Recognizes a protein of 480kDa, which is identified as FAT2. The cadherins represent a family of Ca2+-dependent adhesion molecules that function to mediate cell-to-cell binding that is critical for the maintenance of structure and morphogenesis. Cadherins each contain a large extracellular domain at the N-terminus, which is characterized by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity. The relatively short C-terminal intracellular domain interacts with a variety of cytoplasmic proteins, including β-catenin, to regulate cadherin function. The cadherin superfamily includes cadherins, protocadherins, desmogleins and desmocollins. FAT2 (FAT tumor suppressor homolog 2) is a single-pass type I membrane protein that belongs to the protocadherin subfamily of cadherins. FAT2 contains one Laminin G-like domain, two EGF-like domains and 32 cadherin domains and is believed to function as a cell adhesion molecule, controlling cell proliferation and playing an important role in cerebellum development.

Titering of the FAT2 antibody may be required for optimal performance.

A recombinant human Protocadherin Fat 2 fusion protein was used as the immunogen for this FAT2 antibody.

The FAT2 antibody (with azide) can be stored at 2-8oC. The azide-free format should be aliquoted and stored at -20oC or colder.