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Description
LAIR2/CD306 Fc Chimera Protein, HumanProduct Specification Species Human Accession Q6ISS4 Amino Acid Sequence Gln22 Pro152, with C terminal hIgG1 Fc Expression System HEK293 Molecular Weight 46 52 kDa(Reducing) Purity 95%, by SDS PAGE under reducing conditions Endotoxin <0. 1EU g Conjugation Unconjugated Tag Human Fc Tag Physical Appearance Lyophilized Powder Storage Buffer PBS, pH7. 4 Reconstitution Reconstitute at less than 1 mg mL according to the size in ultrapure water after rapid
Product Specification
| Species | Human |
| Accession | Q6ISS4 |
| Amino Acid Sequence | Gln22-Pro152, with C-terminal hIgG1 Fc |
| Expression System | HEK293 |
| Molecular Weight | 46-52 kDa(Reducing) |
| Purity | ＞95%, by SDS-PAGE under reducing conditions |
| Endotoxin | <0.1EU/μg |
| Conjugation | Unconjugated |
| Tag | Human Fc Tag |
| Physical Appearance | Lyophilized Powder |
| Storage Buffer | PBS, pH7.4 |
| Reconstitution | Reconstitute at less than 1 mg/mL according to the size in ultrapure water after rapid centrifugation. |
| Stability & Storage | · 12 months from date of receipt, lyophilized powder stored at -20 to -80℃. · 3 months, -20 to -80℃ under sterile conditions after reconstitution. · 1 week, 2 to 8℃ under sterile conditions after reconstitution. · Please avoid repeated freeze-thaw cycles. |
Background
The leukocyte-associated Ig-like receptor-1 (CD305) is an ITIM-containing inhibitory immune receptor, belonging to the Ig superfamily. LAIR-2 is encoded by a gene located in the vicinity of the LAIR-1 gene in the leukocyte receptor complex on human chromosome 19q13.4. The predicted LAIR-2 protein has a single Ig-like domain sharing 84% sequence homology with hLAIR-1, and the molecule lacks a transmembrane and cytoplasmic region suggesting it is a secreted protein. In contrast to hLAIR-1, LAIR-2 has no orthologs in mice or rats. The membrane ligand for LAIR-1 and LAIR-2 was expressed extensively and ligand recognition was of cross-species. LAIR-2 blocked the interaction of LAIR-1 with its ligand but LAIR-1 didn't block the interaction of LAIR-2 with its ligand. LAIR-2 had a higher affinity for collagen than did LAIR-1. LAIR-2 is a more potent antagonist of LAIR-1 function in vivo, while both sLAIR-1 and LAIR-2 are potential biomarkers. Recently shown that recombinant LAIR-2–Fc is able to interfere with collagen-induced platelet aggregation and that it efficiently inhibits the binding of collagen to glycoprotein VI and von Willebrand factor.
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