immunoglobulin-like domain containing receptor;Ildr;Dbsm;C1orf;DJ782G;Angulin;Angulin-3;Dbsm1;DJ782G3.1;immunoglobulin-like domain containing receptor 2;LISCH-Like;C1orf32;ILDR2

HEK293 Cells

Leu21-Glu186

Q71H61

Human

19.5 kDa

45-55 kDa

C-His

Not validated for activity

> 95 % as determined by reducing SDS-PAGE.

< 1.0 EU per μg of the protein as determined by the LAL method.

Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

This product is provided as lyophilized powder which is shipped with ice packs.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Normally 5% - 8% trehalose, mannitol and 0.01% Tween 80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the printed manual.

Please refer to the printed manual for detailed information.

ILDR2 is a member of the B7-like family of proteins that regulate T cell activity, is also a known endoplasmic reticulum molecule that regulates lipid homeostasis. 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. ILDR2 plays critical roles in hepatic clearance of lipoproteins and in lipid homeostasis. ILDR2 regulates human dendritic cells (DC2 cells, a subpopulation of polarized DCs that promotes Th2 differentiation). 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.