Pan-Cadherin Recombinant Rabbit Monoclonal Antibody [ST54-01] (ET1609-70)

UNIPROT #

P19022

PROTEIN NAME

Pan-Cadherin

SYNONYMS

Cadherin antibody;CDH3 antibody;CDHP antibody;7B4 antigen antibody;Cadherin-1 antibody;Cadherin-2 antibody;Cadherin-3 antibody;Cadherin-4 antibody;Cadherin-5 antibody;CAM 120/80 antibody;CD144 antibody;CD324 antibody;CD325 antibody;Cdh4 antibody;CDH5 antibody;CDHE antibody;CDHN antibody;E-cadherin antibody;Epithelial cadherin antibody;N-cadherin antibody;NCAD antibody;Neural cadherin antibody;P-cadherin antibody;Placental cadherin antibody;UVO antibody;Uvomorulin antibody;Vascular endothelial cadherin antibody

TISSUE SPECIFICITY

Non-neural epithelial tissues.

POST-TRANSLATIONAL MODIFICATION

During apoptosis or with calcium influx, cleaved by a membrane-bound metalloproteinase (ADAM10), PS1/gamma-secretase and caspase-3. Processing by the metalloproteinase, induced by calcium influx, causes disruption of cell-cell adhesion and the subsequent release of beta-catenin into the cytoplasm. The residual membrane-tethered cleavage product is rapidly degraded via an intracellular proteolytic pathway. Cleavage by caspase-3 releases the cytoplasmic tail resulting in disintegration of the actin microfilament system. The gamma-secretase-mediated cleavage promotes disassembly of adherens junctions. During development of the cochlear organ of Corti, cleavage by ADAM10 at adherens junctions promotes pillar cell separation (By similarity).; N-glycosylation at Asn-637 is essential for expression, folding and trafficking. Addition of bisecting N-acetylglucosamine by MGAT3 modulates its cell membrane location.; Ubiquitinated by a SCF complex containing SKP2, which requires prior phosphorylation by CK1/CSNK1A1. Ubiquitinated by CBLL1/HAKAI, requires prior phosphorylation at Tyr-754.; O-glycosylated. O-manosylated by TMTC1, TMTC2, TMTC3 or TMTC4. Thr-285 and Thr-509 are O-mannosylated by TMTC2 or TMTC4 but not TMTC1 or TMTC3.

SUBCELLULAR LOCATION

Cell membrane, Cell junction, Endosome, Golgi apparatus.

FUNCTION

Cadherins comprise a family of Ca2+-dependent adhesion molecules that function to mediate cell-cell binding critical to the maintenance of tissue structure and morphogenesis. The classical cadherins, E-, N- and P-cadherin, consist of large extracellular domains characterized by a series of five homologous NH₂ terminal repeats. The most distal of these cadherins is thought to be responsible for binding specificity, transmembrane domains and carboxy terminal intracellular domains. The relatively short intracellular domains interact with a variety of cytoplasmic proteins, such as -catenin, to regulate cadherin function. Members of this family of adhesion proteins include rat cadherin K (and its human homolog, cadherin, R-cadherin, B-cadherin, E/P cadherin and cadherin-5.