Recombinant Human Siglec-15 His-tag Protein, CF

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Measured by its ability to inhibit anti-CD3 antibody induced IL-2 secretion by human T cells. The ED50 for this effect is 0.2‑2 μg/mL

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human Siglec-15 His-tag 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 0.2-2 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human Siglec-15 protein
Phe20-Tyr251, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Phe20
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
26 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
27-37 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
>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 Human Siglec-15 His-tag 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

Sialic acid-binding Ig-like lectin 15 (Siglec-15) is a transmembrane glycoprotein in the Siglec family of sialic acid-binding immune regulatory molecules (1). Siglecs can be divided into 2 classes: evolutionarily conserved Siglecs and CD33-related Siglecs (2). Siglec-15 belongs to the evolutionarily conserved class and is the only Siglec highly conserved throughout vertebrate evolution (3). Mature human Siglec-15 consists of an extracellular domain (ECD) with two Ig-like domains, a transmembrane segment, and a cytoplasmic domain. Within the ECD, human Siglec-15 shares 85% and 84% amino acid sequence identity with mouse and rat Siglec‑15, respectively. Alternative splicing of Siglec-15 generates an additional isoform that lacks the signal peptide and first Ig-like domain. Siglec-15 is expressed on osteoclasts, macrophages, and dendritic cells (3-7) and binds to the sialyl-Tn antigen (3, 4, 7). Siglec-15 function is important for osteoclast formation and TRANCE/RANK Ligand signaling in osteoclasts (5-7) and for the production of TGF-beta by tumor-associated macrophages (4). Additionally, Siglec-15 associates with the signaling molecules DAP12 and DAP10 through a lysine residue located in the transmembrane domain (3-6). Siglec-15 is broadly upregulated on human cancer cells and tumor infiltrating myeloid cells (8). 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 (8).
  1. Humphrey, M.B. and M.C. Nakamura (2016) Clin. Rev. Allergy Immunol. 51:48.
  2. Varki, A. and Angata, T. (2006) Glycobiology, 16:1R.
  3. Angata, T. et al. (2007) Glycobiology 17:838.
  4. Takamiya, R. et al. (2013) Glycobiology 23:178.
  5. Kameda, Y. et al. (2013) J. Bone Miner. Res. 28:2463.
  6. Stuible, M. et al. (2014) J. Biol. Chem. 289:6498.
  7. Ishida-Kitagawa, N. et al. (2012) J. Biol. Chem. 287:17493.
  8. Wang, J. et al. (2019) Nat. med. 25:656.

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