epitope mapping within a cytoplasmic domain of claudin-17 of human origin
Modification Notes
The claudin superfamily consists of many structurally related proteins in humans. These proteins are important structural and functional components of tight junctions in paracellular transport. Claudins are located in both epithelial and endothelial cells in all tight junction-bearing tissues. Three classes of proteins are known to localize to tight junctions, including the claudins, Occludin and Junction adhesion molecules (JAMs). Claudins, which consist of four transmembrane domains and two extracellular loops make up tight junction strands. Emerging evidence suggests that the Claudin family of proteins regulates transport through tight junctions via differential discrimination for solute size and charge. Mammalian claudin-17 and claudin-8 may be the result of a gene duplication. Claudin-17 is expressed in stratum granulosum of the epidermis and infundibulum and predominantly localizes to the plasma membrane.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of claudin-17 of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine and porcine:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope mapping within a cytoplasmic domain of claudin-17 of human origin
Tissue Specificity
epitope mapping within a cytoplasmic domain of claudin-17 of human origin
Western blot analysis of claudin-17 expression in HEK293 (A) and Jurkat (B) whole cell lysates.
Application Notes
recommended for detection of claudin-17 of mouse, rat and human origin by WB, IP, IF and ELISA also reactive with additional species, including equine, canine and porcine:
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.