epitope corresponding to amino acids 666-832 mapping at the C-terminus of LI-cadherin of human origin
Modification Notes
The cadherins are a family of Ca++-dependent adhesion molecules that function to mediate cell-cell binding critical to the maintenance of tissue structure and morphogenesis (1-4). Cadherins each contain a large extracellular domain at the amino terminus, which is characterized by a series of five homologous repeats, the most distal of which is thought to be responsible for binding specificity (5,6). The relatively short carboxy terminal, intracellular domain interacts with a variety of cytoplasmic proteins, including catenin b, to regulate cadherin function (7). LI-cadherin (for liver-intestine-cadherin) expression is restricted to liver and intestine tissues and is specifically localized to the basolateral domain of hepatocytes and enterocytes (8).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of LI-cadherin of mouse, rat and human origin by WB, IP, IF and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 666-832 mapping at the C-terminus of LI-cadherin of human origin
Tissue Specificity
epitope corresponding to amino acids 666-832 mapping at the C-terminus of LI-cadherin of human origin