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Recombinant Human Fibulin 5 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 9006-FB

HEK293-derived
R&D Systems, part of Bio-Techne
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9006-FB-050

Key Product Details

Source

HEK293

Accession #

Conjugate

Unconjugated

Applications

Bioactivity

Product Specifications

Source

Human embryonic kidney cell, HEK293-derived human Fibulin 5/DANCE protein
Gln24-Phe448, with an N-terminal HA tag

Purity

>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.

N-terminal Sequence Analysis

Tyr

Predicted Molecular Mass

49 kDa

SDS-PAGE

60-72 kDa, reducing conditions

Activity

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.

Formulation, Preparation and Storage

9006-FB
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.

Reconstitution Buffer Available:
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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.

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 alphaV beta3, alphaV beta5, alpha9 beta1, alpha4 beta1, and alpha5 beta1 (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).

References

  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.

Alternate Names

DANCE, EVEC, FBLN5, UP50

Entrez Gene IDs

10516 (Human)

Gene Symbol

FBLN5

UniProt

Additional Fibulin 5/DANCE Products

Product Documents for Recombinant Human Fibulin 5 Protein, CF

Certificate of Analysis

To download a Certificate of Analysis, please enter a lot number in the search box below.

Note: Certificate of Analysis not available for kit components.

Product Specific Notices for Recombinant Human Fibulin 5 Protein, CF

For research use only

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