Recombinant Human Fibulin 1C Protein, CF

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Recombinant Human Fibulin 1C Protein, CF Summary

Product Specifications

>95%, 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 support the adhesion of HFL1 human fetal lung fibroblast cells. The ED50 for this effect is 0.7-3.5 μg/mL.
Human embryonic kidney cell, HEK293-derived human Fibulin 1 protein
Asp30-Leu683, with an N-terminal HA tag
Accession #
N-terminal Sequence
Predicted Molecular Mass
73 kDa
84-104 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 PBS.
Reconstitution Reconstitute at 250 μg/mL in PBS.
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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Reconstitution Calculator

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Background: Fibulin 1

Fibulin 1 is a 95 kDa matricellular glycoprotein component of the elastic fiber core in connective tissues (1-3). It contains 3 tandem anaphylatoxin-like domains followed by 9 tandem EGF-like domains (4). Alternative splicing of human Fibulin 1 generates additional isoforms with a deletion or substitution of the C-terminal 137 amino acids (aa) (4). The Fibulin 1c isoform carries a 117 aa substitution for this region which includes a portion of the ninth EGF-like domain and the C-terminal region. Human Fibulin 1c shares 86% aa sequence identity with mouse and rat Fibulin 1c. It self-aggregates and additionally binds to several extracellular matrix and cellular proteins including Aggrecan, Versican, Fibronectin, ECM1, NOV/CCN3, and pro-HB-EGF (5-9). Fibulin 1c enhances ADAMTS-1 mediated cleavage of Aggrecan and Versican (10, 11) and can itself be cleaved by neutrophil elastase or MMP-13 (12, 13). It functions as a bridge between Fibrinogen and Fibrin, enabling Fibrin attachment to the platelet cell surface via Integrin  alpha 2b beta 3 (14). Fibulin 1 inhibits cardiomyocyte proliferation and Fibronectin-mediated cell adhesion and can promote bone formation (11, 15, 16).

  1. Zheng, P. et al. (2015) Pharmacol. Res. 99:11.
  2. Murphy-Ullrich, J.E. and E.H. Sage (2014) Matrix Biol. 37:1.
  3. Roark, E.F. et al. (1995) J. Histochem. Cytochem. 43:401.
  4. Argraves, W.S. et al. (1990) J. Cell Biol. 111:3155.
  5. Aspberg, A. et al. (1999) J. Biol. Chem. 274:20444.
  6. Balbona, K. et al. (1992) J. Biol. Chem. 267:20120.
  7. Fujimoto, N. et al. (2005) Biochem. Biophys. Res. Commun. 333:1327.
  8. Perbal, B. et al. (1999) Proc. Natl. Acad. Sci. USA 96:869.
  9. Brooke, J.S. et al. (2002) BMC Cell Biol. 3:2.
  10. Lee, N.V. et al. (2005) J. Biol. Chem. 280:34796.
  11. Cooley, M.A. et al. (2012) Dev. Dyn. 241:303.
  12. Sasaki, T. et al. (1996) Eur. J. Biochem. 240:427.
  13. Wang, Q. et al. (2015) Oncogene 34:1006.
  14. Godyna, S. et al. (1996) Blood 88:2569.
  15. Twal, W.O. et al. (2001) J. Cell Sci. 114:4587.
  16. Cooley, M.A. et al. (2014) Bone 69:30.
Entrez Gene IDs
2192 (Human); 14114 (Mouse); 315191 (Rat)
Alternate Names
FBLN; FBLN1; FIBL1; FIBL-1; Fibulin 1; fibulin-1


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