Biotinylated Recombinant Human LAIR2 Fc Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
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), Biotinylated
Recombinant Human LAIR2 Fc Chimera Avi-tag (Catalog # AVI10166)
binds with an ED50 of 0.175-1.4 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human LAIR2 protein Human LAIR2 (Gln22-Pro152) Accession # NP_002279.2 | IEGRMD | Human IgG1 (Pro100-Lys333) | Avi-tag | N-terminus | | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Gln22; deduced from Glu23 upon deblocking |
Structure / Form |
Disulfide-linked homodimer, biotinylated via Avi-tag |
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 |
50-59 kDa, under reducing conditions |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °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 Biotinylated Recombinant Human LAIR2 Fc Avi-tag Protein, CF
Background
LAIR2 (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 LAIR1, its transmembrane counterpart, LAIR2
shares 83% aa identity across the signal sequence and extracellular
domains (1-3). Although one is secreted and the other 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 LAIR2 may
compete with LAIR1 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. LAIR2 is a soluble
collagen-receptor, and it can be detected in the synovial fluid of rheumatoid
arthritis patients, urine of pregnant women, and as well as primary cells
(5, 6). In vitro studies have demonstrated LAIR2 can
compete with LAIR1 for the same collagen binding site and suggesting LAIR2 may
play an important role in immune cell activation (5, 6). LAIR2 can
interact with complement component 1q (C1q) and mannose-binding lectin (MBL)
and act as a complement inhibitor for the treatment and prevention of
antibody-mediated allograft rejection and antibody-mediated clinical conditions
(7). Our Avi-tag Biotinylated human LAIR2 features biotinylation at a single
site contained within the Avi-tag, a unique 15 amino acid peptide. Protein
orientation will be uniform when bound to streptavidin-coated surface due to
the precise control of biotinylation and the rest of the protein is unchanged
so there is no interference in the protein's bioactivity.
- Meyaard, L. (2003) J. Biol. Regul. Homeost. Agents 17:330.
- Meyaard, L. et al. (1999) J. Immunol. 162:5800.
- Meyaard, L. et al. (1997) Immunity 7:283.
- Xu, X.G. et al. (2005) Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi. 21:553.
- Lebbink, R.J. et al. (2008) J. Immunol. 180:1662.
- Olde Nordkamp, M.J. et al. (2011) Arthritis Rheum. 63:3749.
- Olde Nordkamp, M.J. et al. (2014) J. Innate Immun. 6:284.
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