Recombinant Human Nectin-1 His-tag Avi-tag Protein, CF Summary
Accession # Q15223.3
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 200 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
2 μg/lane of Biotinylated Recombinant Human Nectin‑1 His-tag Avi-tag Protein (Catalog # AVI2880) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 50-65 kDa.
When Recombinant Human Nectin-3 Protein (3064-N3) is immobilized at 3.0 μg/mL (100 μL/well), the concentration of Biotinylated Recombinant Human Nectin‑1 His-tag Avi-tag Protein (Catalog # AVI2880) that produces 50% of the optimal binding response is 0.100-1.00 μg/mL
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.
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