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Key Documents

F3685

Sigma-Aldrich

Fibroblast Growth Factor-Basic, human

≥97% (SDS-PAGE), recombinant, expressed in E. coli, carrier free, suitable for cell culture

Synonyme(s) :

FGB-b, FGF-2, HBGF-2, HBGH-2, Prostatropin, bFGF

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About This Item

Code UNSPSC :
12352202
Nomenclature NACRES :
NA.77

product name

Fibroblast Growth Factor-Basic, FGF-Basic, from human, recombinant, expressed in E. coli, carrier free

Source biologique

human

Niveau de qualité

Produit recombinant

expressed in E. coli

Pureté

≥97% (SDS-PAGE)

Forme

lyophilized powder

Puissance

<1 ng/mL Biological Activity EC50

Poids mol.

16.0 kDa

Conditionnement

pkg of 4X25 μg
pkg of 25 μg

Conditions de stockage

avoid repeated freeze/thaw cycles

Couleur

white to faint yellow cast

Solubilité

water: soluble 0.025 mg, clear, colorless to faintly yellow

Numéro d'accès UniProt

Température de stockage

−20°C

Informations sur le gène

human ... FGF2(2247)

Description générale

Since FGF-Basic is found in a variety of organs, acts on a wide range of cell types, and has multifunctional actions, it has acquired numerous synonyms, including heparin-binding growth factor (class II or beta), eye-derived growth factor I, cartilage-derived growth factor, and astroglial growth factor II5. Purified bovine and human FGF-basic differ by 3 amino acids in sequence3, and are biologically and immunologically cross-reactive.

Formule chimique

1. Gospodarowicz, D., Localization of a fibroblast growth factor and its effect alone and with hydrocortisone on 3T3 cell growth. Nature, 249, 123-127 (1974).
2. Gospodarowicz, D. et al., Structural characterization and biological functions of fibroblast growth factor. Endo. Rev., 8, 95-114 (1987).
3. Esch, F. et al., Primary structure of bovine pituitary basic fibroblast growth factor (FGF) and comparison with the amino-terminal sequence of bovine brain acidic FGF. Proc. Natl. Acad. Sci. USA, 82, 6507-6511 (1985).
4. Neufeld, G., and Gospodarowicz, D., Basic and acidic fibroblast growth factors interact with the same cell surface receptors. J. Biol. Chem., 261, 5631-5637 (1986).
5. Lobb, R.R. et al., Purification of heparin-binding growth factors. Anal. Biochem., 154, 1-14 (1986).
6. Abraham, J.A., Human basic fibroblast growth factor: nucleotide sequence and genomic organization. EMBO J., 5, 2523- 2528 (1986).

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Parash Parajuli et al.
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PathoGenetics, 2(1), 2-2 (2009-04-30)
Hydrolethalus syndrome (HLS) is a severe fetal malformation syndrome characterized by multiple developmental anomalies, including central nervous system (CNS) malformation such as hydrocephaly and absent midline structures of the brain, micrognathia, defective lobation of the lungs and polydactyly. Microscopically, immature
Xiaotang Wang et al.
MedComm, 4(1), e198-e198 (2022-12-31)
Stem cell therapy is a promising strategy to rescue visual impairment caused by retinal degeneration. Previous studies have proposed controversial theories about whether in situ retinal stem cells (RSCs) are present in adult human eye tissue. Single-cell RNA sequencing (scRNA-seq)
Andrzej Swistowski et al.
PloS one, 4(7), e6233-e6233 (2009-07-15)
Human embryonic stem cells (hESCs) may provide an invaluable resource for regenerative medicine. To move hESCs towards the clinic it is important that cells with therapeutic potential be reproducibly generated under completely defined conditions. Here we report a four-step scalable
Hiroko Kita-Matsuo et al.
PloS one, 4(4), e5046-e5046 (2009-04-09)
Developmental, physiological and tissue engineering studies critical to the development of successful myocardial regeneration therapies require new ways to effectively visualize and isolate large numbers of fluorescently labeled, functional cardiomyocytes. Here we describe methods for the clonal expansion of engineered

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