Recombinant Human OCIL/CLEC2d Fc Chimera Protein, CF

When Recombinant Human CD161 Fc Chimera Protein (7448-CD) is immobilized at 10 μg/mL (100 μL/well), the concentration of Recombinant Human OCIL/CLEC2d Fc Chimera (Catalog # 10506-OC) that produces 50% of the optimal binding response is approximately 1.5-9 μg/mL.

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

Recombinant Human OCIL/CLEC2d Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human CD161 Fc Chimera Protein (Catalog # 7448-CD) is immobilized at 10 μg/mL (100 μL/well), the concentration of Recombinant Human OCIL/CLEC2d Fc Chimera that produces 50% of the optimal binding response is approximately 1.5-9 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human OCIL/CLEC2d protein
  

  MD	Human IgG1 (Pro100-Lys330)	IEGR	Human OCIL/CLEC2d (Ala58-Val191) Accession # Q9UHP7.1
  N-terminus			C-terminus

• Accession #: Q9UHP7.1
• N-terminal Sequence:

  Met

• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >85%, 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: 42 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: 50-60 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: >85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 250 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 OCIL/CLEC2d Fc Chimera Protein, CF

• CLAXLLT-1
• CLEC2D
• C-type lectin domain family 2 member D
• C-type lectin domain family 2, member D
• C-type lectin related f
• Lectin-like NK cell receptor
• Lectin-like transcript 1
• LLT1
• LLT1Osteoclast inhibitory lectin
• OCIL
• OCILmember D

Background

C-type lectin domain family 2 member D (CLEC2D), also known as lectin-like NK cell receptor,as lectin-like transcript 1 (LLT-1) and osteoclast inhibitory lectin (OCIL), is a member of the C-type lectin like (CTL) superfamily of natural killer cell receptors (1, 2). Human OCIL/CLEC2D is highly glycosylated and consists of a cytoplasmic domain, a type II transmembrane domain, a stalk region and a C-type lectin-like (CTL) in the extracellular domain (ECD). Within the ECD, mature human OCIL/CLEC2D shares 45% and 43% amino acid sequence identity with mouse and rat OCIL/CLEC2D, respectively. At least six different isoforms of OCIL/CLEC2D, resulting from alternatively spicing, have been reported (1, 2). OCIL/ CLEC2D plays a role in immunotherapy, inflammation and tissue injury and is expressed mainly on activated lymphocytes (NK cells, T cells, B cells) and antigen presenting cells (1-6).OCIL/CLEC2D forms a disulfide linked homodimer that acts as the only ligand for NKRP1A (CD161) and inhibits NK cell-mediated cytotoxicity and IFN-gamma secretion (1,6,7). OCIL/CLEC2D preferentially binds high molecular weight sulfated glycosaminoglycans and blocks osteoclast differentiation (1, 4).

1. Marrufo, A. et al. (2018) Am. J. Cancer Res. 8:1050.
2. Germain, C. et al. (2010) J. Biol. Chem. 285:36207.
3. Mathew, S. et al. (2016) Oncotarget 7:68650.
4. Lai, J. et al. (2020) Immunity 52:123.
5. Varaden, D. et al. (2019) Eur. J. Obstet. Gynecol. Reprod. Biol. X. 3:100039.
6. Sun, Y. et al. (2019) J. Cancer Metastasis Treat. 5:80.
7. Skalova, T. et al. (2015) Acta. Crystallogr. D. Biol. Crystallogr. 71:578.

Bioinformatics

• Uniprot:
  • Q9UHP7.1()