Recombinant Human TEM5/GPR124 His-tag Protein, CF

Recombinant Human TEM5/GPR124 His-tag Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

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.

Background: TEM5/GPR124

G-protein coupled receptor 124 (GPR124), otherwise known as Adhesion G protein-coupled receptor A2 (AGRA2) and tumor endothelial marker 5 (TEM5), is localized on the surface of endothelial cells. Adhesion GPCRs are the second largest group within the GPCR superfamily, and are implicated in cell-to-cell and cell-to-matrix adhesion with high promiscuity towards ligands (1, 2). Humam TEM5/GPR124 contains a 738 amino acid (aa) extracellular domain (ECD), a transmembrane domain with seven helices of varying lengths, and a 270 aa cytoplasmic domain. Human TEM5/GPR124 shares 90% aa identity to both mouse and rat TEM5/GPR124 within the  N-terminal ECD. TEM5/GPR124 shares structural characteristics with other adhesion GPCR family members because of its relatively large N and C-terminal domains, and a GAIN domain (1, 2). The N-terminal ECD contains an exposed RGD motif and binds to RGD-dependent integrins on the surface of endothelial cells. TEM5/GPR124 mediates endothelial cell survival during angiogenesis by linking integrin to glycosaminoglycans. TEM5/GPR124 has also been shown to interact with DLG1 through its PDZ-binding motif (3). In humans, TEM5/GPR124 appears to play a role in tumor vascular biology, as TEM5/GPR124 transcripts are dramatically up-regulated in vascular ECs in tumors relative to ECs in normal tissue (4). The most N-terminal domain of RECK binds to the leucine-rich repeat (LRR) and immunoglobulin (Ig) domains of TEM5/GPR124 (4). RECK is the predominant binding partner of TEM5/GPR124 (5). TEM5/GPR124 and RECK act primarily in an extracellular fashion. RECK has been identified as a TEM5/GPR124-associated Wnt7 receptor that forms a 1:1 complex with active, monomeric, hydrophobic Wnt7 (5). RECK and TEM5/GPR124 are part of the cell surface protein complex that transduces Wnt7a- and Wnt7b-specific signals in mammalian CNS ECs to promote angiogenesis and regulate the blood-brain barrier (BBB) (4).

Related Research Areas

• Adhesion G Protein-Coupled Receptors
• Orphan G Protein-Coupled Receptors