Recombinant Human VIGR/GPR126 Fc Chimera Protein, CF Summary
|Human VIGF/GPR126 |
Accession # AAH75798.1
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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.
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).
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