Recombinant Mouse PDGFRL Fc Chimera Protein, CF

Recombinant Mouse PDGFRL Fc Chimera (Catalog #9739‑PR) inhibits HCT‑116 human Colorectal carcinoma proliferation. The ED50for this effect is 1‑6 μg/mL.

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

Recombinant Mouse PDGFRL Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its ability to inhibit proliferation of HCT-116 human colorectal carcinoma cells. The ED₅₀ for this effect is 1-6 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived mouse PDGFRL protein
  

  Mouse PDGFRL (Gln22-Ser375) Accession # Q6PE55	IEGRMDP	Mouse IgG2a (Glu98-Lys330)
  N-terminus		C-terminus

• Accession #: Q6PE55
• N-terminal Sequence: No results obtained. Gln22 inferred from enzymatic pyroglutamate treatment revealing His23
• Structure / Form: Disulfide-linked homodimer
• 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: 67 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: 65-82 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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 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 PDGFRL Fc Chimera Protein, CF

• PDGFRL
• PDGFR-Like Protein
• PDGRL
• platelet-derived growth factor receptor-like protein
• platelet-derived growth factor receptor-like
• platelet-derived growth factor-beta-like tumor suppressor
• PRLTS
• PRLTSPDGF receptor beta-like tumor suppressor

Background

Platelet-derived growth factor receptor-like protein (PDGFRL) is a 67 kDa glycoprotein protein consisting of two Ig-like C2-type domains. By sequence similarity, mouse PDGFRL is 90% similar to the human version and 95% similar to that of the rat. It is a secreted protein related to the class III subfamily of receptor tyrosine kinases (RTK), the platelet-derived growth factor receptors (1-5). The high frequency of loss of heterozygosity (LOH) near the gene of PDGFRL indicated in several studies that PDGFRL can be a tumor suppressor gene (TSG) in breast cancer (6-9), colorectal cancer, prostate cancer (10), non-small cell lung cancers (11) and hepatocellular carcinoma (12). A variant of PDGFRL is found to play a role in the development of Behçet disease, a complex immunoregulatory disease (13). The autoimmune role of PDGFRL is also supported by its up-regulation in a mouse model for Rheumatoid Arthritis (14). Another study also showed that PDGFRL may play a role in chondrocyte proliferation and differentiation (15).

1. Guo, F-J. et al. (2010). World J Gastroenterol. 16:1465.
2. Andrae, J. et al. (2008) Genes Dev. 22:1276.
3. Heldin, C-H. and B. Westermark (1999) Physiol. Rev. 79:1283.
4. Claesson-Welsh, L. et al. (1989) Proc. Natl. Acad. Sci. USA 86:4917.
5. Matsui, T. et al. (1989) Science 243:800.
6. Seitz, S. et al. (2006). Genes Chromosomes Cancer 45:612.
7. Yaremko, M.L. et al. (1996). Genes, Chromosome Cancer 16:189.
8. Seitz, S. et al. (2000). Eur J Cancer. 36:1507.
9. Rennstam, K. et al. (2003). Cancer Res. 63:8861.
10. Komiya, A. et al. (1997). Jpn J Cancer Res. 88:389.
11. Lerebours, F. et al. (1999). Int J Cancer. 81:854.
12. Kahng, Y.S. et al. (2003) J Gastroenterol Hepatol. 18:430.
13. Hou, S. et al. (2013). Hum Mutat. 34:74.
14. Fujikado N. et al. (2006). Arthritis Res.& Ther. 8:R100.
15. Kawata, K. et al. (2017) J Cell Biochemistry. 118:4033.

Bioinformatics

• Uniprot:
  • Q6PE55()