UNC93B1 (E6C3E) Rabbit mAb recognizes endogenous levels of total UNC93B1 protein.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Tyr40 of human UNC93B1 protein.

Signaling by Toll-like receptors (TLRs) is essential for innate and adaptive immune responses (1-3). The endoplasmic reticulum (ER) protein, UNC93B1, was initially identified by a genetic screen analyzing defects in TLR signaling (1,2). UNC93B1 is a multipass transmembrane protein required for normal TLR function and facilitates trafficking of TLRs from the ER to endolysosomes (4,5). UNC93B1 is essential for signaling of TLR3, TLR7, and TLR9 in both humans and mice, and physically interacts with these TLRs in the ER via adaptor protein complex 2 (AP-2) and syntenin-1 (4-7). Mice carrying mutations in UNC93B1 are susceptible to viral infection and autoimmune disease, and mutations in several regions of UNC93B1 in humans have been implicated in autoimmune diseases such as systemic lupus erythematosus, highlighting the role of UNC93B1 in innate and autoimmunity (7-9).