Hu-Cytokines

Recombinant Human FGF-8b

Cat No. Size Price Add Cart
HST-F8-0010 10ug $ 121.00 Add Cart
HST-F8-0100 100ug $ 660.00 Add Cart
HST-F8-1000 1000 $ 3350.00 Add Cart

Product Specifications

•      Expression of Human Proteins in Human Cells

•      Extreme low Endotoxin

•      High Purity

•      Animal Free and Xeno Free

•      Tag Free

Source: Human cells derived

Structure: Glycosylated homodimer

Purity: >95% by SDS-PAGE

Endotoxin Level: <0.5EU/ug

Molecular Weight: 30-45kDa

Formulation: Lyophilized from a 0.2μm filtered solution in PBS without carrier protein

 

Activity Assay

The activity was measured by its ability to stimulate the proliferation of 3T3 mouse fibroblast cells.

Reconstitution

Briefly centrifuge the vial before opening. It is recommended to reconstitute the protein in sterile PBS containing 0.1% endotoxin-free recombinant human serum albumin.

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles. In general: 12 months from date of receipt, -20 to -80°C as supplied. 1 month, 2 to 8°C under sterile conditions after reconstitution. 3 months, -20 to -80°C under sterile conditions after reconstitution.

Protein Description

FGF-8b(FGF-8) is belonging to the FGF family, which is widely expressed during embryogenesis. There are four  known  alternate  spliced  forms of FGF-8: FGF-8a, FGF-8b, FGF-8e and FGF-8f. Proteins of this family play an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. FGF-8b is required for normal brain,  eye,  ear and limb  development  during  embryogenesis. It is also required for normal development of the gonadotropin-releasing hormone (GnRH) neuronal system during prenatal development, postnatal growth and regeneration of a variety of tissues, by promoting cellular proliferation and differentiation. FGF-8b shows the strongest receptor affinity and oncogenic transforming capacity.

References

Gemel J, et al. (1996) Genomics 35,253-257.

Ornitz DM, et al. (1996) J. Biol. Chem. 271, 15292-15297.

Vantaggiato C, et al. (2011) Brain 134, 1808-1828.