Recombinant Mouse Mer Fc (HEK293-expressed) Protein, CF

Measured by its binding ability in a functional ELISA. When Recombinant Mouse Mer Fc Chimera (HEK293-expressed) (Catalog # 11314-MR) is immobilized at 2.00 µg/mL (100 µL/well), Recombinant Mouse Gas6 (Full Length) Protein (8310-GS) binds with an ED50 of 0.400 -3.60 µg/mL

2 μg/lane of Recombinant Mouse Mer Fc (HEK293-expressed) Protein (Catalog # 11314-MR) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 114-131 kDa and 228-262 kDa, respectively.

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

Recombinant Mouse Mer Fc (HEK293-expressed) Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Mouse Mer Fc Chimera (HEK293-expressed) (Catalog # 11314-MR) is immobilized at 2.00 µg/mL (100 µL/well), Recombinant Mouse Gas6 (Full Length) Protein (Catalog # 8310-GS) binds with an ED₅₀ of 0.400-3.60 µg/mL
• Source: Human embryonic kidney cell, HEK293-derived mouse Mer protein
  

  Mouse Mer (Glu23-Phe498) Accession # Q60805.1	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: Q60805.1
• N-terminal Sequence: Glu23
• 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: 79 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: 114-131 kDa, under 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 with Trehalose.
• 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 Mer Fc (HEK293-expressed) Protein, CF

• c-Eyk
• c-mer proto-oncogene tyrosine kinase
• C-mer
• EC 2.7.10
• EC 2.7.10.1
• MER receptor tyrosine kinase
• Mer
• MerTK
• MGC133349
• Receptor tyrosine kinase MerTK
• RP38Proto-oncogene c-Mer
• STK kinase
• tyrosine-protein kinase Mer

Background

Tyrosine-protein Kinase Mer, also known as c-Mer and MerTK, is a member of the receptor tyrosine kinase subfamily TAM (Tyro3, Axl, and Mer). Mature mouse Mer consists of 478 aa extracellular domain, 21 aa transmembrane domain, and 475 aa cytoplasmic domain. Within the extracellular domain, mouse Mer shares 77.1% and 90.4% homology with human and rat Mer, respectively. Similar to Axl and Tyro3, the extracelluar domain of Mer contains two Ig-like motifs and two fibronectin type III motifs. Mer is not expressed in normal B- and T-cells but expressed in neoplastic B- and T-cell lines (1-2).  It is also show higher expression in immunosuppressive M2‑like macrophages (3).  Mer is known to bind Gas6, Protein S, Tubby, Tubby-like protein 1 (Tulp1), and Galectin-3 (4-7). Upon binding ligands via the Ig-like motif, Mer is dimerized to trans-autophosphorylate the kinase domain to induce downstream signaling. It has been shown that Mer signaling in macrophages induces M2 polarization, which promote tumor growth, metastasis and evasion of anti-tumor immunity in tumor microenviroment (8). Inhibition of Mer, especially on leukocytes and macrophages, is an effective anti-cancer therapy (9).

1. Graham, D.K. et al. (1994) Cell Growth Differ. 5:647.
2. Graham, D.K. et al. (2006) Clin. Cancer Res. 12:2662.
3. Shibata, T. et al. (2014) J. Immunol. 192:3569.
4. Nagata, K. et al. (1996) J. Biol. Chem. 271:30022.
5. Uehara, H. et al. (2008) J. Immunol. 180:2522.
6. Caberoy, N.B. et al. (2010) EMBO J. 29:3898.
7. Caberoy, N.B. et al. (2012) J. Cell Physiol. 227:401.
8. Kim, S.Y. et al. (2016) Sci. Rep. 6:29673.
9. Cummings, C.T. et al. (2013) Clin. Cancer Res. 19:5275.

Bioinformatics

• Uniprot:
  • Q60805.1()