CLIC1 Antibody - #DF13985
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Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Fold/Unfold
Chloride channel ABP; Chloride intracellular channel 1; Chloride intracellular channel protein 1; CLIC 1; CLIC1; CLIC1_HUMAN; G6; hRNCC; NCC 27; NCC27; Nuclear chloride ion channel 27; Nuclear chloride ion channel protein; p64CLCP; Regulatory nuclear chloride ion channel protein; RNCC protein;
Immunogens
A synthesized peptide derived from Human CLIC1.
- O00299 CLIC1_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGVSQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKALK
Research Backgrounds
Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle.
Hydrogen peroxide treatment causes a conformation change, leading to dimerization and formation of an intramolecular disulfide bond between Cys-24 and Cys-59.
Nucleus. Nucleus membrane>Single-pass membrane protein. Cytoplasm. Cell membrane>Single-pass membrane protein.
Note: Mostly in the nucleus including in the nuclear membrane (PubMed:9139710, PubMed:12681486). Small amount in the cytoplasm and the plasma membrane (PubMed:9139710). Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain (PubMed:11940526, PubMed:11551966, PubMed:14613939).
Expression is prominent in heart, placenta, liver, kidney and pancreas.
Monomer. Homodimer (in vitro). Interacts with TRAPPC2. Dimerization requires a conformation change that leads to the exposure of a large hydrophobic surface. In vivo, this may lead to membrane insertion. Interacts with AKAP9.
Members of this family may change from a globular, soluble state to a state where the N-terminal domain is inserted into the membrane and functions as chloride channel. A conformation change of the N-terminal domain is thought to expose hydrophobic surfaces that trigger membrane insertion.
Belongs to the chloride channel CLIC family.
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