NLRX1 (D4M3Z) Rabbit mAb #13829

The nucleotide-binding oligomerization domain (NOD)-like receptor (NLR) family of proteins is a diverse family of cytoplasmic innate immune receptors. They are characterized by the presence of an amino-terminal effector domain, which is often either a caspase activation and recruitment domain (CARD) or a pyrin domain (PYD), followed by a NACHT domain and carboxy-terminal leucine-rich-repeats (LRR) involved in recognition of pathogen-associated molecular patterns (PAMPs) (1). NLR proteins play a variety of roles during the innate immune response including pathogen sensing, transcriptional activation of proinflammatory cytokines through NF-κB, transcriptional activation of type I interferons through IRFs, and formation of inflammasomes leading to activation of inflammatory caspases (1-7).
NLRX1 (CLR11.3/NOD26/NOD5/NOD9) is unique among NLR family members in that it contains an amino-terminal mitochondrial targeting sequence resulting in localization to the mitochondria (8,9). In contrast to most NLR proteins, NLRX1 has been shown to act as a negative regulator of innate immune responses through inhibition of MAVS-Rig-I signaling, as well as inhibition of Toll-like receptor (TLR)-mediated NF-κB activation (9-11). In addition, overexpression of NLRX1 enhanced the production of reactive oxygen species (ROS), resulting in prolonged NF-κB and JNK signaling in response to TNF-α (8).