Anti-NME8 / TXNDC3 / Thioredoxin domain-containing protein 3

Adding 0.2 ml of distilled water will yield a concentration of 500 ug/ml. NME8 antibody detects Thioredoxin domain-containing protein 3, a microtubule-associated oxidoreductase that stabilizes axonemal structures in motile cilia. The UniProt recommended name is Thioredoxin domain-containing protein 3 (NME8). Also known as TXNDC3 or SPTRX2, this protein contains a thioredoxin-like domain and functions as part of the dynein regulatory complex involved in ciliary motility and organization.Functionally, NME8 antibody identifies a 588-amino-acid protein localized to cilia and flagella, where it forms disulfide-linked complexes that maintain axonemal integrity. NME8 acts as a redox-active thioredoxin enzyme, regulating disulfide bond formation and stabilization of microtubule doublets. It is crucial for proper assembly of outer dynein arms, which generate the bending motion of motile cilia.The NME8 gene is located on chromosome 7p14.1 and is expressed in ciliated tissues such as respiratory epithelium, oviduct, and testis. Through its thioredoxin activity, NME8 supports sperm motility, mucociliary clearance, and left-right body asymmetry during embryonic development.Pathologically, mutations in NME8 cause primary ciliary dyskinesia (PCD), a disorder characterized by chronic respiratory infections, male infertility, and situs inversus due to impaired ciliary movement. Dysregulation of NME8 expression has also been implicated in neurodegenerative diseases such as Alzheimer?s, where it may influence axonal transport and oxidative stress. Research using NME8 antibody supports studies in ciliary biology, redox regulation, and cytoskeletal organization.NME8 antibody is validated for western blotting, immunofluorescence, and immunohistochemistry to detect ciliary structural and redox-regulating proteins. NSJ Bioreagents provides NME8 antibody reagents optimized for cell motility, developmental, and oxidative stress research.Structurally, Thioredoxin domain-containing protein 3 contains an N-terminal thioredoxin fold and multiple coiled-coil regions that mediate protein dimerization and microtubule binding. This antibody enables detailed study of NME8's role in ciliary structure and redox homeostasis.