FGF basic/bFGF Protein, Human (146a.a)

FGF-2 is a member of the fibroblast family involved in bone healing, cartilage repair, bone repair, and nerve regeneration. FGF-2 is also a mitotic promoter that accelerates cell proliferation. FGF-2 regulates immune processes by specifically targeting tyrosine kinase receptors and activating the FGF/FGFR signaling pathway. For example, FGF-2 is involved in the JAK-STAT signaling pathway to regulate cartilage metabolism and also activates ERK signaling to promote cartilage regeneration. FGF-2 combined with FGFR1/3 promoted degeneration and repair of articular cartilage, respectively^[1]. FGF-2 is also a known carcinogen in GBM, which contributes to glioma growth and vascularization^[2].FGF basic/bFGF Protein, Human (146a.a), consists of 146 amino acids, produced by E.coli with tag free.

FGF-2/bFGF is a member of the fibroblast family and has a high affinity for heparin. FGF-2 plays an important role in tendon to bone healing, cartilage repair, bone repair, and nerve regeneration. FGF-2 specifically binds to tyrosine kinase receptors and activates the FGF/FGFR signaling pathway. Subsequently, FGF-2 influences cell proliferation, differentiation and apoptosis, as well as immune regulation by transducing other classical pathways. For example, FGF-2 regulates the JAK-STAT signaling pathway to regulate cartilage metabolism. FGF-2 also acts as a mitotic promoter to accelerate cell proliferation. Therefore, (1) FGF-2 is an important growth factor in the healing process of ligament/tendon injury. In vitro experiments, low-dose FGF-2 can stimulate the proliferation and differentiation of bone marrow mesenchymal stem cells, and up-regulate the mRNA expression of type I/III collagen and fibronectin. However, high doses of FGF-2 did not stimulate extracellular matrix (ECM) protein proliferation and gene expression. (2) FGF-2 is also an endogenous and intrinsic growth factor in cartilage repair. FGF-2 binds to heparan sulfate proteoglycan and is stored in the ECM of articular cartilage. When cartilage is damaged or degenerated, ECM rapidly releases FGF-2 and activates ERK signaling pathways to promote cartilage regeneration. FGF-2 exhibits a biphasic effect in combination with its specific receptor. FGF-2 combined with FGFR3 promoted the repair of articular cartilage. FGF-2 combined with FGFR1 promoted the degeneration of articular cartilage^[1]. FGF-2 is expressed in granulosa cells and colliculus cells, as well as hepatocellular cancer cells, but not in non-cancerous liver tissues. This reveals the role of FGF-2 in brain tumors, particularly glioblastoma. According to studies, FGF-2 is a known carcinogenic factor in GBM. FGF-2 increases the self-renewal of glioblastoma stem cells and contributes to the growth and vascularization of glioma^[2]. FGF-2 protein is highly conserved in some species, and the similarity rate of human FGF-2 protein sequence to rat, mouse, and bovine was 97.4%, 95.45%, and 98.71%, respectively.

FGF-2 (human; 3 ng/mL, 30 ng/mL; 7-28 d) triggers the biphasic bone marrow stromal cell (BMSC) response at 3 ng/mL, promotes cell proliferation to peak on day 7, and significantly enhances mRNA expression of type I collagen, type III collagen, fibronectin, and alpha-smooth muscle actin on day 14 and 28. But there is no obvious effect at 30 ng/mL^[3].

The ED₅₀ is <2 ng/mL as measured by 3T3 cells, corresponding to a specific activity of > 5.0 × 10⁵ units/mg.

• 
  Measured in a cell proliferation assay using NIH-3T3 mouse embryonic fibroblasts. The ED₅₀ for this effect is 0.3582 ng/mL, corresponding to a specific activity is 2.79×10⁶ units/mg.

Human

E. coli

Tag Free

P09038-4 (P143-S288)

2247  [NCBI]

Full Length of Isoform-4 Mature Protein

PALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS

Approximately 14-20 kDa, based on SDS-PAGE under reducing conditions.

• 
  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4 .
2.Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 100 mM NaCl, 0.02% Tween 80, pH 7.5.
3.Lyophilized from a 0.22 μm filtered solution of 50 mM Tris-HCl, 300 mM NaCl, pH 7.4.
4.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 5% trehalose, 5% mannitol and 0.01% Tween 80.
5.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% trehalose.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<0.2 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O or PBS. 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 from date of receipt. 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]. /biology-dictionary/nci-h460-cell.html  [Content Brief]

  [2]. Zhang J, et al. FGF2: a key regulator augmenting tendon-to-bone healing and cartilage repair. Regen Med. 2020 Sep;15(9):2129-2142.  [Content Brief]

  [3]. Westermann R, et al. Basic fibroblast growth factor (bFGF), a multifunctional growth factor for neuroectodermal cells. J Cell Sci Suppl. 1990;13:97-117.  [Content Brief]

  [4]. Jimenez-Pascual A, et al. FGF2: a novel druggable target for glioblastoma? Expert Opin Ther Targets. 2020 Apr;24(4):311-318.  [Content Brief]

  [5]. Rusnati M, et al. Interaction of angiogenic basic fibroblast growth factor with endothelial cell heparan sulfate proteoglycans. Biological implications in neovascularization. Int J Clin Lab Res. 1996;26(1):15-23.  [Content Brief]

  [6]. Hankemeier S, et al. Modulation of proliferation and differentiation of human bone marrow stromal cells by fibroblast growth factor 2: potential implications for tissue engineering of tendons and ligaments. Tissue Eng. 2005 Jan-Feb;11(1-2):41-9.  [Content Brief]