Recombinant Human IGSF8/CD316 Fc Chimera Protein, CF Summary
Accession # Q969P0-1
When Recombinant Human IGSF8/CD316 Fc Chimera (Catalog# 1241-S8) is immobilized at 1 µg/mL (100 µL/well), Biotinylated RecombinantCD81 Fc Chimera binds with an ED50 of 1.2-7.2 μg/mL.
2 μg/lane of Recombinant Human IGSF8/CD316 Fc Chimera was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 86-113 kDa and 170-230 kDa, respectively.
IGSF8 (Immunoglobulin superfamily member 8), also known as EWI-2, KCT-4, LIR-D1, and PGRL, is a 75-kDa cell surface protein belonging to the immunoglobulin superfamily (1). IGSF8 is widely expressed, with pronounced mRNA expression in the brain and protein expression on peripheral blood lymphocytes and hepatocytes where it colocalizes with CD81 (1-3). It strongly associates with tetraspanins CD9 and CD81 which may act as physical linkers to form a complex with alpha 3 beta 1 integrin that may regulate cell aggregation and motility on laminin-5 (4). Human IGSF8 is synthesized as a 613 aa protein that includes a 27 aa signal peptide, a 552 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 13 aa cytoplasmic tail. Within the ECD, human IGSF8 shares 91% and 90% aa sequence identity with mouse and rat IGSF8, respectively. IGSF8 is an inducible receptor for Heat Shock Protein A8 (HSPA8) on activated dendritic cells (5). IGSF8 can interact with alpha -Actinin to regulate T cell immune synapses and HIV viral infection (6). In human glioma patients, low IGSF8 expression correlates with shorter survival time. Studies have shown that re-expression of IGSF8 in malignant glioblastoma cell lines inhibited glioblastoma colony formation in soft agar and caused diminished cell motility and invasion (7).
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- Gordón-Alonso, M. et al. (2012) J Immunol 189:689.
- Kolesnikova, T. et al. (2009) Neoplasia.11:77.
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