CLIC1 Mouse Monoclonal Antibody
- Known as:
- CLIC1 Mouse Monoclonal Antibody
- Catalog number:
- BIN-001192-M01
- Product Quantity:
- 0.1mg
- Category:
- -
- Supplier:
- Zyagen
- Gene target:
- CLIC1 Mouse Monoclonal Antibody
Related genes to: CLIC1 Mouse Monoclonal Antibody
- Gene:
- CLIC1 NIH gene
- Name:
- chloride intracellular channel 1
- Previous symbol:
- -
- Synonyms:
- NCC27, p64CLCP, G6
- Chromosome:
- 6p21.33
- Locus Type:
- gene with protein product
- Date approved:
- 1997-07-01
- Date modifiied:
- 2016-12-09
- Gene:
- CLIC6 NIH gene
- Name:
- chloride intracellular channel 6
- Previous symbol:
- CLIC1L
- Synonyms:
- CLIC5
- Chromosome:
- 21q22.12
- Locus Type:
- gene with protein product
- Date approved:
- 2000-05-23
- Date modifiied:
- 2015-08-28
Related products to: CLIC1 Mouse Monoclonal Antibody
Related articles to: CLIC1 Mouse Monoclonal Antibody
- The chloride intracellular channels (CLICs) engage in cancer pathogenesis and have been considered various cancer biomarkers and therapeutic targets. Preliminary research suggests CLICs may be important players in head and neck squamous cell carcinoma (HNSCC). There is a need for reliable HNSCC biomarkers besides well-known HPV and PD-L1. - Source: PubMed
Publication date: 2025/10/24
Wojtera Bartosz PawełOstrowska KamilaOstapowicz JuliaSzewczyk MateuszKozikowska JuliaSuchorska Wiktoria MariaGolusiński Wojciech - The chloride intracellular channels (CLICs) family includes six ion channels (CLIC1-CLIC6) expressed on the cellular level and secreted into interstitial fluid and blood. They are involved in the physiological functioning of multiple systems as well as the pathogenetic processes of cancer. CLICs play essential roles in the tumor microenvironment. The current systematic review aimed at identifying and summarizing the research of CLICs in oncology on clinical material to assess CLICs' potential as novel biomarkers and personalized therapy targets. - Source: PubMed
Publication date: 2024/06/06
Wojtera BartoszOstrowska KamilaSzewczyk MateuszMasternak Michał MGolusiński Wojciech - Pancreatic ductal adenocarcinoma (PDAC) is associated with poor prognosis. In this context, the identification of biomarkers regarding the PDAC diagnosis, monitoring, and prognosis is crucial. - Source: PubMed
Magouliotis Dimitrios ESakellaridis NikosDimas KonstantinosTasiopoulou Vasiliki SSvokos Konstantina ASvokos Alexis AZacharoulis Dimitris - Five members of the newly identified chloride intracellular channel (CLIC) gene family of intracellular chloride channels (CLIC1-CLIC5) have previously been described in humans. Here we report the molecular cloning and initial characterisation of two splice forms of a novel member of this family, CLIC6, mapping to human chromosome 21. Two essential features distinguish CLIC6 from other members of the family. The CLIC6 protein is significantly longer and the CLIC6 gene contains a GC rich segment, which encodes a 10 amino acid motif repeated 14 times in the amino-terminus. Surprisingly, the repeat is conserved in the lagomorphs, but not in the rodents lineage. The putative bovine orthologue of CLIC5, p64, also exhibits a repeated motif, which is different from that of CLIC6. Attempts to functionally characterise CLIC6 by voltage clamp failed to show any chloride channel activity. Hence, the exact function of this protein remains unknown. - Source: PubMed
Friedli MarcGuipponi MichelBertrand SoniaBertrand DanielNeerman-Arbez MargueriteScott Hamish SAntonarakis Stylianos EReymond Alexandre - Parchorin, p64 and the related chloride intracellular channel (CLIC) proteins are widely expressed in multicellular organisms and have emerged as candidates for novel, auto-inserting, self-assembling intracellular anion channels involved in a wide variety of fundamental cellular events including regulated secretion, cell division and apoptosis. Although the mammalian phosphoproteins p64 and parchorin (49 and 65K, respectively) have only been indirectly implicated in anion channel activity, two CLIC proteins (CLIC1 and CLIC4, 27 and 29K, respectively) appear to be essential molecular components of anion channels, and CLIC1 can form anion channels in planar lipid bilayers in the absence of other cellular proteins. However, these putative ion channel proteins are controversial because they exist in both soluble and membrane forms, with at least one transmembrane domain. Even more surprisingly, soluble CLICs share the same glutaredoxin fold as soluble omega class glutathione-S-transferases. Working out how these ubiquitous, soluble proteins unfold, insert into membranes and then refold to form integral membrane proteins, and how cells control this potentially dangerous process and make use of the associated ion channels, are challenging prospects. Critical to this future work is the need for better characterization of membrane topology, careful functional analysis of reconstituted and native channels, including their conductances and selectivities, and detailed structure/function studies including targeted mutagenesis to investigate the structure of the putative pore, the role of protein phosphorylation and the role of conserved cysteine residues. - Source: PubMed
Ashley R H