Recombinant Mouse CD300g/Nepmucin Fc Chimera Protein, CF

Measured by its ability to inhibit anti-CD3 antibody induced IL-2 secretion by human T cells. The ED50 for this effect is 0.40-4.0 μg/mL.

2 μg/lane of Recombinant Mouse CD300g/Nepmucin Fc Chimera (Catalog # 10801-NE) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 88-100 kDa and 176-200 kDa, respectively.

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

Recombinant Mouse CD300g/Nepmucin Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its ability to inhibit anti-CD3 antibody induced IL-2 or IFN-gamma secretion by human T cells. The ED₅₀ for this effect is 0.40-4.00 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse CD300g/Nepmucin protein
  

  Mouse CD300g/Nepmucin (Leu19-Ile284) Accession # NP_001154183.1	IEGRMDP	Mouse IgG2a (Glu98-Lys330)
  N-terminus		C-terminus

• Accession #: NP_001154183.1
• N-terminal Sequence: Leu19
• 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: 55 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: 88-100 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.
• 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 CD300g/Nepmucin Fc Chimera Protein, CF

• CD300 antigen like family member G
• CD300 antigen-like family member G
• CD300 molecule like family member g
• CD300 molecule-like family member g
• CD300g antigen
• CD300g
• CD300LG
• CLM9
• CLM-9
• CLM9Trem4
• CMRF35-like molecule 9
• Nepmucin
• TREM4
• TREM-4
• Triggering receptor expressed on myeloid cells 4

Background

Nepmucin, also known as CMRF35-like molecule 9 (CLM-9), TREM-4 and CD300g, is a 75-95 kDa type I transmembrane O-glycosylated member of the CD300 family of molecules. Nepmucin (mucin not expressed in Peyer's Patches) is expressed on capillary endothelium and its expression appears to be influenced by factors that are locally produced in tissues (1, 2). Nepmucin contains a single V-type immunoglobulin domain and a mucin-like domain (3). Mature human Nepmucin is composed of 313 amino acid (aa), containing 186 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 106 aa cytoplasmic region. Within the ECD, mouse nepmucin shares 53% aa identity with human Nepmucin. Nepmucin plays a critical role in promoting lymphocyte transendothelial migration of high endothelial veins and mediates lymphocyte adhesion with endothelial cells by its Ig domain, which is independent of LFA-1 or VLA-4 adhesion pathway (3). Glycosylated Nepmucin with MECA-79 epitope associate with L-selectin to mediate L-selectin-dependent lymphocyte rolling by its mucin-like domain (4). Expression of Nepmucin is down-regulated in tumors and tumor-draining lymph nodes, indicating that the expression of Nepmucin is negatively regulated by locally produced signals under these circumstances (2). Nepmucin induction can significantly improve the killing activity of CIK cells (5).

1. Jin, S. et al. (2008) FEBS Lett. 582:3018.
2. Umemoto, E. et al. (2013) PloS One. 8:e83681.
3. Umemoto, E. et al. (2006) J. Exp. Med. 203:1603.
4. Takatsu, H, et al. (2006) Biochem. Biophys. Res. Commun. 348:183.
5. Wang, Q. et al. (2017) Cent. Eur. J. Immunol. 42:117.

Bioinformatics

• Uniprot:
  • NP_001154183.1()