This website uses cookies to ensure you get the best experience on our website.
- Table of Contents
1 Citations
Facts about Claudin-16.
Required for a selective paracellular conductance. May form, alone or in partnership with other components, an intercellular pore permitting paracellular passage of calcium and magnesium ions down their electrochemical gradients.
Human | |
---|---|
Gene Name: | CLDN16 |
Uniprot: | Q9Y5I7 |
Entrez: | 10686 |
Belongs to: |
---|
claudin family |
claudin 16; Claudin16; Claudin-16; CLDN16; HOMG3; HOMG3paracellin-1; Paracellin-1; PCLN1; PCLN-1; PCLN1hypomagnesemia 3, with hypercalciuria and nephrocalcinosis
Mass (kDA):
33.836 kDA
Human | |
---|---|
Location: | 3q28 |
Sequence: | 3; NC_000003.12 (190290361..190412138) |
Kidney-specific, including the thick ascending limb of Henle (TAL).
Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.
If you are searching for anti-CLDN16 antibodies, you have come to right place. Learn more about the specificity of this antibody, its applications, and testing methods. Start your CLDN16 research by downloading your free sample. There are many options. To learn more, you can also visit Boster Bio's website. Don't miss our blog post about Boster Bio's benefits.
The CLDN16 protein is an important component to the chromatin structure within ciliary muscles. This gene code contains the information about this protein. The gene code is also known as "claudin". CLDN16 also encodes a number of other ciliary-muscle proteins. These proteins are useful in many cell biology experiments. The CLDN16 gene has a high level of conservation among ciliary muscle cells.
The western blotting is the most commonly used method for antibody detection. These methods are based on the use of secondary antibody to detect antibodies. The type of secondary antibodies used in an experiment will affect the Boster ECL chemically luminescent detection system. The secondary antibody is then added into the blot. This allows for the detection of primary antibody.
The CLDN16 genes encode an essential protein in human bones and muscles. They are required for proper splicing of premRNA. This process is disrupted by mutations in the CLDN16 genes. Numerous studies have examined the molecular as well as cellular consequences of these mutations. This information is crucial for the development and implementation of therapeutic strategies. The CLDN16 gene was amplified by PCR.
Immunostaining MDCK cells and slices of rat kidneys revealed the subcellular distributions of CLDN16. The CLDN16 anti-body was FLAG-tagged. The protein was detected using a 488nm excitation, and 543nm emission. A red channel was made from the CLDN16 signal. It was used to quantify CLDN16's fluorescence. ZO-1 was quantified using mean pixel density. ImageJ software was used in order to measure the CLDN16 as well as ZO-1 fluorescence intensity. The ZO-1 signal was then manually tagged to define the interior of the cell.
CLDN16 was previously shown to be only expressed in the TAL of Henle's loop mice and humans. CLDN16 was also associated in the TJ with STX8, a protein that was also abundant in the kidney. Anti-CLDN16 antibody increased the cytoplasmic distribution of CLDN16. This association was further validated by experiments using mice lacking the STX8 gene.
Paracellular permeation can only be achieved through the CLDN16 genes. Its role in DCT of the mouse renal is unknown. In the present study, CLDN16 was expressed at the mRNA level in the DCT, but the specific role of the protein remains unclear. It is possible that CLDN16 may be involved in the transmembrane transportation of calcium and/or phosphorus from DCT into the plasma membrane.
The CLDN16 gene encodes an interaction between the STX16 protein and a phosphoprotein. The phosphorylation site of CLDN16 was found to bind with the SNARE domain of STX8. The S217A variant was also not able to bind STX8. However, it co-localized in intracellular compartments with STX8. These results suggest that CLDN16 plays a role in regulating Mg2+ reabsorption.
The CLDN16 gene interactome is implicated in disorders that involve water, electrolytes and acid-base metabolism. CLDN16-containing epithelial cell in the TAL form a water impermeable barrier that actively transports Na+ and CI-. Paracellular pathways for selective reabsorption of Ca2+ or Mg2+ can also be provided by the CLDN16 gene. Studies have shown altered salt metabolism in mice that are CLDN16 deficient.
The CLDN16 amino acid sequence was downloaded using FASTA format from Uniprot. Its UniprotKBID is Q9Y5I7. ProtParam is used to predict CLDN16 properties. To predict the protein's properties, subcellular location, and other factors, the SignalP v.4.1 Server and the Phobius database were used. MitoProt II and Mitofates were used to identify mitochondrial targeting sequences and phosphorylation sites.
Primary hypomagnesemia (a condition characterized in massive magnesium wasting) has been linked with the CLDN16 mutation. Mutations in this gene have been linked with altered intracellular transportation, subcellular locization, and pore formation functions. To determine the role CLDN16 plays in the cytoplasmic space, scientists analysed CLDN16 protein and processed nucleotide information in 14 databases. This allowed them to examine the subcellular location of CLDN16.
CLDN6/CLDN10 expression is negatively associated with gene markers of dendritic cells, monocytes, and NK cells in ovarian carcinoma. These markers are negatively correlated generally with gene markers NK cells and T cell markers. However, their negative correlations to other immune cell subsets of ovarian cancer suggests that CLDN6 & CLDN10 do not exist in isolation.
We have created new tests to test the CLDN16 mark by fusing an Nterminal FLAG tag with a mutant CLDN16-coding gene. These mutants were expressed using Madin-Darby canine kidney cell cells and characterized with immunoblotting using an anti FLAG antibody. These mutations did not affect the expression of any other endogenous junctional protein, such as CLDN1, CLDN2, CLDN4, and CLDN19.
Two databases were used to design an assay for the CLDN16 protein. To predict the protein’s secondary and phosphorylation site structures, we used two databases: the DISPHOS 1.3 DB and the PSIPRED v.3.3 DB. We also chose transport for a functional classification and used DISOPRED2 as a database to determine its disorder. The CLDN16 mark has been identified by DISOPRED2 to be a novel, highly predicted protein. MitoProt also predicts it.
We performed immunofluorescence analyses on cell samples containing mutant or WT CLDN16. The immunofluorescence assays revealed that the WT CLDN16 genes were more abundant than those of the mutant, and primaquine had no effect. We also looked at the effects of primoquine on transepithelial magnesium and ter in WT and T303R cell lines.
Mutations in CLDN16 impair paracellular ion transport and reduce its ability to localize to TJs. The study also showed that CLDN16 mutations affect the localization and distribution of magnesium in the kidney. These findings suggest CLDN16 could contribute to chronic kidney disease. This condition can lead to the need for renal transplantation. Moreover, mutations at the BSND gene can be linked to the CLDN16 intergenerational gene network.
The CLDN16 gene is coded by the CLDN16 genes. The UCSC Genome Browser can help you locate the CLDN16 gene within the human genome. In addition to gene expression, CLDN16 has multiple possible interactions with many other genes. The transcription and posttranscriptional levels may be heavily regulated by the CLDN16 gene. Therefore, CLDN16 testing will help determine if the gene is active.
CLDN16 protein is found within the tight junctions and cells of the kidney epithelial cells. A different clinical phenotype may be possible if CLDN16 mutations affect ZO1. This suggests that the CLDN16 gene could be involved in other kidney diseases. It will be difficult to treat this disease, but it is worth the effort of understanding the potential implications of its mutations.
PMID: 10390358 by Simon D.B., et al. Paracellin-1, a renal tight junction protein required for paracellular Mg2+ resorption.
PMID: 10878661 by Weber S., et al. Familial hypomagnesaemia with hypercalciuria and nephrocalcinosis maps to chromosome 3q27 and is associated with mutations in the PCLN-1 gene.
*More publications can be found for each product on its corresponding product page