FGF2
Spezies: Human
Wirt: Escherichia coli (E. coli)
Recombinant
Purity is > 98 % , as determined by Coomassie stained SDS-PAGE.
Func, AbP, STD, PI
Active
Functional Studies (Func), Antibody Production (AbP), Standard (STD), Protein Interaction (PI)
Spezifität
Optimal preservation of protein structure, post-translational modifications and functions.
Produktmerkmale
Recombinant human FGF basic / FGF2 protein expressed in E. coli.
Produced with end-sequenced ORF clone
Tested for bioactivity.
Reinheit
Purity is > 98 % , as determined by Coomassie stained SDS-PAGE.
Endotoxin-Niveau
Less than 0.01 ng per ug protein as determined by the LAL method.
Biological Activity Comment
The ED50 is 1 - 4 ng/ml, corresponding to a specific activity of 1 - 0.25 x 10^6 units/mg, determined by the dose dependent stimulation of NIH/ 3T3 cell proliferation. The bioactivity is equivalent to competitor reported values.
FGF2
Spezies: Ratte
Wirt: Escherichia coli (E. coli)
Recombinant
>95 % as determined by reducing SDS-PAGE.
Applikationshinweise
Recombinant human proteins can be used for: Native antigens for optimized antibody production Positive controls in ELISA and other antibody assays Protein-protein interaction In vitro biochemical assays and cell-based functional assays
Beschränkungen
Nur für Forschungszwecke einsetzbar
Konzentration
> 50 μg/mL
Buffer
10 mM NaH2PO4, 150 mM NaCl, pH 7.2, 1 mM DTT
Lagerung
-80 °C
Informationen zur Lagerung
Store at -80°C. Thaw on ice, aliquot to individual single-use tubes, and then re-freeze immediately. Only 2-3 freeze thaw cycles are recommended.
The protein encoded by this gene is a member of the fibroblast growth factor (FGF) family. FGF family members bind heparin and possess broad mitogenic and angiogenic activities. This protein has been implicated in diverse biological processes, such as limb and nervous system development, wound healing, and tumor growth. The mRNA for this gene contains multiple polyadenylation sites, and is alternatively translated from non-AUG (CUG) and AUG initiation codons, resulting in five different isoforms with distinct properties. The CUG-initiated isoforms are localized in the nucleus and are responsible for the intracrine effect, whereas, the AUG-initiated form is mostly cytosolic and is responsible for the paracrine and autocrine effects of this FGF.