation in Fgf9 causes multiple synostoses syndrome (SYNS) via the disturbance of joint interzone formation. These results further implicate the crucial role of Fgf9 during embryonic joint development PMID: 28169396
These studies identify FGF9 as a target of DICER1 in lung epithelium that functions as an initiating factor for pleuropulmonary blastoma. PMID: 25978641
Data indicate that expressing either human FGF9 in the kidney subcapsular space of female BALB/c mice yielded rapidly expanding local tumors. PMID: 26183774
FGF9 was strongly expressed in CAFs in comparison with NGFs, being compatible with microarray data indicating that FGF9 was a novel growth factor overexpressed in Cancer-associated fibroblasts PMID: 25925261
the relative levels of FGF9 in relation to other members of the FGF family may prove key to understanding vulnerability or resilience in affective disorders. PMID: 26351673
we found that Kl treatment impairs Nodal mRNA expression and Fgf9-mediated Nanos2 induction, reinforcing the antagonistic effect of these two growth factors on the meiotic fate of male germ cells PMID: 25766327
our data demonstrate that FGF9 can initiate a complex astrocytic response predicted to compromise remyelination, while at the same time stimulating microglial/macrophage recruitment in multiple sclerosis lesions PMID: 25907862
expression is associated with poor prognosis in lung cancer PMID: 24239165
MAP3K1 mutations tilt the balance in the sex-determining pathways by downregulating SOX9 and FGF9. PMID: 24135036
The data demonstrates that FGF9 IRES functions as a cellular switch to turn FGF9 protein synthesis 'on' during hypoxia, a likely mechanism underlying FGF9 overexpression in cancer cells. PMID: 24334956
FGF9 was proved to be a direct target of miR-26a PMID: 24015269
FGF9 can be associated with epithelial-to-mesenchymal transition and invasion by inducing VEGF-A expression in prostate cancer cells. PMID: 24511001
In addition to the role of sex determination, FGF9 is expressed in postnatal Leydig cells and is involved in cell-to-cell interaction of testicular function. Aberrant expression of testicular FGF9 is associated with SCOS. PMID: 24011613
The results demonstrate that FGF9 protein increased in regions of active cellular hyperplasia, metaplasia, and fibrotic expansion of idiopathic pulmonary fibrosis lungs. PMID: 23797050
The importance of Fgf9 in hair follicle regeneration suggests that it could be used therapeutically in humans. PMID: 23727932
neither DMRT1 nor FGF9 abnormalities are frequently involved in dysgenetic male gonad development in patients with non-syndromic 46,XY disorder of sex development. PMID: 22939835
the FGF9(S99N) monomer is preferred to bind with the FGFR3c receptor to form an inactive complex, leading to impaired FGF signaling; the impaired FGF signaling is believed to be a potential cause of synostoses syndrome, implicating an important role for FGF9 in normal joint development PMID: 22920789
These results indicate that FGF9 can stimulate proliferation and invasion in prostate cancer cells, thus FGF9 could be a candidate of a predictive factor for recurrence after radical prostatectomy. PMID: 22006051
Fibroblast growth factor 9 was also overexpressed in all serous ovarian tumors with greater than 1000-fold increase in gene expression in 4 tumors. PMID: 21666490
Microvessels formed in the presence of FGF9 had enhanced capacity to receive flow and were vasoreactive. PMID: 21499246
FGF9 is an autocrine estromedin endometrial stromal growth factor that plays roles in cyclic proliferation of uterine endometrial stroma PMID: 12072406
The capability of proliferation possessed by endometriotic stromal cell during menstruation when ovarian 17 beta-estradiol is in the nadir may be mediated, at least in part, by autocrined estrogen-stimulated expression of FGF-9 and its receptors. PMID: 14602803
Recombinant human FGF-9 signaling enhances the intrinsic osteogenic potential by selectively expanding committed chick embryo osteogenic cell populations as well as inversely regulating bone morphogenetic protein 2 (BMP-2) and noggin gene expression. PMID: 15780951
Mesothelial and epithelial transgenic FGF9 directs lung development by regulating mesenchymal growth, and the pattern and expression levels of mesenchymal growth factors that signal back to the epithelium. PMID: 16540513
Our findings may also provide a molecular framework for considering roles for PGE2 in FGF-9-related embryonic development and/or human diseases. PMID: 16982695
Polymorphic microsatellite in the 3'-UTR of FGF9 in patients with Gonadal dysgenesis. PMID: 17154280
FGF9 mutant tumors showed normal membranous beta-catenin expression and the absence of mutation in the beta-catenin gene PMID: 18165946
Inhibition of fibroblast growth factor 19 reduces tumor growth by modulating beta-catenin signaling. PMID: 18593907
Androgen receptor-negative human prostate cancer cells induce osteogenesis in mice through FGF9-mediated mechanisms. PMID: 18618013
the study ruled out microdeletions on the critical region as a common cause of Moebius syndrome and excluded FGF9 gene PMID: 19460469
Data demonstrate that homodimerization autoregulates FGF9 and FGF20's receptor binding and concentration gradients in the extracellular matrix. PMID: 19564416
Data demonstrate a previously uncharacterized mutation in FGF9 as one of the causes of Multiple synostoses syndrome, implicating an important role of FGF9 in normal joint development. PMID: 19589401

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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.