Recombinant Human LAIR1 Fc Chimera Protein, CF Summary
Product Specifications
| Human LAIR1 (Gln22-His163) Accession # NP_002278 | IEGRMD | Human IgG1 (Pro100-Lys330) |
| N-terminus | C-terminus | |
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
9964-LR
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
| Reconstitution | Reconstitute at 500 μg/mL in PBS. |
| Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: |
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Scientific Data
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When Bovine Collagen I is coated at 10 µg/mL, Recombinant Human LAIR-1 Fc Chimera binds with an ED50 of 25-150 ng/mL.
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2 μg/lane of Recombinant Human LAIR1 was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® blue staining, showing bands at 55-65 kDa and 110-130 kDa, respectively.
Reconstitution Calculator
Background: LAIR1
LAIR1 (leukocyte-associated Ig-like receptor-1, designated CD305) is an approximately 40 kDa type I transmembrane inhibitory glycoprotein belonging to the Ig superfamily (1-4). LAIR1 is a collagen-binding protein that is expressed in a differentiation- and activation-dependent manner on most immune cells, including T, B, NK and dendritic cells (DC), monocytes, CD34+ hematopoietic progenitors, most thymocytes, and selected granulocyte populations (2-7). Mature human LAIR1 is a 266 amino acid (aa) type I transmembrane protein that includes a 144 aa extracellular domain (ECD) with one collagen-binding C2-type Ig-like domain, and a 101 aa cytoplasmic domain with two ITIM motifs (2, 3, 8, 9). Of four potential human LAIR1 splice variants, LAIR1b has a 17 aa deletion within the ECD, but outside the Ig domain. LAIR1c differs from LAIR1b by one aa. LAIR1d has a 78 aa cytoplasmic truncation and lacks ITIM motifs. Human LAIR1 ECD shares <45% aa sequence identity with mouse, rat, bovine or canine LAIR1 ECD, but all are functional orthologs. Humans, but not rodents, also express the 152 aa secreted protein LAIR2, which shares 83% aa sequence identity with the LAIR1 ECD up to aa 140 and can block LAIR1 collagen binding (1, 2). A soluble form of LAIR1 found in plasma and urine also binds collagen (10). Adhesion of LAIR1 to collagens in the extracellular matrix, transmembrane collagens expressed by tumor cells, or antibody-mediated crosslinking of LAIR1, inhibits signals relayed by ITAM-bearing receptors and some cytokine-mediated signals (6-8, 13). Processes that are inhibited include B and T cell receptor-mediated activation, NK and T cell‑mediated cytotoxicity, and basophil degranulation (1-4, 8). LAIR1 is reduced or absent on chronic lymphocytic leukemia (CLL) B cells, and some B and DC cells in systemic lupus erythematosus (SLE). Its under‑expression potentially enhances CLL proliferation and SLE immune responses (7, 11, 12).
- Meyaard, L. (2008) J. Leukoc. Biol. 83:799.
- Meyaard, L. et al. (1997) Immunity 7:283.
- Lebbink, R.J. et al. (2004) J. Immunol. 172:5535.
- Ouyang, W. et al. (2003) Biochem. Biophys. Res. Commun. 310:1236.
- Verbrugge, A. et al. (2006) J. Leukoc. Biol. 79:828.
- Lebbink, R.J. et al. (2006) J. Exp. Med. 203:1419.
- Bonaccorsi, I. et al. (2010) PLoS ONE 5:e15080.
- Tang, X. et al. (2009) J. Immunol. 182:5446.
- Brondijk, T.H.C. et al. (2010) Blood 115:1364.
- Olde Nordkamp, M.J. et al. (2011) Arthritis Rheum. 63:3749.
- Poggi, A. et al. (2008) Leukemia 22:980.
- Colombo, B.M. et al. (2012) PLoS ONE 7:e31903.
- Rygiel, T.P. et al. (2011) Mol. Immunol. 49(1-2):402.
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