Recombinant Mouse Endorepellin His-tag Protein, CF

Immobilized Recombinant Mouse Endorepellin supports theadhesion of SVEC4‑10 mouse vascular endothelial cells. The ED50 for thiseffect is 0.75‑4.5 μg/mL.

2 μg/lane of Recombinant Mouse Endorepellin/Perlecan was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 85-95 kDa.

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse Endorepellin His-tag Protein, CF Summary

• Details of Functionality: Measured by the ability of the immobilized protein to support the adhesion of SVEC4‑10 mouse vascular endothelial cells. The ED₅₀ for this effect is 0.75-4.5 μg/mL.
  
• Source: Chinese Hamster Ovary cell line, CHO-derived mouse Endorepellin/Perlecan protein
  Glu3683-Ser4383, with a C-terminal 6-His tag
• Accession #: NP_032331.2
• N-terminal Sequence: Glu3683
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, 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: 75.8 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: 85-95 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage:
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 300 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Mouse Endorepellin His-tag Protein, CF

• basement membrane-specific heparan sulfate proteoglycan core protein
• endorepellin (domain V region)
• heparan sulfate proteoglycan 2
• Heparan Sulfate Proteoglycan
• HSPG
• perlecan proteoglycan
• perlecan
• PLCSchwartz-Jampel syndrome 1 (chondrodystrophic myotonia)
• PRCAN
• SJA
• SJS
• SJS1

Background

Endorepellin is an 80 kDa glycoprotein derived from the C-terminal end of the heparan sulfate proteoglycan Perlecan. Human Perlecan is an approximately 850 kDa basement membrane heparan sulfate proteoglycan containing multiple LDLR, EGF-like, Laminin-like, and immunoglobulin-like domains. Mouse Perlecan lacks several of the EGF, Laminin-like and Ig-like domains found in the human protein (1-3). Mouse Endorepellin, also termed Domain V (DV) of Perlecan, consists of three Laminin G domains separated by a single EGF-like domain. Mouse Endorepellin shares 89% amino acid sequence identity with human Endorepellin. Endorepellin has been shown to broadly inhibit angiogenesis, including endothelial cell migration, collagen-induced capillary morphogenesis, and blood vessel growth (4). Endostatin, an inhibitor of Endorepellin, has been shown to bind Endorepellin directly and block its anti-angiogenic activity (4). Endorepellin can be further processed into a 26 kDa fragment, termed LG3, containing the third Laminin G-like domain of Endorepellin. LG3 possesses anti-angiogenic activity of its own and its release is mediated by either Cathepsin L or BMP-1/Tolloid family cleavage (4-7). Endorepellin binds to Integrin alpha 2/ beta 1, preventing the integrin-dependent adhesion of vascular endothelial cells (EC) to fibronectin and collagen I (7, 8). Additionally, Endorepellin binds to VEGF R1 and VEGF R2 on EC (10). Its binding to VEGF R2 and Integrin alpha 2/beta 1 on EC induces the association and down‑regulation of both proteins, resulting in a reduction in EC migration and overall antiangiogenic activity (4, 7-10). Endorepellin has been shown to disrupt tumor vasculature and inhibit tumor growth, invasion and angiogenesis (8, 11), and it has recently been proposed as a potential stroke therapy by helping with brain repair following injury (12).

1. Whitelock, J.M. et al. (2008) Biochemistry 47:11174.
2. Murdoch, A.D. et al. (1992) J. Biol. Chem. 267:8544.
3. Noonan, D.M. et al. (1991) J. Biol. Chem. 266:22939.
4. Mongiat, M. et al. (2003) J. Biol. Chem. 278:4238.
5. Cailhier, J.-F. et al. (2008) J. Biol. Chem. 283:27220.
6. Gonzalez, E.M. et al. (2005) J. Biol. Chem. 280:7080.
7. Bix, G. et al. (2004) J. Cell Biol. 166:97.
8. Woodall, B.P. et al. (2008) J. Biol. Chem. 283:2335.
9. Goyal, A. et al. (2011) J. Biol. Chem. 286:25947.
10. Nystrom, A. et al. (2009) Blood 114:4897.
11. Bix, G. et al. (2006) J. Natl. Cancer Inst. 98:1634.
12. Bix G. (2013) ACS Chem Neurosci. 4:370.

Bioinformatics

• Uniprot:
  • NP_032331.2()