Recombinant Human Nectin-1 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 Nectin-3 Protein
(Catalog #
3064-N3) is immobilized at 3.0 μg/mL (100 μL/well), the concentration of Biotinylated Recombinant Human Nectin‑1 His-tag Avi-tag (Catalog # AVI2880) that produces 50% of the optimal binding response is 0.10-1.00 μg/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human Nectin-1 protein Human Nectin-1 (Gln31-Gly346) Accession # Q15223.3 | 6-His tag | Avi-tag | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Gln31 inferred from enzymatic pyroglutamate treatment revealing Val32. |
Structure / Form |
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 |
35 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 |
50-65 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 200 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-1 His-tag Avi-tag Protein, CF
Background
Nectin-1, also called poliovirus
receptor-related protein-1 (PRR1), is a member of the Nectin family which are
Ca++-independent immunoglobulin (Ig)-like cell adhesion molecules (CAMs) that
organize intercellular junctions. The Nectin family is comprised of 4 family
members and 5 nectin-like molecules and they are structurally homologous to the
poliovirus receptors (1). Mature human Nectin-1 consists of an extracellular
domain (ECD) with three immunoglobulin-like domains, a single transmembrane
segment, and a cytoplasmic domain that interacts with
the F-actin–binding protein afadin (2). Within the ECD, human Nectin-1 shares 93%
and 94% amino acid sequence identity with mouse and rat Nectin1, respectively.
Two splice variants of Nectin-1 are known, one with an alternate cytoplasmic
domain and a soluble form (4). Nectin-1 binds viral glycoprotein D to mediate
herpesvirus (but not poxvirus) entry into vaginal mucosa, sensory neurons and
fibroblasts (4-7). In forming adherens junctions and synapses, Nectins-1 and -3
initiate cell-cell interactions, recruiting alpha v beta 3 integrin
extracellularly and cadherins intracellularly through afadin and other
junctional proteins (2, 8-11). Nectin-1 forms homodimers in cis,
followed by interactions in trans with Nectin-1, -3 or -4 (1). These
interactions organize the cytoskeleton, strengthen attachment to basement
membrane and promote further cell-cell connections. Nectin-1 also recognizes
CD96 on NK cells (12). Deficiency of Nectin-1 can result in cleft lip/palate
ectodermal dysplasia (13). Nectin-1 down-regulation in epithelial cancers,
mediated in part by ectodomain shedding, may contribute to invasiveness (14).
In colorectal cancer, Nectin-1 expression was found to be associated with a
high risk for early disease recurrence (15). Our Avi-tag Biotinylated Nectin-1 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.
- Takai, Y. et al. (2008) Nat. Rev. Mol. Cell Biol. 9:603.
- Samanta, D. et al. (2012) PNAS 109:14836.
- Fabre, S. et al. (2002) J. Biol. Chem. 277:27006.
- Lopez, M. et al. (2001) J. Virol. 75:5684.
- Cocchi, F. et al. (1998) Proc. Natl. Acad. Sci. USA 95:15700.
- Linehan, M. M. et al. (2004) J. Virol. 78:2530.
- Simpson, S. A. et al. (2005) J. Neurovirol. 11:208.
- Mizoguchi, A. et al. (2002) J. Cell Biol. 156:555.
- Togashi, H. et al. (2006) J. Cell Biol. 174:141.
- Tachibana, K. et al. (2000) J. Cell Biol. 150:1161.
- Takai, Y. and H. Nakanishi (2003) J. Cell Science 116:17.
- Seth, S. et al. (2007) Biochem. Biophys. Res. Commun. 364:959.
- Suzuki, K. et al. (2000) Nat. Genet. 25:427.
- Tanaka, Y. et al. (2002) Biochem. Biophys. Res. Commun. 299:472.
- Tampakis, A. et al. (2019) Oncology. 96:318.
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