Recombinant Human FGF-9, Animal-Free Protein New

Catalog #: Qk039 Datasheet / COA / SDS

Catalog #	Availability	Size / Price	Qty
Qk039-0050
QK039-0250

Recombinant Human FGF-9, Animal-Free Protein Bioactivity

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Product Details

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Summary Product Datasheets Carrier Free Data Images Reconstitution Calculator Background Related Research Areas

Recombinant Human FGF-9, Animal-Free Protein Summary

Product Specifications

Endotoxin Level

<0.10 EU per 1 μg of the protein by the LAL method.

Activity

No significant difference between EC₅₀ of reference and test lots

Source

E. coli-derived human FGF-9 protein

Accession #

P31371.3

Predicted Molecular Mass

23 kDa

SDS-PAGE

Monomeric FGF-9 protein only

Product Datasheets

QK039

Product Datasheet

COA

SDS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Qk039

Formulation	Lyophilized from HEPES/NaCl
Reconstitution	Resuspend in water at >100 µg/ml, prepare single use aliquots, add carrier protein if desired.
Shipping	The product is shipped lyophilized at ambient temperture, on ice blocks or dry ice. Shipping at ambient temperture does not affect the bioactivity or stability of the protein. Upon reciept, store immediately at the conditions stated below.
Stability & Storage:	Store lyophilized protein between -20 and -80 °C until the date of expiry. Avoid freeze-thaw cycles.

Scientific Data

Bioactivity

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FGF-9 activity is determined using the Promega serum response element luciferase reporter assay (*) in transfected HEK293T cells. Cells are treated in triplicate with a serial dilution of FGF-9 for 3 hours. Firefly luciferase activity is measured and normalized to the control Renilla luciferase activity. EC₅₀ = 5.7 ng/ml (0.25 nM).*Promega pGL4.33[luc2P/SRE/Hygro] #E1340

SDS-PAGE

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FGF-9 protein migrates as a single band at 23 kDa in non-reducing (NR) conditions and upon reduction (R). No contaminating protein bands are visible. Purified recombinant protein (3 µg) was resolved using 15% w/v SDS-PAGE in reduced (+ beta -mercaptothanol, R) and non-reduced (NR) conditions and stained with Coomassie Brilliant Blue R250.

Reconstitution Calculator

Background: FGF-9

Fibroblast growth factor 9 (FGF-9), also known as HBGF9 and GAF, is a member of the FGF family of secreted glycoproteins involved in mammalian skeleton morphogenesis and growth (1). The FGF family is characterized by a core heparin-binding FGF domain of approximately 120 amino acids (aa) that exhibits a beta -trefoil structure (2). Mature mouse FGF-9 shares 99% and 100% aa sequence identity with human and rat FGF-9, respectively. FGF-9, along with FGF-16 and -20, form a FGF subfamily that shares 65-71% aa sequence identity, binds FGFR3(IIIb), and are efficiently secreted despite having an uncleavable, bipartite signal sequence (2-4). In addition to FGFR3(IIIb), FGF-9 binding to the IIIc splice forms of FGFR-1, -2 and -3 have been reported (1,4,6). In the mouse embryo, the location and timing of FGF-9 expression affects development of the skeleton, cerebellum, lungs, heart, vasculature, digestive tract, and testes (2, 6-11). Deletion of mouse FGF-9 is lethal at birth due to lung hypoplasia, and causes rhizomelia, or shortening of the proximal skeleton (2,10,11). Additionally, a mutation in mouse FGF-9 is responsible for Elbow knee synostosis (Eks), which causes joint fusions in the elbow and knee (6). In humans, FGF9 mutations that lower receptor binding can result multiple synostoses syndrome (SYNS) (7). Altered FGF-9 expression or function is reported in human colon, endometrial, and ovarian cancers, correlating with progression, invasiveness, and survival (12-15).

References

Mohammadi, M. et al. (2005) Cytokine Growth Factor Rev. 16:107.
Itoh, N. and D.M. Ornitz (2008) Dev. Dyn. 237:18.
Miyamoto, M. et al. (1993) Mol. Cell. Biol. 13:4251.
Santos-Ocampo, S. et al. (1996) J. Biol. Chem. 271:1726.
Plotnikov, A.N. et al. (2001) J. Biol. Chem. 276:4322.
Harada, M. et al. (2009) Nat. Genet. 41:289.
Wu, X.L. et al. (2009) Am. J. Hum. Genet. 85:53.
Colvin, J.S. et al. (1999) Dev. Dyn. 216:72.
Lin, Y. et al. (2009) Dev. Biol. 329:44.
Hung, I.H. et al. (2007) Dev. Biol. 307:300.
Colvin, J.S. et al. (2001) Dev. Dyn 128:2095.
Krejci, P. et al. (2009) Hum. Mutat. 30:1245.
Leushacke, M. et al. (2011) PLoS ONE 6:e23381.
Hendrix, N.D. et al. (2006) Cancer Res. 66:1354.
Abdel-Rahman, W.M. et al. (2008) Hum. Mutat. 29:390.

Long Name

Fibroblast Growth Factor 9

Entrez Gene IDs

2254 (Human); 14180 (Mouse)

Alternate Names

FGF9; FGF-9; fibroblast growth factor 9 (glia-activating factor); Fibroblast growth factor 9; GAF; glia-activating factor; HBFG-9; HBGF-9; Heparin-binding growth factor 9; MGC119914; MGC119915; SYNS3

Product Specific Notices

The above product was manufactured, tested and released by R&D System's contract manufacturer, Qkine Ltd, at 1 Murdoch House, Cambridge, UK, CB5 8HW. The product is for research use only and not for the diagnostic or theraputic use.