Anti-CEACAM6 Antibody, clone 1H7-4B clone 1H7-4B, from mouse

The carcinoembryonic antigen- (CEA-) related cell adhesion molecules (CEACAMs) constitute a 12-member subgroup of the CEA family of immunoglobulin-related proteins first described in 1965 (PMID 4953873). CEACAMs are reported to participate in diverse physiological processes, including cell adhesion, differentiation, proliferation, and survival, as well as in carcinogenesis and bacterial pathogenesis. CEACAM molecules from neighbouring cells can interact via their respective extracellular N-terminal IgV-like domain and mediate cell-cell adhesion through trans-oligomerization. CEACAM molecules within the same cell can also undergo transmembrane domain-mediated cis-oligomerization, an event important for sustaining downstream cellular signaling. Athough CEACAM1 is shown to utilize its cytoplasmic domain for transducing cellular signaling, not all CEACAM members are expressed with a significant cytoplasmic domain, and others (CEACAM5/6/7/8) are GPI-anchored without even a transmembrane domain. (PMID 4735478). Human CEACAM6 (also known as CD66c, Non-specific crossreacting antigen, Normal cross-reacting antigen; UniProt P40199) is encoded by the CEACAM6 (or CEAL & NCA) gene (NCBI Gene ID 4680). It is a GPI-anchored CEACAM with three extracellular Ig domains. Clone 1H7-4B does not cross-react with human CEACAM1/3/4/5/7/8, rat CECAM1, or mouse CEACAM1/2.