epitope corresponding to amino acids 460-525 mapping within an extracellular domain of R-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 ß, to regulate cadherin function (7). R-cadherin (for retinal-cadherin, also designated cadherin-4), which was first identified in the retina of chicken, has been shown to be involved in the development of striated muscle and potentially epithelia in addition to its involvement in retinal development (8).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of R-cadherin of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine, bovine, porcine and avian:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 460-525 mapping within an extracellular domain of R-cadherin of human origin
Tissue Specificity
epitope corresponding to amino acids 460-525 mapping within an extracellular domain of R-cadherin of human origin
Western blot analysis of human recombinant R-cadherin fusion protein.
Application Notes
recommended for detection of R-cadherin of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine, bovine, porcine and avian:
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.