Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
NLRX1 Antibody recognizes endogenous levels of total NLRX1 protein. This antibody cross-reacts with a 65 kDa protein of unknown origin.
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Lys441 of human NLRX1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
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).
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