FGF-9 Protein, Mouse (N-His)

FGF-9 is a member of mouse heparin-binding fibroblast growth factors located on the outside of cell membranes. FGF-9 is a regulator of chondrogenesis and vascularization during bone development. FGF-9 binds to fibroblast growth factor receptors (FGFRs) to activate downstream signaling pathways, such as PI3K-AKT, RAS-MAPK and protein kinase C (PKC) pathways. FGF-9 regulates embryonic development, cell proliferation, cell differentiation and cell migration. FGF-9 plays an important role in differentiation, survival of neuronal cells and growth stimulation of glial tumors. FGF-9 Protein, Mouse (N-His) is a recombinant protein with a N-His label that consisting of 208 amino acids and is produced in E. coli^{[1][2][3][4][5]}.

Fibroblast growth factors are important growth factors for physiological systems, and play critical and multifunctional roles during development, tumorigenesis, neuronal systems and disease progressions. FGF-9 Protein (Mouse) involves in neuronal disorders, plays an important role for brain development and functions^[1].
FGF-9 Protein (Mouse) expression is principally restricted to the splanchnic mesodermal plate (SMP) and the mesothelium during early development, then subsequently expressed by both the mesothelium and rare epithelial cells splanchnic mesodermal plate (SMP) of mice^[1].
Loss of FGF-9 Protein (Mouse) in mice leads to pancreatic hypoplasia and asplenia^[1].
FGF-9 Protein (Mouse) reduces TBHP-induced oxidative stress in chondrocytes and diminishes mouse osteoarthritis by activating ERK/Nrf2 signaling pathway^[2].
FGF-9 Protein (Mouse) inhibits cell apoptosis and senescence by activating intracellular HO-1 and γ-GCSc in PD models, upregulated Nrf2 expression and enhanced antioxidant effects in HD striatal cells^[2].
FGF-9 Protein (Mouse) attenuates sepsis-induced fulminant hepatitis in mice^[3].
FGF-9 Protein (Mouse) alleviates the infltration of neutrophils into the liver, and decreased the serum levels of pro‐infammatory cytokines such as tumor necrosis factor-alpha (TNF-α) and interleukin-6 (IL-6) in Lipopolysaccharide (LPS) (HY-D1056)/D-galactosamine (D-Gal) (HY-42682) (LPS/D-Gal)-challenged mice^[3].
FGF-9 Protein (Mouse) facilitates palatal growth and timely elevation by regulating cell proliferation and hyaluronic acid accumulation in mice^[4].

FGF-9 Protein (Mouse) (50, 100 ng/mL) protects chondrocytes against apoptosis from tert-butyl hydroperoxide (TBHP) (40 μM)-induced cellular damage^[2].
FGF-9 Protein (Mouse) (100 ng/mL) reduces TBHP (40 μM)-induced oxidative stress, mitochondrial dysfunction and arouses the Nrf2 signaling pathway in chondrocytes^[2].

Loss of FGF-9 Protein (Mouse) leads to asplenia, abnormal pancreatic and gastric development, hypoplastic lungs leading to respiratory failure in mice with a functional knockout of FGF-9. Additionally, loss of FGF-9 Protein (Mouse) reduces numbers of early pancreatic progenitors and displays defects in epithelial structure and mesothelial development in mice with a functional knockout of FGF-9^[1].
FGF-9 Protein (Mouse) (1 µg/kg, intraarticular injection, daily for 8 weeks) ameliorates osteoarthritis (OA) in medial meniscus instability (DMM) mice^[2].
FGF-9 Protein (Mouse) (0.5 or 1.5 mg/kg, i.p., administered 1 h before and after intraperitoneal injection of LPS/D-Gal) signifcantly attenuates LPS/D-Gal-induced liver damage in mice^[3].
FGF-9 Protein (Mouse)^−/− mouse embryos displays defective palatal growth and palatal elevation, exhibits aberrant cell proliferation and increases cell density, impairs palatal growth and elevation due to abnormal HA accumulation and cell proliferation^[4].
Loss of FGF-9 Protein (Mouse) in mouse tendon progenitors leads to impaired apophyseal, entheseal growth and enthesis mechanical properties^[5].

Measured in a cell proliferation assay using NIH/3T3 mouse fibroblast cells in the presence of 10 µg/mL of heparin. The ED₅₀ is 0.4023 ng /mL.

Mouse

E. coli

N-6*His

P54130 (A2-S208)

14180  [NCBI]

APLGEVGSYFGVQDAVPFGNVPVLPVDSPVLLSDHLGQSEAGGLPRGPAVTDLDHLKGILRRRQLYCRTGFHLEIFPNGTIQGTRKDHSRFGILEFISIAVGLVSIRGVDSGLYLGMNEKGELYGSEKLTQECVFREQFEENWYNTYSSNLYKHVDTGRRYYVALNKDGTPREGTRTKRHQKFTHFLPRPVDPDKVPELYKDILSQS

Approximately 27.91 kDa

• 
  Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.2 μm filtered solution of 20 mM Tris, 500 mM NaCl, pH 8.5.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Patzek S, et al. Loss of Fgf9 in mice leads to pancreatic hypoplasia and asplenia. iScience. 2023 Mar 25;26(4):106500.  [Content Brief]

  [2]. Pan YN, et al. Fibroblast growth factor 9 reduces TBHP-induced oxidative stress in chondrocytes and diminishes mouse osteoarthritis by activating ERK/Nrf2 signaling pathway. Int Immunopharmacol. 2023 Jan;114:109606.  [Content Brief]

  [3]. Li A, et al. Fibroblast growth factor 9 attenuates sepsis-induced fulminant hepatitis in mice. Amino Acids. 2022 Jul;54(7):1069-1081.  [Content Brief]

  [4]. Li R, Sun Y, et al. The Fibroblast Growth Factor 9 (Fgf9) Participates in Palatogenesis by Promoting Palatal Growth and Elevation. Front Physiol. 2021 Apr 20;12:653040.  [Content Brief]

  [5]. Ganji E, et al. Targeted deletion of Fgf9 in tendon disrupts mineralization of the developing enthesis. FASEB J. 2023 Mar;37(3):e22777. doi: 10.1096/fj.202201614R. Erratum in: FASEB J. 2023 Apr;37(4):e22856.  [Content Brief]