Recombinant Human Nectin-2/CD112 His-tag Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human DNAM-1 Fc Chimera (Catalog #
666-DN) is immobilized at 2.00 µg/mL (100 µL/well), Biotinylated Recombinant Human Nectin-2/CD112 His-tag Avi-tag protein binds with an ED 50 of 0.600-3.60 µg/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human Nectin-2/CD112 protein Human Nectin-2 (Gln32-Leu360) Accession # NP_002847.1 | 6-His tag | Avi-tag | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Gln32 |
Structure / Form |
|
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 |
38 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 |
43-55 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 100 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 Nectin-2/CD112 His-tag Avi-tag Protein, CF
Background
Nectin-2, also known as Poliovirus
receptor-related 2 (PRR2), is a member of the Nectin family which are Ca++-independent immunoglobulin (Ig)-like cell adhesion molecules
(CAMs) that organize intercellular junctions (1). The Nectin family is
comprised of 4 family members and 5 nectin‑like molecules and they are structurally
homologous to the poliovirus receptors (2). Mature human Nectin‑2 consists of
an extracellular domain (ECD) with three immunoglobulin-like domains, a single transmembrane
segment, and a cytoplasmic domain bind the F-actin–binding protein afadin (3).
Within the ECD, human Nectin‑2 shares 72% amino acid (aa) sequence
identity with mouse Nectin‑2. Alter native splicing generates an isoform with a
truncated cytoplasmic tail (1). Nectin-2 localizes to adherens junctions
between neurons, endothelial cells, epithelial cells, and fibroblasts (3, 4).
It forms homodimers in
cis, followed by dimers in trans (between
cells) (4). It does not
cis‑dimerize with other Nectins but forms
cis‑dimers between its two splice forms. Notably, a Nectin-2
cis‑dimer on one
cell can heterodimerize with a Nectin‑3
cis‑dimer on a neighboring cell (4).
Nectin‑2 additionally binds to DNAM-1/CD226 on NK cells and triggers NK
cell cytolytic activity (5, 6). Nectin‑2 is known to bind pseudorabies virus
and herpes simplex virus-2 (HSV-2), but not HSV-1 or poliovirus (4, 7).
Nectin‑2 is a component of cardiac intercalated discs and limits fibrosis and
dysfunction resulting from pressure overload (8). Our Avi-tag Biotinylated Nectin‑2 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.
- Eberle, F. et al. (1995) Gene 159:267.
- Samanta, D. and S.C. Almo (2015) Cell. Mol. Life Sci. 72:645.
- Samanta, D. et al. (2012) PNAS 109:14836.
- Struyf, F. et al. (2002) J. Virol. 76:12940.
- Bottino, C. et al. (2003) J. Exp. Med. 198:557.
- Pende, D. et al. (2005) Mol. Immunol. 42:463.
- Warner, M.S. et al. (1998) Virology 246:179.
- Satomi-Kobayashi, S. et al. (2009) Hypertension 54:825.
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