CLDN16 (claudin 16)

GWB-E78860

Synthetic peptide sequence derived from: FLAGAVLTCCLYLFKDVGPERNYPYSLRKAYSAAGVSMAKSYSAPRTETA

0. 5ug/ml

Suggested starting concentrations are provided. Optimal dilutions should be determined by end-user. Differences in calculated versus apparent molecular weight may be due to post-translational modifications or protein hydrophobicity. Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. These junctions are comprised of sets of continuous networking strands in the outwardly facing cytoplasmic leaflet with complementary grooves in the inwardly facing extracytoplasmic leaflet. Claudin-16 a member of the claudin family is an integral membrane protein and a component of tight junction strands. It is found primarily in the kidneys specifically in the thick ascending limb of Henle where it acts as either an intercellular pore or ion concentration sensor to regulate the paracellular resorption of magnesium ions. Defects in the corresponding gene are a cause of primary hypomagnesemia which is characterized by massive renal magnesium wasting with hypomagnesemia and hypercalciuria resulting in nephrocalcinosis and renal failure. Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. These junctions are comprised of sets of continuous networking strands in the outwardly facing cytoplasmic leaflet with complementary grooves in the inwardly facing extracytoplasmic leaflet. The protein encoded by this gene a member of the claudin family is an integral membrane protein and a component of tight junction strands. It is found primarily in the kidneys specifically in the thick ascending limb of Henle where it acts as either an intercellular pore or ion concentration sensor to regulate the paracellular resorption of magnesium ions. Defects in this gene are a cause of primary hypomagnesemia which is characterized by massive renal magnesium wasting with hypomagnesemia and hypercalciuria resulting in nephrocalcinosis and renal failure. Publication

Plays a major role in tight junction-specific obliteration of the intercellular space through calcium-independent cell-adhesion activity. Involved in paracellular magnesium reabsorption. Required for a selective paracellular conductance. May form alone or in partnership with other constituents an intercellular pore permitting paracellular passage of magnesium and calcium ions down their electrochemical gradients. Alternatively it could be a sensor of magnesium concentration that could alter paracellular permeability mediated by other factors.

Kidney-specific including the thick ascending limb of Henle (TAL).

Belongs to the claudin family. Summary: Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. These junctions are comprised of sets of continuous networking strands in the outwardly facing cytoplasmic leaflet with complementary grooves in the inwardly facing extracytoplasmic leaflet. The protein encoded by this gene a member of the claudin family is an integral membrane protein and a component of tight junction strands. It is found primarily in the kidneys specifically in the thick ascending limb of Henle where it acts as either an intercellular pore or ion concentration sensor to regulate the paracellular resorption of magnesium ions. Defects in this gene are a cause of primary hypomagnesemia which is characterized by massive renal magnesium wasting with hypomagnesemia and hypercalciuria resulting in nephrocalcinosis and renal failure. Muller. D. . et al. . (2003) Am. J. Hum. Genet. 73 (6). 1293-1301.