Recombinant Human VIGR/GPR126 Fc Chimera Protein, CF

When Laminin is immobilized at 5 µg/mL (100 µL/well), Recombinant Human VIGR/GPR126 Fc Chimera (Catalog # 10577-GP) binds with an ED50 of 1.5-12 µg/mL.

2 μg/lane of Recombinant Human VIGR/GPR126 Fc Chimera Protein (Catalog # 10577-GP) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 96-111 kDa and 180-210 kDa, respectively.

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

Recombinant Human VIGR/GPR126 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Laminin is immobilized at 5 µg/mL (100 µL/well), Recombinant Human VIGR/GPR126 Fc Chimera (Catalog # 10577-GP) binds with an ED₅₀ of 1.5-12 µg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human VIGR/GPR126 protein
  

  Human VIGF/GPR126 (Cys38-Lys437) Accession # AAH75798.1	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: AAH75798.1
• N-terminal Sequence: Cys38
• 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: 71 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: 96-111 kDa, under 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 with Trehalose.
• 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 VIGR/GPR126 Fc Chimera Protein, CF

• APG1
• Developmentally regulated G-protein-coupled receptor
• DREG
• FLJ14937
• G protein-coupled receptor 126
• Gm222
• GPR126
• G-protein coupled receptor 126
• HBV PreS1-transactivated protein 2
• PS1TP2
• Vascular inducible G protein-coupled receptor
• vascular-inducible G protein-coupled receptor
• VIGR
• VIGRPS1TP2

Background

VIGR (Vascular Inducible G Protein-coupled Receptor), also known as ADGRG6, DREG, and GPR126, is a neuronal 7 TM pass (G protein)-coupled receptor (GPCR) involved in myelination and glial and Schwann cell development (1, 2). Human VIGR cDNA encodes a 1221 amino acid (aa) residue membrane protein with a 37 aa signal peptide, a 825 aa extracellular domain (ECD) with 27 potential N-linked glycosylation sites, seven transmembrane segments that span between aa 863 and aa 1113, and a 108 aa residue cytoplasmic domain. Within ECD human VIGR shares 83% aa sequence identity with mouse and rat VIGR. VIGR is essential for the development of diverse organs (1, 2). Type IV collagen, a major constituent of the basement membrane, binds to VIGR and activates its signaling function (3). This interaction stimulated the production of cAMP in rodent Schwann cells, which require VIGR activity to differentiate, and in human embryonic kidney (HEK293) cells expressing exogenous VIGR. Laminin-211 binds a novel laminin-binding domain in VIGR N-terminal fragment between aa 446 and 807 (4). VIGR-Laminin-211 interactions regulate terminal differentiation and myelination by ensuring appropriate levels of cAMP for a given stage of Schwann cell development (4).

1. Rughetti, A. et al. (2005) J. Immunol. 174:7764.
2. Engelstaedter, V. et al. (2012) BMC Cancer 12:600.
3. Taylor-Papadimitriou, J. et al. (1999) Biochim. Biophys. Acta 1455:301.
4. Geng, Y. et al. (2012) Front Oncol. 2:76.
5. Tanida, S. et al. (2013) J Biol Chem. 288:31842.
6. Beatson, R. et al. (2016) Nat Immunol. 17:1273.
7. Piyush, T. et al. (2017) Cell Death Differ. 24:1937.

Bioinformatics

• Uniprot:
  • AAH75798.1()