Recombinant Mouse LAIR1 Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Mouse LAIR1 Protein, CF Summary

Details of Functionality
Measured by the ability of the immobilized protein to support the adhesion of HT‑29 human colon adenocarcinoma cells. When 5 x 104 cells/well are added to Recombinant Mouse LAIR1-coated plates (50 µg/mL with 100 µL/well), approximately 30‑60% will adhere after 10 minutes at 37° C.
Optimal concentration depends on cell type as well as the application or research objectives.
Source
Mouse myeloma cell line, NS0-derived mouse LAIR1 protein
Gln22-Tyr141 & Ser25-Tyr141, both with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ser25 & No results obtained: Gln22 predicted
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

Theoretical MW
14.3 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
20-35 kDa, 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
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse LAIR1 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). The 253 amino acid (aa) type I transmembrane (TM) protein contains a 21 aa signal sequence, a 124 aa extracellular domain (ECD), a 20 aa TM domain and a 98 aa cytoplasmic domain. The ECD includes one C2-type Ig-like domain and two potential N-linked glycosylation sites. 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). Four mouse LAIR1 splice variants have been identified, but it is not known whether they are expressed as proteins (3). LAIR1b, which is the major alternate transcript, lacks most of the ECD. Of the minor transcripts, LAIR1c lacks a signal sequence, and LAIR1d and 1e lack a TM sequence. All mouse splice forms are identical in the last 90 aa of the cytoplasmic domain. LAIR1 shows high-affinity binding of collagens that results in inhibition of degranulation in a basophilic leukemia cell line (6). Human and mouse LAIR1 ECD share only 32% aa identity but, where studied, sites of expression and activity are similar (3-6). Mouse LAIR1 ECD also shares 62%, 31% and 28% aa identity with rat, canine, and bovine orthologs, respectively.
  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.

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