Anti-MPYS antibody produced in rabbit

MPYS is a recently identified plasma membrane tetraspanner that is associated with major histocompatibility complex class II (MHC-II) and mediates its transduction of apoptotic signals. It has also been found to be associated with VISA, a mitochondrial protein that acts as an adaptor in virus-triggered signaling. MPYS also interacts with IRF3 and recruits the kinase TBK1 to the VISA-associated complex, acting as a critical mediator of virus-triggered IRF3 activation and interferon (IFN) expression. It is thought that the binding of nucleic acid to the innate immune protein RIG-I causes complex formation between RIG-I, VISA, and MPYS. This complex then recruits TBK1 to phosphorylate IRF3 which then directly activates IFN transcription. At least three isoforms of MPYS are known to exist.

TMEM173 (transmembrane protein 173) gene is mapped to human chromosome 5q31.2. The encoded protein localizes in the endoplasmic reticulum.

MPYS antibody was raised against a 17 amino acid peptide near the carboxy terminus of human MPYS.

The innate immune response against the viral and bacterial infections is mostly regulated by TMEM173 (transmembrane protein 173), also known as stimulator of interferon genes (STING). It is considered as an important adaptor protein for cytosolic DNA sensing pathways. Downregulation of the gene was observed in tumor tissues. TMEM173 acts as a pattern recognition receptor and identifies pathogen-associated molecular patterns. It also mediates signal transduction pathways. TMEM173 is significantly associated with immunity and inflammation.

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Supplied at approx. 1 mg/mL in phosphate buffered saline containing 0.02% sodium azide.

The action of this antibody can be blocked using blocking peptide SBP3500076.

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