Recombinant Cynomolgus LAIR1 Fc Chimera Protein, CF

When Bovine Collagen I is coated at 10 μg/mL, 100 μL/well, Recombinant Cynomolgus LAIR1 Fc Chimera (Catalog # 10226-LR) binds with an ED50 of 1‑6 ng/mL.

2 μg/lane of Recombinant Cynomolgus LAIR1 Fc Chimera was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 58-64 kDa and 110-130 kDa, respectively.

• Reactivity: Pm-Cm
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Cynomolgus LAIR1 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Bovine Collagen I is coated at 10 µg/mL, 100 μL/well, Recombinant Cynomolgus Monkey LAIR1 Fc Chimera binds with an ED₅₀ of 1‑6 ng/mL.
• Source: Human embryonic kidney cell, HEK293-derived cynomolgus monkey LAIR1 protein
  

  Cynomolgus Monkey LAIR1 (Gln22-His163) Accession # XP_015297320.1	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: XP_015297320.1
• N-terminal Sequence: Gln22, deduced from deblocked sequence at Glu23
• 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: 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: 58-64 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 LAIR1 Fc Chimera Protein, CF

• CD305 antigen
• CD305
• CD305leukocyte-associated Ig-like receptor 1
• HLAIR1
• LAIR1
• LAIR-1
• leukocyte-associated immunoglobulin-like receptor 1

Background

Leukocyte-associated Ig-like receptor-1 (LAIR1) is an inhibitory receptor of the Ig superfamily that is structurally related to inhibitory members of KIR and ILT/CD85 families (1-3). It is expressed on immune cells, including NK cells, T cells, B cells, monocytes, immature neutrophils, dendritic cells and most thymocytes (2-4). Cynomolgus LAIR-1 cDNA encodes a 296 amino acid (aa) polypeptide precursor. Based on the similarity with human LAIR1, it is likely to be a type I transmembrane (TM) protein containing a 21 aa signal sequence, a 144 aa extracellular domain (ECD), a 21 aa TM domain and a 110 aa cytoplasmic domain. Within ECD cynomolgus LAIR-1 shares 82% aa identity with human LAIR-1. LAIR-1 ECD includes one C2-type Ig-like domain. Tyrosine phosphorylation of two cytoplasmic ITIM motifs results in recruitment of phosphatases and down-regulation of signaling through activating receptors (2, 3, 5). Crosslinking of LAIR1 inhibits processes such as B cell receptor-mediated activation, NK cell and T cell cytotoxicity and basophil degranulation (1-3). LAIR1 shows high-affinity binding of collagens that results in inhibition of degranulation in a basophilic leukemia cell line (6).

1. Meyaard, L.(2003) J. Biol. Regul. Homeost. Agents 17:330.
2. Meyaard, L. et al. (1997) Immunity 7:283.
3. Lebbink, R.J. et al. (2004) J. Immunol. 172:5535.
4. Verbrugge, A. et al. (2006) J. Leukoc. Biol. 79:828.
5. Verbrugge, A. et al. (2003) Int. Immunol. 15:1349.
6. Lebbink, R.J. et al. (2006) J. Exp. Med. 203:1419.

Bioinformatics

• Uniprot:
  • XP_015297320.1()