Recombinant Cynomolgus Monkey Mer Fc Chimera Protein, CF

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2 μg/lane of Recombinant Cynomolgus Monkey Mer Fc Chimera Protein (Catalog # 10576-MR) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...read more

Product Details

Summary
Reactivity Pm-CmSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Cynomolgus Monkey Mer Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Cynomolgus Monkey Mer Fc Chimera (Catalog # 10576-MR) is immobilized at 2 μg/mL, 100 μL/well, Recombinant Human Protein S/PROS1  (Catalog # 9489-PS) binds with an ED50 of 2-10 μg/mL
Source
Chinese Hamster Ovary cell line, CHO-derived cynomolgus monkey Mer protein
Cynomolgus Monkey Mer
(Ala23-Ala501)
Accession # XP_005575320.1
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminus C-terminus
Accession #
N-terminal Sequence
Ala23
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
118-140 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 Cynomolgus Monkey Mer Fc Chimera 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 cynomolgus Mer consists of 484 amino acid (aa) extracellular domain (ECD), a 20 aa transmembrane segment, and a 472 aa cytoplasmic domain. Within the ECD, cynomolgus Mer shares 95% and 99% sequence identity with human and rhesus monkey, respectively. Similar to Axl and Tyro3, the ECD of Mer contains two Ig-like motifs and two fibronectin type III motifs. Mer is not expressed in normal B- and T-cells but is expressed in neoplastic B- and T-cell lines (1-2).  It also shows 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). Binding of Gas6 lead to cell proliferation, migration or the prevention of apoptosis. 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 promotes 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.

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