Recombinant Human ILDR2 Fc Chimera Protein, CF

Recombinant Human ILDR2 Fc Chimera 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: ILDR2

ILDR2 (Immunoglobulin-like domain-containing receptor 2) is a member of the B7-like family of proteins that regulate T cell activity (1). ILDR2 is also a known endoplasmic reticulum molecule that regulates lipid homeostasis (2, 3). It contains a signal peptide, an Ig-like V-type domain, a stalk region, a transmembrane domain and a CCP-rich domain (1, 4). The human ILDR2 lumenal domain shares a 99% and 98% homology with the mouse and rat respectively. The human gene encoding ILDR2 is located in a region on Chr1q23–25 that has been associated with type 2 diabetes (5). ILDR2 and its two paralogs, ILDR1 and lipolysis-stimulated receptor (LSR; also named ILDR3), are members of angulin family proteins (angulin-1/LSR, angulin-2/ILDR1, and angulin-3/ILDR2), and they are identified as protein components of tricellular tight junctions (tTJs), which are required for recruitment of tricellulin to tTJs (6). ILDR2 plays critical roles in hepatic clearance of lipoproteins and in lipid homeostasis (3). ILDR2 regulates human dendritic cells (DC2 cells, a subpopulation of polarized DCs that promotes Th2 differentiation) (7). Recent publications reported that ILDR2 displayed negative regulatory functions on human and mouse T cells in various experimental systems. Fusion protein of ILDR2 lumenal domain with an Fc fragment, displays therapeutic effects in collagen-induced arthritis (CIA), a mouse model of rheumatoid arthritis (RA). ILDR2 represents a novel B7-like ligand that exerts negative immune modulation via interaction with a putative counterpart receptor expressed on activated T cells (1, 4).

Related Research Areas

• Adhesion Molecules on Endothelial Cells
• Adhesion Molecules on VSMC
• Cell to Cell Adhesion Disassembly During EMT
• Epithelial Cell Polarity