Recombinant Human VSIG3 C-Terminal Fc Chimera Protein, CF

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Recombinant Human VSIG3 C-Terminal Fragment Fc Chimera (Catalog # 10075-VS) inhibits anti-CD3 antibody induced IFN-gamma secretion by human peripheral blood mononuclear cells. The ED50 for this effect is 1-6 ...read more
2 μg/lane of Recombinant Human VSIG3 C-Terminal Fragment was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 41-51 kDa and ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human VSIG3 C-Terminal Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit anti-CD3 antibody induced IL-17 or IFN-gamma secretion by human peripheral blood mononuclear cells (PBMC). The ED50 for this effect is 1-6 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human VSIG3 protein
Human VSIG3
(Pro144-Gly241)
Accession # Q5DX21
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Pro144
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
37 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
41-51 kDa, 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.
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 VSIG3 C-Terminal Fc Chimera Protein, CF

  • Brain and testis-specific immunoglobulin superfamily protein
  • BTIGSF
  • BT-IgSF
  • cancer/testis antigen 119
  • CT119
  • CXADR like 1
  • CXADRL1
  • IGSF11
  • Igsf13
  • immunoglobulin superfamily member 11
  • immunoglobulin superfamily, member 11
  • MGC35227
  • V-set and immunoglobulin domain containing 3
  • V-set and immunoglobulin domain-containing protein 3
  • VSIG3
  • VSIG3brain and testis-specific immunoglobin superfamily protein

Background

VSIG3, also known as IGSF11, BT-IgSF, and CLMP, is an approximately 50 kDa transmembrane adhesion protein (1). Mature human VSIG3 consists of a 219 amino acid (aa) extracellular domain (ECD), a 21 aa transmembrane segment, and a 169 aa cytoplasmic domain (2). Within the ECD, human VSIG3 shares 95% aa sequence identity with mouse and rat VSIG3. Human ECD contains two tandem Ig-like domains, and this product includes only the C-terminal Ig-like domain (aa 144-241). Alternative splicing generates additional isoforms with a substituted signal peptide that may also have a deletion in the second Ig-like domain (3). VSIG3 is expressed on epithelial and endothelial cells, neurons and glial cells, and platelets (2-4). It localizes to epithelial tight junctions and mediates homophilic in trans cell adhesion (3-5). VSIG3 also localizes to neuronal postsynaptic densities where it recruits the GluA1 and GluA2 subunits of AMPA receptors and supports excitatory synaptic transmission (6). The short isoform can be up-regulated in gastric cancer (7). In zebrafish, VSIG3 is expressed in melanophores and plays a role in the development and patterning of pigment cells (8).
  1. Schreiber, J. et al. (2014) Adv. Neurobiol. 8:21.
  2. Suzu, S. et al. (2002) Biochem. Biophys. Res. Commun. 296:1215.
  3. Katoh, M. and M. Katoh (2003) Int. J. Oncol. 23:525.
  4. Raschperger, E. et al. (2004) J. Biol. Chem. 279:796.
  5. Harada, H. et al. (2005) J. Cell. Physiol. 204:919.
  6. Jang, S. et al. (2016) Nat. Neurosci. 19:84.
  7. Watanabe, T. et al. (2005) Cancer Sci. 96:498.
  8. Eom, D.S. et al. (2012) PLoS Genet. 8:e1002899.

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