COPZ1 Recombinant Rabbit mAb (S-4445-53)

COPZ1 is one of the seven core subunits constituting the COPI coatomer complex. As a soluble protein localized in the cytoplasm, its primary function is to serve as a "molecular coat" involved in retrograde vesicular transport from the Golgi apparatus to the endoplasmic reticulum, as well as intracellular protein trafficking. It mediates vesicle budding and cargo loading by recognizing and binding specific sorting signals (such as dilysine motifs), thereby maintaining the homeostasis of the endomembrane system. Beyond its physiological functions, COPZ1 has garnered considerable attention in cancer biology and genetic diseases: it is pharmacologically targetable and exhibits differential expression compared to COPZ2, as normal cells express both isoforms while various tumor cells rely exclusively on COPZ1 for growth and survival—therefore, targeting COPZ1 has been proposed as an anticancer strategy that specifically eliminates tumor cells, including dormant ones, with the potential to overcome tumor relapse caused by conventional antiproliferative drugs. Concurrently, autosomal recessive mutations in the COPZ1 gene (such as nonsense and missense mutations) have been found to cause a novel severe congenital neutropenia syndrome; the mutant proteins, due to weakened interactions with other subunits of the COPI complex, impair retrograde Golgi-to-ER transport, consequently disrupting key signaling pathways such as JAK/STAT and myeloid differentiation, ultimately leading to hematopoietic dysfunction characterized by neutropenia.