Recombinant Mouse Siglec-15 Fc Chimera Protein, CF

Recombinant Mouse Siglec-15 Fc Chimera (Catalog # 10101-SL) inhibits IL-2 secretion by mouse T cells in the presence of Rat Anti-Mouse CD3 Monoclonal Antibody (Catalog # MAB4841). The ED50 for this effect is 1-6 μg/mL.

2 μg/lane of Recombinant Mouse Siglec-15 Fc Chimera (Catalog # 10101-SL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 57-64 kDa and 110-130 kDa, respectively.

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

Recombinant Mouse Siglec-15 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its ability to inhibit IL-2 secretion by mouse T cells in the presence of anti-CD3. The ED₅₀ for this effect is 1-6 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse Siglec-15 protein
  

  Mouse Siglec-15 (Arg24-Tyr250) Accession # NP_001094508.1	IEGRMDP	Mouse IgG2a (Glu98-Lys330)
  N-terminus		C-terminus

• Accession #: NP_001094508.1
• N-terminal Sequence: Arg24
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, 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: 52 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: 57-64 kDa

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: >90%, 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 Siglec-15 Fc Chimera Protein, CF

• CD33 antigen-like 3SIGLEC-15
• CD33 molecule-like 3
• CD33L3
• HsT1361
• sialic acid binding Ig-like lectin 15
• sialic acid-binding Ig-like lectin 15
• Siglec15
• Siglec-15

Background

Siglec-15 is a transmembrane glycoprotein in the Siglec family of sialic acid-binding immune regulatory molecules (1). Mature mouse Siglec-15 consists of a 239 amino acid (aa) extracellular domain (ECD) with two Ig-like domains, a 21 aa transmembrane segment, and a 59 aa cytoplasmic domain. Within the ECD, mouse Siglec-15 shares 85% and 92% aa sequence identity with human and rat Siglec-15, respectively. In human Siglec-15, alternative splicing generates an additional isoform that lacks the signal peptide and first Ig-like domain. Siglec-15 associates with the signaling molecules DAP12 and DAP10 (2-5). It is expressed on osteoclasts, macrophages, and dendritic cells (2-6) and binds to the sialyl-Tn antigen (2, 3, 6). This interaction induces the production of TGF-beta by tumor-associated macrophages (3). Siglec-15 function is important for osteoclast formation and TRANCE/RANK Ligand signaling in osteoclasts (4-6). Siglec-15 is broadly upregulated on human cancer cells and tumor infiltrating myeloid cells (7). Siglec-15 suppresses antigen-specific T cell responses in vitro and in vivo therefore it is considered to be an immune suppressor and potential target for normalization cancer immunotherapy (7).

1. Humphrey, M.B. and M.C. Nakamura (2016) Clin. Rev. Allergy Immunol. 51:48.
2. Angata, T. et al. (2007) Glycobiology 17:838.
3. Takamiya, R. et al. (2013) Glycobiology 23:178.
4. Kameda, Y. et al. (2013) J. Bone Miner. Res. 28:2463.
5. Stuible, M. et al. (2014) J. Biol. Chem. 289:6498.
6. Ishida-Kitagawa, N. et al. (2012) J. Biol. Chem. 287:17493.
7. Wang, J et al. (2019) Nat. med. 25:656.

Bioinformatics

• Uniprot:
  • NP_001094508.1()