Fibroblast Growth Factors, FGFs

Expression system: E. coli
Length: 38-208, Full Length of Mature Protein
Activity: Organoid Coculture、Cells

Expression system: E. coli
Length: 143-288, Full Length of Mature Protein of Isoform 1
Activity: Organoid Coculture、Cells

In mammalian embryos, transient Fgf8 expression defines the developing isthmic region, lying between the midbrain and the first rhombomere, but there has been uncertainty about the existence of a distinct isthmic segment in postnatal mammals. Retinoic acid (RA) directly represses Fgf8 through a RARE-mediated mechanism that promotes repressive chromatin, thus providing valuable insight into the mechanism of RA-FGF antagonism during progenitor cell differentiation. Fgf8 encodes a key signaling factor, and its precise regulation is essential for embryo patterning.

Expression system: E. coli
Length: 32-194, Full Length of Mature Protein
Activity: Cell Activity

Expression system: E. coli
Length: 1-208, Full Length
Activity: Cell Activity

Expression system: E. coli
Length: 1-154, Full Length
Activity: Cell Activity

Expression system: E. coli
Length: 54-206, Partial
Activity: Cell Activity

Expression system: E. coli
Length: 23-216, Full Length of Mature Protein
Activity: Cell Activity

Fibroblast growth factor-9 (FGF-9) is an approximately 26 kDa secreted glycoprotein of the FGF family. Secreted mouse FGF-9 lacks the N-terminal 1-3 aa and shares >98% sequence identity with rat, human, equine, porcine and bovine FGF-9. FGF-9 plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. In the mouse embryo the location and timing of FGF-9 expression affects development of the skeleton, cerebellum, lungs, heart, vasculature, digestive tract, and testes .It 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. Deletion of mouse FGF-9 is lethal at birth due to lung hypoplasia, and causes rhizomelia, or shortening of the proximal skeleton. An unusual constitutive dimerization of FGF 9 buries receptor interaction sites which lowers its activity, and increases heparin affinity which inhibits diffusion. A spontaneous mouse mutant, Eks, interferes with dimerization, resulting monomeric, diffusible FGF-9 that causes elbow and knee synostoses (joint fusions) due to FGF-9 misexpression in developing joints.

FGF-18 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 22.5 kDa and the accession number is A0A7U3JW51.

Expression system: E. coli
Length: 16-155, Full Length of Mature Protein
Activity: Cell Activity

FGF-21 Protein, Human, Recombinant is expressed in E. coli expression system. The predicted molecular weight is 19.55 kDa and the accession number is NP_061986.1.

Expression system: HEK293 Cells
Length: 1-210, Full Length
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 13-158, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 16-155, Full Length of Mature Protein
Activity: Cell Activity

FGF-18 Protein, Rat, Recombinant is expressed in E. coli. The accession number is O88182.

Expression system: E. coli
Length: 32-194, Full Length of Mature Protein
Activity: Organoid Coculture

FGF-2 Protein, Human, Recombinant (K128N) is expressed in E. coli expression system. The predicted molecular weight is 17 KDa and the accession number is P09038-2.

Expression system: HEK293 Cells
Length: 4-208, Partial
Activity: Cell Activity

In mammalian embryos, transient Fgf8 expression defines the developing isthmic region, lying between the midbrain and the first rhombomere, but there has been uncertainty about the existence of a distinct isthmic segment in postnatal mammals. Retinoic acid (RA) directly represses Fgf8 through a RARE-mediated mechanism that promotes repressive chromatin, thus providing valuable insight into the mechanism of RA-FGF antagonism during progenitor cell differentiation. Fgf8 encodes a key signaling factor, and its precise regulation is essential for embryo patterning.

FGF-2 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 18.5 kDa and the accession number is P15655.

FGF19, also known as FGF-19, is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF19 interacts with FGFR1, FGFR2, FGFR3 and FGFR4. Affinity between fibroblast growth factors (FGFs) and their receptors is increased by KL, KLB and heparan sulfate glycosaminoglycans that function as coreceptors. It interacts with KL and KLB directly. However, it interacts with FGFR4 in the presence of heparin, KL or KLB. FGF19 is involved in the suppression of bile acid biosynthesis through down-regulation of CYP7A1 expression, following positive regulation of the JNK and ERK1 2 cascades. It also stimulates glucose uptake in adipocytes.

Expression system: E. coli
Length: 11-154, Partial
Activity: Cell Activity

Fibroblast growth factor 4(FGF-4) is a heparin binding member of the FGF family. The human FGF4 cDNA encodes 206 amino acids (aa) with a 33 aa signal sequence and a 173 aa mature protein with an FGF homology domain that contains a heparin binding region near the C-terminus. Mature human FGF4 shares 91%, 82%, 94% and 91% aa identity with mouse, rat, canine and bovine FGF4, respectively. Human FGF-4 has been shown to exhibit cross species activity. Expression of FGF-4 and its receptors, FGF R1c, 2c, 3c and 4, is spatially and temporally regulated during embryonic development. FGF-4 is proposed to play a physiologically relevant role in human embryonic stem cell selfrenewal. It promotes stem cell proliferation, but may also aid differentiation depending on context and concentration, and is often included in embryonic stem cell media in vitro. FGF-4 is mitogenic for fibroblasts and endothelial cells in vitro and has autocrine transforming potential. It is a potent angiogenesis promoter in vivo and has been investigated as therapy for coronary artery disease.