Recombinant Human Fibulin 5 Protein, CF


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Product Details

Reactivity HuSpecies Glossary
Applications Bioactivity

Order Details

Recombinant Human Fibulin 5 Protein, CF Summary

Additional Information
Details of Functionality
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
Protein/Peptide Type
Recombinant Proteins
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


Theoretical MW
49 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
60-72 kDa, reducing conditions

Packaging, Storage & Formulations

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.
Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl, EDTA and CHAPS with Trehalose.
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in water.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Fibulin 5 Protein, CF

  • ARMD3fibulin-5
  • Developmental arteries and neural crest EGF-like protein
  • EVEC
  • FBLN5
  • Fibulin 5
  • UP50
  • UP50FLJ90059
  • Urine p50 protein


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.

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Gene Symbol FBLN5