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ActoFactor™ Recombinant Human Fibroblast growth factor 2 (basic) (147 aa)
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Cat.No.
CSC-CTK0137
Description
Recombinant Human basic Fibroblast Growth Factor (rHu bFGF) is a heparin binding growth factor, which stimulates the proliferation of a wide variety of cells including mesenchymal, neuroectodermal and endothelial cells. rHu bFGF also exerts a potent angiogenic activity in vivo. Recombinant human FGF-b (FGF-2) produced in E. coli is a single, non-glycosylated polypeptide chain of 147 amino acids having a molecular mass of 16,539 Dalton.
Species
Human
Product Overview
Human FGF2 expressed in E.coli
Molecular Mass
16.54 kDa
Size
CAT# CSC-CTK0137-10 (10 μg); CAT# CSC-CTK0137-50 (50 μg)
Expression System
E.coli
Purity
Greater than 97% as determined by SDS-PAGE and HPLC analysis.
Activity
The ED50, calculated by the dose-dependent proliferation of mouse BALB/c 3T3 cells, was found to be 0.01-0.17 ng/ml, corresponding to a specific activity of between 5.8 x 10^6 and 1 x 10^7 units/mg.
Endotoxin Level
N/A
Formulation
FGF-2 was lyophilized from a concentrated (1 mg/ml) sterile protein solution containing 10 mM sodium phosphate buffer (pH 8).
Reconstitution
Please centrifuge product briefly before opening vial. The lyophilized protein should be reconstituted in sterile, ultra-pure water to a concentration of 0.1 - 1.0 mg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted protein should be used immediately or stored long-term in undiluted working aliquots at -20°C. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
Citation Guidance
If you use this products in your scientific publication, it should be cited in the publication as: Creative Bioarray cat no. If your paper has been published, please click here to submit the PubMed ID of your paper to get a coupon.
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