Recombinant Human VSTM4 Fc Chimera Protein, CF

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Recombinant Human VSTM4 Fc Chimera (Catalog # 2086-VT) inhibits IFN-gamma secretion byhuman peripheral blood mononuclear cells in the presence of anti-CD3 antibody. TheED50 for this effect is 1-10 μg/mL.
2 μg/lane of Recombinant Human VSTM4 (Catalog # 2086-VT) was resolved with SDS-PAGE underreducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Bluestaining, showing bands at 58-74 kDa and ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human VSTM4 Fc Chimera Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit anti-CD3 antibody induced IFN-gamma secretion by human peripheral blood mononuclear cells (PBMC). The ED50 for this effect is 1-10 μg/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human VSTM4 protein
Human VSTM4
(Leu24-Tyr180)
Accession # Q8IW00.3
IEGRMD Human IgG1
(Pro100-Lys330)
N-terminusC-terminus
Accession #
N-terminal Sequence
Leu24
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
45 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
58-74 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 °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 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 VSTM4 Fc Chimera Protein, CF

  • C10orf72
  • FLJ31737
  • hypothetical protein LOC196740
  • V-set and transmembrane domain containing 4
  • VSTM4

Background

V-set and transmembrane domain-containing protein 4 (VSTM4) is a single-pass type I membrane protein in the immunoglobulin superfamily. Human VSTM4 is synthesized as a 320 amino acid (aa) precursor that contains a 23 aa signal sequence, 157 aa extracellular region, 21 aa TM domain, and 119 aa cytoplasmic tail. In humans, part of the extracellular region is cleaved into a 50 aa secreted peptide (aa 55-104) compared to mouse, which is cleaved into a 49 aa peptide (aa 55-103) (1). Because of its role in enhancing L-type voltage-gated calcium channel (L-VGCC) currents in photoreceptors, this peptide was named peptide Lv (1). Peptide Lv is expressed in the central nervous system and a variety of organs including spleen, intestine, retina, and lung (1, 2). The peptide may have possible roles in regulating the cardiovascular system and L-VGCC dependent neural plasticity (1, 2). Human VSTM4 gene is located on chromosome 10, which may be linked to late-onset Alzheimer's disease (3). Down-regulation of VSTM4 increased tamoxifen sensitivity and suppressed growth in cultured breast cancer cells (4). Within the ECD, human VSTM4 shares 87% and 85% aa sequence identity with mouse and rat VSTM4, respectively. The biological functions of VSTM4 remain unknown. Our in-house data show that VSTM4 inhibits the human T cell activation, including anti-CD3 induced IL-2 and IFN-gamma secretion, and T cell proliferation.
  1. Shi, L. et al. (2012) PLoS. 7:e43091.
  2. Shi, L. et al. (2015) Biochim. Biophys. Acta. 1853:1154.
  3. Grupe, A. et al. (2006) Am. J. Hum. Genet. 78:78.
  4. Mendes-Pereira, A. et al. (2012) Proc. Natl. Acad. Sci. 109:2730.

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