Recombinant Mouse LAIR1 Fc Chimera Protein, CF Summary
Accession # Q8BG84
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.
|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:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Bovine Collagen I is coated at 10 µg/mL, 100 μL/well, Recombinant Mouse LAIR1 Fc Chimera (Catalog # 10092-LR) binds with an ED50 of 0.2‑1.6 μg/mL
2 μg/lane of Recombinant Mouse 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 55-62 kDa and 100-120 kDa, respectively.
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.
- Meyaard, L. (2003) J. Biol. Regul. Homeost. Agents 17:330.
- Meyaard, L. et al. (1997) Immunity 7:283.
- Lebbink, R.J. et al. (2004) J. Immunol. 172:5535.
- Verbrugge, A. et al. (2006) J. Leukoc. Biol. 79:828.
- Verbrugge, A. et al. (2003) Int. Immunol. 15:1349.
- Lebbink, R.J. et al. (2006) J. Exp. Med. 203:1419.
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