Recombinant Human Fibulin 5 Protein, CF

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R&D Systems Recombinant Proteins and Enzymes
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Recombinant Human Fibulin 5 Protein, CF Summary

Product Specifications

>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by the ability of the immobilized protein to enhance the adhesion of HUVEC human umbilical vein endothelial cells. The ED50 for this effect is 15-90 ng/mL.
Human embryonic kidney cell, HEK293-derived human Fibulin 5/DANCE protein
Gln24-Phe448, with an N-terminal HA tag
Accession #
N-terminal Sequence
Predicted Molecular Mass
49 kDa
60-72 kDa, reducing conditions

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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.


Formulation Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl, EDTA and CHAPS with Trehalose.
Reconstitution Reconstitute at 500 μg/mL in water.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Background: Fibulin 5/DANCE

Fibulin 5, also known as DANCE and EVEC, is a secreted 55 kDa matricellular glycoprotein that plays an important role in elastic fiber network assembly and angiogenesis (1). Mature human Fibulin 5 contains an N-terminal EGF-like domain with an RGD motif, a 44 amino acid (aa) spacer region, five more tandem EGF-like domains, and a 115 aa Fibulin-like C-terminal region (2, 3). Mature human Fibulin 5 shares 95% aa sequence identity with mouse and rat Fibulin 5. Fibulin 5 is expressed by smooth muscle cells and endothelial cells of the developing vasculature as well as by migrating neural crest cells and lung interstitial fibroblasts (2-4). It is downregulated in the adult vasculature but is re-expressed at aortic branching points, in the uterus, and at sites of mechanical or atherosclerotic injury (2, 3, 5). The RGD motif of Fibulin 5 binds to several cell surface Integrins including alpha V beta 3, alpha V beta 5, alpha 9 beta 1, alpha 4 beta 1, and alpha 5 beta 1 (2, 6, 7). The calcium-dependent binding of Fibulin 5 to elastic fibers serves to anchor cells to the extracellular matrix (8). Fibulin 5 promotes elastic fiber assembly and maturation by organizing Tropoelastin, LTBP-2,
LTBP-4, and the crosslinking lysyl oxidase-like enzymes LOXL1,2, and 4 along Fibrillin microfibrils (6, 9-12). In aged mice with decreased tissue elasticity, proteolytic removal of the N-terminal EGF-like domain prevents Fibulin 5 from interacting with Fibrillin-1 microfibrils (10). Fibulin 5 functions as an angiogenesis inhibitor by inhibiting vascular smooth muscle proliferation and migration and by limiting vascular sprouting (5, 13). Depending on the context, Fibulin 5 can function either as a tumor suppressor or enhancer of tumor cell invasiveness (14, 16). Defects in Fibulin 5 expression or function can result in a loss of connective tissue integrity, cardiac elasticity, and ability to remodel the vasculature after injury (8, 5, 15).

  1. Papke, C.L. and H. Yanagisawa (2014) Matrix Biol. 37:142.
  2. Nakamura, T. et al. (1999) J. Biol. Chem. 274:22476.
  3. Kowal, R.C. et al. (1999) Circ. Res. 84:1166.
  4. Kuang, P.-P. et al. (2003) Am. J. Physiol. Lung Cell. Mol. Physiol. 285:L1147.
  5. Spencer, J.A. et al. (2005) Proc. Natl. Acad. Sci. USA 102:2946.
  6. Nakamura, T. et al. (2002) Nature 415:171.
  7. Lomas, A.C. et al. (2007) Biochem. J. 405:417.
  8. Yanagisawa, H. et al. (2002) Nature 415:168.
  9. Wachi, H. et al. (2008) J. Biochem. 143:633.
  10. Hirai, M. et al. (2007) J. Cell Biol. 176:1061.
  11. Hirai, M. et al. (2007) EMBO J. 26:3283.
  12. Noda, K. et al. (2013) Proc. Natl. Acad. Sci. USA 110:2852.
  13. Sullivan, K.M. et al. (2007) Lab. Invest. 87:818.
  14. Lee, Y.-H. et al. (2008) Carcinogenesis 29:2243.
  15. Loeys, B. et al. (2002) Hum. Mol. Genet. 11:2113.
  16. Yue, W. et al. (2009) Cancer Res. 69:6339.
Entrez Gene IDs
10516 (Human)
Alternate Names
ARMD3fibulin-5; DANCE; DANCEFIBL-5; Developmental arteries and neural crest EGF-like protein; EVEC; FBLN5; Fibulin 5; UP50; UP50FLJ90059; Urine p50 protein

Citation for Recombinant Human Fibulin 5 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

1 Citation: Showing 1 - 1

  1. The Different Binding Properties of Cultured Human Corneal Endothelial Cell Subpopulations to Descemet's Membrane Components
    Invest Ophthalmol Vis Sci, 2016;57(11):4599-605.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay


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