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Proteins and Enzymes

Human aFGF / FGF1 Protein View larger

Human aFGF / FGF1 Protein

10013-HNAE

Activity: Measured in a cell proliferation assay using BALB/c 3T3 mouse fibroblasts. The ED50 for this effect is typically 50-200 pg/ml.


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Data sheet

Molecular WeightThe recombinant human FGF acidic consists of 141 amino acids and has a calculated molecular mass of 16 kDa as estimated by SDS-PAGE under reducing conditions.
Storage ConditionSamples are stable for up to twelve months from date of receipt at -70℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Purity95% as determined by SDS-PAGE

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Protein Construction: A DNA sequence encoding the mature form of human FGF acidic (AAA79245.1) (Phe 16-Asp 155) was expressed, with an additional Met at the N-terminus.

Formulation: Lyophilized from sterile PBS, pH 7.41. Normally 5% - 8% trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.2. Please contact us for any concerns or special requirements.Please refer to the specific buffer information in the hard copy of CoA.

Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

FGF1 Background Information: aFGF, also known as FGF1 and HBGF-1, is a member of the fibroblast growth factor family. The biological activity of aFGF protein is exerted through binding to four high affinity cell surface receptors (FGFR1–4), which results in receptor dimerization and transphosphorylation in the tyrosine kinase domain. aFGF protein shows a wide range of endocrine-like activities. As a multiple function growth factor, this protein is involved in embryo development and tissue repair. Additionally, this protein is considered to function in several important physiological and pathological processes, such as embryonic development, morphogenesis, angiogenesis, wound healing and atheromatosis, carcinogenesis, development, and invasion of cancer.

References:

  • Jaye M., et al.,-1986, Human endothelial cell growth factor: cloning, nucleotide sequence, and chromosome localization. Science 233:541-545.
  • Mergia A., et al.,-1989, Structural analysis of the gene for human acidic fibroblast growth factor.Biochem. Biophys. Res. Commun. 164:1121-1129.
  • Wang W.P., et al.,-1989, Cloning of the gene coding for human class 1 heparin-binding growth factor and its expression in fetal tissues.Mol. Cell. Biol. 9:2387-2395.