Recombinant Human IGSF8/CD316 Fc Chimera Protein, CF

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.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human IGSF8/CD316 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human IGSF8/CD316 Fc Chimera is immobilized at 1 µg/mL (100 µL/well), Biotinylated Recombinant CD81 Fc Chimera binds with an ED₅₀ of 1.2-7.2 μg/mL
• Source: Human embryonic kidney cell, HEK293-derived human IGSF8/CD316 protein
  

  Human IGSF8 (Arg28-Thr579) Accession # Q969P0-1	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: Q969P0-1
• N-terminal Sequence: Arg28
• Structure / Form: Disulfide-linked homodimer
• 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:
  • Bioactivity
• Theoretical MW:
  85 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: 86-113 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage:
  • 12 months from date of receipt, ≤ -20 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, ≤ -20 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS.
• 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 Recombinant Human IGSF8/CD316 Fc Chimera Protein, CF

• CD316 antigen
• CD316
• CD81P3
• CD81P3LIR-D1
• EWI2
• EWI-2
• EWI2CD81 partner 3
• Glu-Trp-Ile EWI motif-containing protein 2
• IGSF8
• immunoglobulin superfamily, member 8
• KCT4
• KCT-4
• Keratinocytes-associated transmembrane protein 4
• PGRL
• PGRLimmunoglobulin superfamily member 8

Background

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).

1. Clark, K.L. et al. (2001) J. Immunol. 167:5115.
2. Stipp, C.S. et al. (2001) J. Biol. Chem. 276:40545.
3. Charrin, S. et al. (2003) Biochem. J. 373:409.
4. Stipp, C.S. et al. (2003) J. Cell Biol. 163:1167.
5. Kettner, S. et al. (2007) Mol Cell Biol. 27:7718.
6. Gordón-Alonso, M. et al. (2012) J Immunol 189:689.
7. Kolesnikova, T. et al. (2009) Neoplasia.11:77.

Bioinformatics

• Uniprot:
  • Q969P0-1()