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Validated All-in-One™ qPCR Primer for CLIC1(NM_001287594.3) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
Chloride channels are a diverse group of proteins that regulate fundamental cellular processes including stabilization of cell membrane potential, transepithelial transport, maintenance of intracellular pH, and regulation of cell volume. Chloride intracellular channel 1 is a member of the p64 family; the protein localizes principally to the cell nucleus and exhibits both nuclear and plasma membrane chloride ion channel activity. [provided by RefSeq].
Gene References into function
- NCC27 (CLIC1) is a 27 kDa intracellular ion channel localized to the nucleus and cytoplasm that exists in both a soluble and integral membrane form
- By selectively tagging either N- or C-termini of NCC27 (CLIC1) and varying the side of the membrane from which channel activity is recorded, NCC27 can be seen to be a TM protein forming part of an ion channel.
- NCC27 (CLIC1) is broadly expressed and highly conserved. NCC27 blockers led to arrest of CHO-K1 cells in the G2/M stage of the cell cycle, the same stage at which this ion channel is selectively expressed on the plasma membrane
- The soluble form of CLIC1 has been determined at 1.4-A resolution. The protein is monomeric and structurally homologous to the glutathione S-transferase superfamily, and it has a redox-active site resembling glutaredoxin.
- Soluble E. coli-derived recombinant CLIC1 moves from solution into artificial bilayers and forms chloride-selective ion channels with essentially identical properties to those observed in CLIC1-transfected CHO cells.
- The structure of oxidized CLIC1 has been determined. The oxidized CLIC1 dimer maintains its ability to form chloride ion channels in artificial bilayers and vesicles, whereas a reducing environment prevents the formation of ion channels by CLIC1
- on oxidation CLIC1 undergoes a reversible transition from a monomeric to a non-covalent dimeric state due to the formation of an intramolecular disulfide bond (Cys-24-Cys-59)
- Amyloid-b stimulation of neonatal rat microglia increases CLIC1 protein and functional expression of CLIC1 chloride conductance. Blocking CLIC1 or reducing it by siRNA in amyloid-b treated microglia cocultured with neurons inhibits neurotoxicity
- insulin induces the proteasome-dependent degradation of SRp20 as well as the subnuclear relocalization of CLIC1
- In certain polarized columnar epithelia, CLIC1 may play a role in apical membrane recycling.
- CFTR confers cAMP regulation to CLIC1 activity in the plasma membrane
- Data showed that CLIC1 and CLIC5, but not CLIC4, were strongly and reversibly inhibited (or inactivated) by F-actin.
- CLIC1 and TPD52 were significantly (P<0.05) up-regulated in all cases of colorectal cancer investigated, irrespective of localization, pTNM stage and grade of colon cancer.
- Acid-induced destabilization and partial unfolding of CLIC1 involve helix alpha1 which is the major structural element of the transmembrane region.