Recombinant Mouse Fibroblast Growth Factor 9 (FGF9) Protein (His), Active

Name: Recombinant Mouse Fibroblast Growth Factor 9 (FGF9) Protein (His), Active
Brand: Beta LifeScience
SKU: BLC-05923P
Availability: InStock

Greater than 95% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Fibroblast Growth Factor 9 (FGF9) Protein (His), Active is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	The ED50 as determined in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells is less than 10 ng/ml.
Uniprotkb	P54130
Target Symbol	FGF9
Synonyms	Fgf9; Fgf-9Fibroblast growth factor 9; FGF-9; Glia-activating factor; GAF; HBGF-9
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His
Complete Sequence	MAPLGEVGSYFGVQDAVPFGNVPVLPVDSPVLLSDHLGQSEAGGLPRGPAVTDLDHLKGILRRRQLYCRTGFHLEIFPNGTIQGTRKDHSRFGILEFISIAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTQECVFREQFEENWYNTYSSNLYKHVDTGRRYYVALNKDGTPREGTRTKRHQKFTHFLPRPVDPDKVPELYKDILSQS
Expression Range	1-208aa
Protein Length	Full Length
Mol. Weight	24.4 kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	0.2 μm Filtered 20 mM Tris-HCl, 150 mM NaCl, 5% Trehalose, 1 mM EDTA, 20% Glycerol, 1 mM DTT, pH 8.5
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.

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	KEGG: mmu:14180 STRING: 10090.ENSMUSP00000022545 UniGene: PMID: 28395336 the localization of FGF9 and its receptors at different embryonic and postnatal stages in mice testes, was examined. PMID: 27078042 results suggested that the combination of nCS (to support bone formation) with a fibrin-based VEGF/FGF9 release system (support vascular formation) is an innovative and effective strategy that significantly enhanced ectopic bone formation in vivo. PMID: 27269204 FGF9 is a crucial factor required for establishing an appropriate microenvironment for successful implantation and for pregnancy establishment. Additional analyses of pathways through which FGF9 participates in angiogenesis and endometrium-embryo communication should contribute to the understanding of molecular mechanisms that underlay process of implantation. PMID: 28848153 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 Our results suggest that mature osteoblasts are an important source of FGF9, positively regulating skeletal homeostasis in male mice PMID: 28189801 suggests FGF-9 has the potential to attenuate vascular cell apoptosis, activate c-Kit progenitor cells, and enhance angiogenesis and neovascularization in C57BL/6 and db/db mice leading to improved cardiac function. PMID: 26682010 Sox11 directly regulates the expression of Fgf9; ablation of the Sox11 gene results in clefting of the secondary palate resembling the Pierre Robin sequence. PMID: 26826126 data demonstrated that overexpressing FGF9 in PCa cells augmented the formation of reactive stroma and promoted PCa initiation and progression PMID: 26157349 These studies identify FGF9 as a target of DICER1 in lung epithelium that functions as an initiating factor for pleuropulmonary blastoma. PMID: 25978641 FGF-9 possesses novel therapeutic potential in its ability to mediate monocyte to M2 differentiation and confer cardiac protection in the post-infarction diabetic heart. PMID: 25768089 Data show that Fibroblast Growth Factors (FGF) 9 and 20 regulate the number of cochlear progenitors. PMID: 25915623 cerebellar microexplant cultures treated with an FGFR agonist or antagonist, we also show that FGF9/FGFR-mediated signaling inhibits the outward migration of radial glia and Bergmann glia precursors and cells PMID: 24983448 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 Demonstrate the complex role of FGF9-FGFR3 signalling in the initiation, growth and propagation of lung cancer. PMID: 25413587 FGF9 overexpression in lung leads to adenocarcinoma. PMID: 23867472 Loss of Fgf9 in XX Wnt4-/- gonads does not rescue their partial female-to-male sex-reversal. PMID: 22705479 The data suggested that, at a minimum, Fgf9/20 and Bmp7 organize the nephron progenitor niche. FGF signaling likely regulates multiple important steps in the niche, including survival, proliferation, and competence. PMID: 22698282 TGFbeta-FGF9-PITX2 signaling cascade regulates cranial neural crest cell proliferation during palate formation. PMID: 22123828 Data point to a role of Fgf9 signalling in primary and secondary lens fiber cell growth. PMID: 21858205 Data demonstrate that mesothelial- and epithelial-derived FGF9, mesenchymal Wnt2a and epithelial Wnt7b have unique functions in lung development in mouse. PMID: 21750028 Conditional expression of FGF9 promotes myocardial vascularization and hypertrophy with enhanced systolic function and reduced heart failure mortality after MI PMID: 21262993 Results suggest collectively that Fgf9 signalling from the outer mesothelial lining induce Spred/Sprouty expression in the underlying pancreatic mesenchyme. PMID: 20934536 Fgf9 stimulates steroidogenesis in postnatal Leydig cells. PMID: 19508331 data suggest a unique role for Fgf-9 in bone healing, presumably by initiating angiogenesis through Vegf-a PMID: 20547837 Data demonstrate that FGF9 can act as a diffusible conductor for a poleward expansion of tubulogenic programs at early phases of testis differentiation. PMID: 20040496 Recombinant fgf9 protein inhibits the differentiation response of the mesoderm to Shh, but does not affect proliferation. PMID: 12781691 Data show that Fgf9 is necessary for testis development, playing a role in the proliferation of cells that give rise to Sertoli progenitors and in the nuclear localization of FGF receptor R2 in Sertoli cell precursors. PMID: 15229180 To address the role of Fgf9 signaling, we analyzed the inner ears of mice homozygous for Fgf9 null alleles. Fgf9 inactivation leads to a hypoplastic vestibular component of the otic capsule and to the absence of the epithelial semicircular ducts. PMID: 15328018 FGF9 plays an important role in proliferation and organisation of embryonic Sertoli cells during testis morphogenesis PMID: 15470636 An epithelial FGF9 signal is necessary for the expansion of cecal mesenchyme and the expression of mesenchymal genes that are required for epithelial budding. PMID: 16308329 FGF9 acts on the lung mesenchyme to induce proliferation and decrease differentiation PMID: 16494859 FGF9 is necessary for 11.5 days post coitum fetal XY gonocyte survival and is the earliest reported factor with a sex-specific role in regulating germ cell survival. PMID: 16540514 the Sprouty proteins are involved normally in mediating the sexually dimorphic signaling of FGF9 and controlling cell migration from the mesonephros during testis development PMID: 16675530 The fate of the gonad is controlled by antagonism between Fgf9 and Wnt4. PMID: 16700629 Although Fgf9 is expressed in the apical ectodermal ridge in the limb bud, we demonstrate that the Fgf9-/- limb phenotype results from loss of FGF9 functions after formation of the mesenchymal condensation. PMID: 17544391 These data suggest a molecular mechanism through which FGF9 and sonic hedgehog signaling coordinately control the growth and patterning of the lung capillary plexus, and regulate the temporal and spatial expression of Vegfa. PMID: 17881491 The interaction of FGF and TGFbeta signaling pathways in the intestinal mesenchyme could represent novel targets for future short bowel syndrome therapies. PMID: 18653563 Results show that loss of fibroblast growth factor 9 or conditional inactivation of Fgf receptors (Fgfr) 1 and 2 in mouse lung mesenchyme results in ectopic airway smooth muscle cells. PMID: 19097117 A mechanism in which the range of FGF9 signaling in developing tissues is limited by its ability to homodimerize and its affinity for extracellular matrix heparan sulfate proteoglycans. PMID: 19219044 Neuron-derived Fgf9 is essential for scaffold formation of Bergmann radial fibers and migration of granule neurons in the cerebellum. PMID: 19232523 the PGD2 signaling pathway is likely to act independently of FGF9, thus implicating two independent feedforward loops between Sox9/Fgf9 and Sox9/L-Pgds in the coordination of growth, cell differentiation and morphogenesis of the gonad. PMID: 19429785

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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.

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