Recombinant Human/Rat/Bovine FGF-10, Animal-Free Protein

Catalog #: Qk003 Datasheet / COA / SDS

Human/Rat/Bovine/Porcine

Catalog #	Availability	Size / Price	Qty
Qk003-0050
Qk003-0500

Recombinant Human/Rat/Bovine FGF-10, Animal-Free Protein Bioactivity

2 Images

Product Details

Reviews

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

Recombinant Human/Rat/Bovine FGF-10, 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 FGF-10 protein

Accession #

O15520.1

Predicted Molecular Mass

17 kDa

SDS-PAGE

Monomeric FGF-10 protein only

Product Datasheets

QK003

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.

Qk003

Formulation	Lyophilized from HEPES/NaCl/mannitol
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 temperature, on ice blocks or on dryice. Shipping at ambient temperature does not affect the bioactivity or stability ofthe protein. Upon receipt, store immediately at the conditions stated below.
Stability & Storage:	Store lyophilized protein between -20 °C and -80 °C until the date of expiry. Avoid freeze-thaw cycles.

Scientific Data

Bioactivity

View Larger

FGF-10 activity is determined using the firefly luciferase reporter assay (*) in stably transfected HEK293T cells. Cells are treated in triplicate with a serial dilution of FGF-10. Firefly luciferase activity is measured and normalized. EC₅₀ = 0.36 ng/ml (21.1 pM).*Promega pGL4.33[luc2P/SRE/Hygro] #E1340

N/A

View Larger

FGF-10 migrates as a single band at 17 kDa in non-reducing (NR) conditions and upon reduction (R). No contaminating protein bands are visible.Purified recombinant human FGF-10 protein (7 µg) was resolved using 15% w/v SDS-PAGE in reduced (+ beta -mercaptoethanol, R) and non-reduced conditions (NR) and stained with Coomassie Brilliant Blue R250.

Reconstitution Calculator

Background: FGF-10

The Fibroblast Growth Factors (FGFs) are heparin binding glycoproteins that exert a variety of biological activities toward cells of mesenchymal, neuronal, and epithelial origin. FGF-10 belongs to the subgroup of FGFs that also includes FGF-3, -7, and -22 (1). Mature human FGF-10 is an approximately 20 kDa protein that contains a serine-rich region near its N-terminus (2, 3). It shares 93% and 96% amino acid sequence identity with mouse and rat FGF-10, respectively. FGF-10 is secreted by mesenchymal cells and associates with extracellular FGF-BP (1, 4). It preferentially binds and activates epithelial cell FGF R2 (IIIb) and interacts more weakly with FGF R1 (IIIb) (5). The mitogenic and chemotactic properties of FGF-10 are critical in many tissues during embryogenesis. This includes limb bud initiation (6), palate development (7), branching morphogenesis and directional outgrowth of lung buds (8, 9), formation of the otic vesicle and chochlea (10), adipogenesis (11), and the development of prostate, mammary, lacrimal, and submandibular salivary glands (12 - 15). FGF R2 (IIIb) signaling in these responsive tissues is similarly important during embryogenesis (7, 10, 13 ‑ 15). The expression and function of FGF-10 are negatively regulated by Shh and BMP-4 in the developing lung (8, 9). Overlapping expression patterns and activities with FGF-3, -7, and -8 suggest at least a partial redundancy in FGF‑10 biology (7, 10, 14, 15). FGF-10 induced signaling through FGF R2 (IIIb) also contributes to the progression of pancreatic cancer (16).

References

Beenken, A. and M. Mohammadi (2009) Nat. Rev. Drug Discov. 8:235.
Igarashi, M. et al. (1998) J. Biol. Chem. 273:13230.
Emoto, H. et al. (1997) J. Biol. Chem. 272:23191.
Beer, H.-D. et al. (2005) Oncogene 24:5269.
Zhang, X. et al. (2006) J. Biol. Chem. 281:15694.
Min, H. et al. (1998) Genes Dev. 12:3156.
Rice, R. et al. (2004) J. Clin. Invest. 113:1692.
Bellusci, S. et al. (1997) Development 124:4867.
Weaver, M. et al. (2000) Development 127:2695.
Pirvola, U. et al. (2000) J. Neurosci. 20:6125.
Sakaue, H. et al. (2002) Genes Dev. 16:908.
Donjacour, A.A. et al. (2003) Dev. Biol. 261:39.
Mailleux, A.A. et al. (2002) Development 129:53.
Makarenkova, H.P. et al. (2000) Development 127:2563.
Jaskoll, T. et al. (2005) BMC Dev. Biol. 5:11.
Nomura, S. et al. (2008) Br. J. Cancer 99:305.

Long Name

Fibroblast Growth Factor 10

Entrez Gene IDs

2255 (Human); 14165 (Mouse); 25443 (Rat)

Alternate Names

FGF10; FGF-10; fibroblast growth factor 10; Keratinocyte growth factor 2; KGF2; KGF-2; produced by fibroblasts of urinary bladder lamina propria

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.