Recombinant Mouse Endostatin Protein, CF Summary
| Details of Functionality |
Measured by its ability to inhibit the FGF basic/FGF2-dependent proliferation of HUVEC human umbilical vein endothelial cells. Dhanabal, M. et al. (1999) Biochem. Biophys. Res. Commun. 258:345. The ED 50 for this effect is 0.3-1.5 μg/mL in the presence of 20 μg/mL of Goat Anti-Mouse Endostatin Antigen Affinity-purified Polyclonal Antibody (Catalog # AF570). |
| Source |
Mouse myeloma cell line, NS0-derived mouse Endostatin protein His1591-Lys1774, with an N-terminal Met, a substitution, Leu1684Val and a C-terminal 6-His tag |
| Accession # |
|
| N-terminal Sequence |
Met-His1591 |
| Protein/Peptide Type |
Recombinant Proteins |
| Gene |
Col18a1 |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining |
| Endotoxin Note |
<0.01 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
|
| Theoretical MW |
21.3 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 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 3 months, -20 to -70 degreesC 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 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 Mouse Endostatin Protein, CF
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 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). Mouse Endostatin shares 96% aa sequence identity with rat and 85-87% with human, 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, proliferation, 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).
- Dhanabal, M. et al. (1999) Biochem. Biophys. Res. Commun. 10:345.
- O’Reilly, M.S. et al. (1997) Cell 88:277.
- Nilsson, U.W. et al. (2006) Cancer Res. 66:4789.
- Veillard, F. et al. (2011) J. Biol. Chem. 286:37158.
- Folkman, J. (2006) Exp. Cell Res. 312:594.
- Yamaguchi, N. et al. (2001) EMBO J. 18:4414.
- Ling, Y. et al. (2007) Biochem. Biophys. Res. Commun. 361:79.
- Dixelius, J. et al. (2002) Cancer Res. 62:1944.
- Faye, C. et al. (2010) Biochem. J. 427:467.
- Rehn, M. et al. (2001) Proc. Natl. Acad. Sci. USA 98:1024.
- Pollheimer, J. et al. (2011) Endocrinol. 152:4431.
- Seppinen, L. et al. (2008) Matrix Biol. 27:535.
- Sunshine, S.B. et al. (2012) Proc. Natl. Acad. Sci. USA 109:11306.
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