Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
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 rhLAIR-2 coated plates (50 µg/mL with 100 µL/well), approximately 40%-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 human LAIR2 protein Gln22-Pro152, with a C-terminal 6-His tag |
Accession # | |
N-terminal Sequence | No results obtained: Gln22 predicted & Thr37 |
Protein/Peptide Type | Recombinant Proteins |
Gene | LAIR2 |
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. |
Dilutions |
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Theoretical MW | 14.9 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. |
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SDS-PAGE | 20 kDa, reducing conditions |
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Publications |
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Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Buffer | Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity | >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in sterile PBS. |
LAIR-2 (leukocyte-associated Ig-like receptor-2; CD306) is a secreted, 131 amino acid (aa) protein that contains one Ig-like C2 type domain, making it a member of the Ig superfamily. When compared to LAIR-1, its transmembrane counterpart, it shares 83% aa identity across the signal sequence and extracellular domains; (1-3) although one is secreted and one is membrane-bound, the two LAIR proteins are thought to have arisen from a common gene ancestor and appear to share similar adhesion profiles. This suggests that LAIR-2 may compete with LAIR-1 for ligand binding (3, 4). A 114 aa alternate splice form of LAIR-2 is truncated at the C terminus, but retains the entire Ig domain (1-3). The expression profile of these splice forms, and the presence of orthologs in other species, have not been reported.
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