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.
Source
Human embryonic kidney cell, HEK293-derived human Fibulin 5/DANCE protein Gln24-Phe448, with an N-terminal HA tag
>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.
Applications/Dilutions
Dilutions
Bioactivity
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.
SDS-PAGE
60-72 kDa, reducing conditions
Publications
Read Publication using 9006-FB in the following applications:
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.
Buffer
Lyophilized from a 0.2 μm filtered solution in MOPS, NaCl, EDTA and CHAPS with Trehalose.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 μg/mL in water.
Notes
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
DANCE
DANCEFIBL-5
Developmental arteries and neural crest EGF-like protein
EVEC
FBLN5
Fibulin 5
UP50
UP50FLJ90059
Urine p50 protein
Background
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).
Papke, C.L. and H. Yanagisawa (2014) Matrix Biol. 37:142.
Nakamura, T. et al. (1999) J. Biol. Chem. 274:22476.
Kowal, R.C. et al. (1999) Circ. Res. 84:1166.
Kuang, P.-P. et al. (2003) Am. J. Physiol. Lung Cell. Mol. Physiol. 285:L1147.
Spencer, J.A. et al. (2005) Proc. Natl. Acad. Sci. USA 102:2946.
Nakamura, T. et al. (2002) Nature 415:171.
Lomas, A.C. et al. (2007) Biochem. J. 405:417.
Yanagisawa, H. et al. (2002) Nature 415:168.
Wachi, H. et al. (2008) J. Biochem. 143:633.
Hirai, M. et al. (2007) J. Cell Biol. 176:1061.
Hirai, M. et al. (2007) EMBO J. 26:3283.
Noda, K. et al. (2013) Proc. Natl. Acad. Sci. USA 110:2852.
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