Immobilized Recombinant Human CEACAM-20 Fc Chimera (Catalog #9427-CM) enhances L Cells mouse fibroblasts adhesion. The ED50 for this effectis 0.5-2.5 μg/mL.
Carcinoembryonic antigen-related cell adhesion molecule-20
(CEACAM-20) is a member of the CEACAM subfamily of glycoproteins in the immunoglobulin
(Ig) superfamily. Mature human CEACAM-20 consists of a 420 aa extracellular
domain, a 21 aa helical transmembrane, and a 114 aa cytoplasmic domain. The
extracellular domain possesses four IgC2-like domains, which are
stabilized by disulfide bonds, as well as several predicted glycosylation sites
(1-5). The extracellular domain of CEACAM-20 is also unique among the CEACAMs
because it contains a truncated IgV-like N domain (2). The
extracellular domain of human CEACAM-20 has 64% and 62% aa identity to the
mouse and rat protein, respectively. Also, the cytoplasmic domain is unusually
long compared to most other CEACAMs and is predicted to contain four tyrosine
phosphorylation sites, two of which correspond to the immune-receptor
tyrosine-based activation motif (ITAM) (2, 3). Human CEACAM proteins have been
linked to numerous intercellular-adhesion and intracellular signaling processes
including cell adhesion, growth, and recognition, differentiation,
angiogenesis, and apoptosis (7, 8). Human CEACAM-20 expression is limited to the
reproductive system and the intestinal tract, with the highest levels of expression
found in the small intestine and prostate (2, 3). An in vitro model of human prostate morphogenesis showed that
CEACAM-20 is co-expressed with CEACAM-1 and plays a critical role in the
formation of prostate organoids, making it a marker for prostate cancer (2). Although
the exact mechanism is not fully understood, CEACAM-20 may promote the
proliferation of intestinal epithelial cells (IECs) (9). There is evidence suggesting
CEACAM-20 can induce the production of chemokines like interleukin (IL)-8 and
stimulate inflammatory responses in colitis and Crohn's disease (6). CEACAM-20
is also thought be act as a physiological substrate for SAP-1 in the intestinal
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