Recombinant Human Endostatin Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human Endostatin Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit the FGF basic-dependent proliferation of HUVEC human umbilical vein endothelial cells. Dhanabal, M. et al. (1999) Biochem. Biophys. Res. Commun. 258:345. The ED50 for this effect is 0.4-2 μg/mL in the presence of 20 μg/mL of Goat Anti-Human Endostatin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1098).
Source
E. coli-derived human Endostatin protein
His1154-Ser1335, with an N-terminal Met and 8-His tag
Accession #
N-terminal Sequence
Met-His tag
Structure / Form
Monomer
Protein/Peptide Type
Recombinant Proteins
Gene
COL18A1
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
21.6 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
21 kDa, reducing conditions

Packaging, Storage & Formulations

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.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 200 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 Human Endostatin Protein, CF

  • antiangiogenic agent
  • COL18A1
  • collagen alpha-1(XVIII) chain
  • collagen, type XVIII, alpha 1
  • Endostatin
  • FLJ27325
  • FLJ34914
  • human type XVIII collagen10endostatin
  • KNO
  • KNO1MGC74745
  • Knobloch syndrome, type 1
  • KS
  • multi-functional protein MFP

Background

Endostatin, an endogenous non‑glycosylated inhibitor of endothelial cell proliferation and angiogenesis, is an approximately 181 amino acid (aa), 20 kDa proteolytic fragment of the C‑terminal non‑collagenous domain of type XVIII collagen (1, 2). It is produced and/or trimmed by metalloproteinases such as MMP‑2 and MMP‑9, and cathepsins S, B and L (3, 4). The N‑terminal ~27 aa of Endostatin appear to contain the majority of its activity (4, 5). This region contains three zinc binding sites that are thought to be critical for its anti‑endothelial and anti‑tumor effects, as well as multiple cleavage sites that, when used, can modify its activity (4, 5). Human Endostatin shares 84‑87% aa sequence identity with mouse, rat, bovine and equine Endostatin. Endostatin inhibits endothelial cell growth by inducing cell cycle arrest in G1 phase and initiating apoptosis (1, 2). It is also thought to down‑regulate angiogenesis by blocking VEGF‑induced endothelial cell migration (6, 7). It alters the effect of FGF basic on adhesion and cell motility (8). Endostatin can interact with Transglutaminase 2, heparin, and integrins alpha 5 beta 1 and alpha v beta 3, all of which may be secreted by, or expressed on, endothelial cells, and can influence adhesion or migration (9, 10). Endostatin may also be involved with down‑regulation of angiogenesis after establishment of placental circulation in the pregnant uterus (11). Over‑expression in keratinocytes causes delay in healing of excisional wounds, while exogenous systemic Endostatin promotes endothelial and smooth muscle nitric oxide production and decreases blood pressure (12, 13). Since tumor growth and metastasis relies on angiogenesis to provide blood supply, Endostatin is inhibitory for a wide variety of primary and metastatic tumors (5‑8).

  1. Dhanabal, M. et al. (1999) Biochem. Biophys. Res. Commun. 10:345.
  2. O’Reilly, M.S. et al. (1997) Cell 88:277.
  3. Nilsson, U.W. et al. (2006) Cancer Res. 66:4789.
  4. Veillard, F. et al. (2011) J. Biol. Chem. 286:37158.
  5. Folkman, J. (2006) Exp. Cell Res. 312:594.
  6. Yamaguchi, N. et al. (2001) EMBO J. 18:4414.
  7. Ling, Y. et al. (2007) Biochem. Biophys. Res. Commun. 361:79.
  8. Dixelius, J. et al. (2002) Cancer Res. 62:1944.
  9. Faye, C. et al. (2010) Biochem. J. 427:467.
  10. Rehn, M. et al. (2001) Proc. Natl. Acad. Sci. USA 98:1024.
  11. Pollheimer, J. et al. (2011) Endocrinol. 152:4431.
  12. Seppinen, L. et al. (2008) Matrix Biol. 27:535.
  13. Sunshine, S.B. et al. (2012) Proc. Natl. Acad. Sci. USA 109:11306.

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Bioinformatics

Gene Symbol COL18A1
Uniprot