Recombinant Human 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 Human LAIR1 Fc Chimera
binds with an ED50 of 25-150 ng/mL. |
| Source |
Human embryonic kidney cell, HEK293-derived human LAIR1 protein Human LAIR1 (Gln22-His163) Accession # NP_002278 | IEGRMD | Human IgG1 (Pro100-Lys330) | | N-terminus | | C-terminus | |
|
| Accession # |
|
| N-terminal Sequence |
No results obtained. Gln22 inferred from enzymatic pyroglutamate treatment revealing 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 |
|
| 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 |
55-65 kDa, reducing conditions |
Packaging, Storage & Formulations
| Storage |
- 12 months from date of receipt, ≤ -20 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, ≤ -20 °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 Human LAIR1 Fc Chimera Protein, CF
Background
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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