F5542
Fibroblast Growth Factor-Acidic human
FGF-Acidic, recombinant, expressed in E. coli, suitable for cell culture
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Synonym(s):
FGF-1, aFGF
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biological source
human
Quality Level
recombinant
expressed in E. coli
Assay
≥97% (SDS-PAGE)
form
lyophilized powder
potency
0.287 ng/mL
quality
endotoxin tested
mol wt
15.5 kDa
packaging
pkg of 25 μg
storage condition
avoid repeated freeze/thaw cycles
technique(s)
cell culture | mammalian: suitable
impurities
≤1.0 EU/mg (LAL test)
UniProt accession no.
storage temp.
−20°C
Gene Information
human ... FGF1(2246)
Related Categories
General description
Fibroblast Growth Factor-Acidic (FGF1) belongs to the FGF family and comprises a nuclear export sequence (NES). FGF1 gene is mapped to human chromosome 5q31.3. FGF1 is highly expressed in the central and peripheral nervous system.
Application
Fibroblast Growth Factor-Acidic human has been used:
- as a component of growth factor cocktail for treating neural stem cell (NSC) transplants
- as a component of Human Neural Stem Cell (HNSC) proliferation medium for Neural Tissue Spheres (NTS) propagation
- as a growth factor component in fibrin matrix to support embryonic day 14 (E14) cells graft survival
Biochem/physiol Actions
Fibroblast Growth Factor-Acidic (FGF1) is a potent mitogenic agent associated with a variety of tissue origins including liver, vasculature, and skin. These include for a wide variety of mesoderm-derived cells including BALB/c 3T3 fibroblasts, capillary and endocardial endothelial cells, myoblasts, vascular smooth muscle cells, mesothelial cells, glial and astroglial cells, and adrenal cortex. FGF1 participates in glucose homeostasis, adipose tissue remodeling and is a key transducer of the nuclear receptor, peroxisome proliferator-activated receptor γ (PPARγ). FGF1 is a neuronal cell neurotrophic factor and binds to most of the isoforms of the FGF receptor (FGFR) isoforms. Along with FGF2, FGF1 plays a key role in angiogenesis and favors blood vessel formation in chronic inflammatory diseases and cancer. The FGF1 mutant R50E leads to suppression of its angiogenic potential making it a potential anti-angiogenesis agent.
Physical form
The product is lyophilized from a 0.2 μm filtered solution of 20 mM Tris, 1 M NaCl, 5 mM DTT containing 50 μg of bovine serum albumin per 1 μg of cytokine.
Analysis Note
The proliferative activity is tested in culture using quiescent NR6R-3T3 fibroblasts.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Seiji Mori et al.
PloS one, 8(2), e57927-e57927 (2013-03-08)
Fibroblast growth factor-1 (FGF1) and FGF2 play a critical role in angiogenesis, a formation of new blood vessels from existing blood vessels. Integrins are critically involved in FGF signaling through crosstalk. We previously reported that FGF1 directly binds to integrin
Paul Lu et al.
Cell, 150(6), 1264-1273 (2012-09-18)
Neural stem cells (NSCs) expressing GFP were embedded into fibrin matrices containing growth factor cocktails and grafted to sites of severe spinal cord injury. Grafted cells differentiated into multiple cellular phenotypes, including neurons, which extended large numbers of axons over
Xing-Rong Yan et al.
Cell biochemistry and function, 31(6), 526-531 (2012-11-23)
In mammals, breeding is preceded by species-specific mating behaviours. In this study, we investigated whether parthenogenetic embryo quality could be improved by mating behaviours in mice. To investigate this hypothesis, female mice were mated with vasectomized Kunming white male mice
Zhifeng Huang et al.
Cell reports, 20(7), 1717-1728 (2017-08-17)
The recent discovery of metabolic roles for fibroblast growth factor 1 (FGF1) in glucose homeostasis has expanded the functions of this classically known mitogen. To dissect the molecular basis for this functional pleiotropy, we engineered an FGF1 partial agonist carrying triple
T Yamashita et al.
Biochemical and biophysical research communications, 277(2), 494-498 (2000-10-18)
We isolated mouse cDNA encoding a novel FGF (251 amino acids). As this is the 23rd documented FGF, we termed it FGF-23. FGF-23 has a hydrophobic amino terminus ( approximately 24 amino acids), which is a typical signal sequence. As
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