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This protein carries no "tag".
The protein has a calculated MW of 19.0 kDa. The protein migrates as 27 kDa±3 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under non-reducing (NR) condition (SDS-PAGE) due to glycosylation.
>95% as determined by SDS-PAGE.
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.
Contact us for customized product form or formulation.
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
Human FGF-7 Protein, premium grade on SDS-PAGE under non-reducing (NR) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).
Immobilized Human FGF-7 Protein, premium grade (Cat. No. FG7-H5213) at 5 μg/mL (100 μL/well) can bind Human FGF R2 (IIIb), Fc Tag (Cat. No. FGB-H5256) with a linear range of 1-78 ng/mL (Routinely tested).
Human FGF R2 (IIIb), Fc Tag (Cat. No. FGB-H5256) immobilized on CM5 Chip can bind Human FGF-7 Protein, premium grade (Cat. No. FG7-H5213) with an affinity constant of 176 nM as determined in a SPR assay (Biacore 8K) (Routinely tested).
GMP Human Activin A Protein (Cat. No. GMP-ACAH37) and Human FGF-7 Protein, premium grade (Cat. No. FG7-H5213) coating with GMP Human Laminin 521 Protein (Cat. No. GMP-LA5H24) could induce the PP2 (Pancreatic progenitor cells) differentiation, with high expression of marker genes (PDX1 and SOX9) in immunofluorescence.
GMP Human Activin A Protein (Cat. No. GMP-ACAH37) and Human FGF-7 Protein, premium grade (Cat. No. FG7-H5213) coating with GMP Human Laminin 521 Protein (Cat. No. GMP-LA5H24) could induce the PP2 (Pancreatic progenitor cells) differentiation, with high expression of marker genes (PDX1, SOX9 and NKX6.1) in FACS.
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