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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. Additionally we are shipping CLIC4 Antibodies (99) and CLIC4 Proteins (19) and many more products for this protein.
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CLIC1 (show CLIC1 ELISA Kits) and CLIC4 are overexpressed in specific tumor types or their corresponding stroma and change localization and function from hydrophilic cytosolic to integral transmembrane proteins. (Review)
CLIC4 knockdown decreases cell-matrix adhesion, cell spreading and integrin signaling, whereas it increases cell motility.
CLIC4, ERp29 (show ERP29 ELISA Kits), and Smac/DIABLO (show DIABLO ELISA Kits) integrated into a novel panel based on cancer stem-like cells in association with metastasis stratify the prognostic risks of colorectal cancer.
This study investigated the proteome modulated by oncogenic KRAS in immortalized airway epithelial cells.
Increased CLIC4 expression is an early manifestation and mediator of endothelial dysfunction in pulmonary hypertension.
CLIC4 increases tumor cell migration and invasion in a TGF-beta (show TGFB1 ELISA Kits)-dependent manner.
In addition to CLIC1 (show CLIC1 ELISA Kits) and TPM1 (show TPM1 ELISA Kits), which were the proteins initially discovered in a xenograft mouse model, CLIC4, TPM2 (show TPM2 ELISA Kits), TPM3 (show TPM3 ELISA Kits), and TPM4 (show TPM4 ELISA Kits) were present in ovarian cancer patient sera at significantly elevated levels compared with controls.
Our data indicate that CLIC4 protein may be a key element in the apoptotic response to oxidative stress.
These results demonstrate that CLIC4 nuclear translocation is an integral part of the cellular response to starvation.
Reduced CLIC4 expression and nuclear residence detected in cancer cells is associated with the altered redox state of tumor cells and the absence of detectable nuclear CLIC4 in cancers contributes to TGF-beta (show TGFB1 ELISA Kits) resistance and enhances tumor development.
CLIC4 is not required for collaterogenesis but is essential for perinatal maturation of nascent collaterals through a mechanism that supports VEGF signaling.
However, the absence of CLIC4 has no significant impact on the extent of functional recovery or fibrosis following acute injury.
Data suggest that compartmentalized expression of chloride intracellular channel 4 (CLIC4) in specific adult tissues and cells provides a focus to explore potential functions of this protein.
These results indicate that CLIC4 participates in skin healing and corneal wound reepithelialization through enhancement of epithelial migration by a mechanism that may involve a compromised TGF-beta (show TGFB1 ELISA Kits) pathway.
Data suggest that iNOS (show NOS2 ELISA Kits)-induced nuclear CLIC4 is an essential part of the macrophage deactivation program.
CLIC4 is required for an optimal macrophage response to diverse pathogens. CLIC4-null these findings suggest that CLIC4 is an LPS (show TLR4 ELISA Kits)-induced product that can serve as a positive regulator of LPS (show TLR4 ELISA Kits) signaling
S-nitrosylation governs CLIC4 structure, its association with protein partners, and thus its intracellular distribution
mtCLIC/CLIC4, an organellular chloride channel protein (show CLCA1 ELISA Kits), is increased by DNA damage and participates in the apoptotic response to p53 (show TP53 ELISA Kits).
mtCLIC is involved in mitochondrial membrane potential generation in mitochondrial DNA-depleted cells.
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 4 (CLIC4) protein, encoded by the CLIC4 gene, is a member of the p64 family\; the gene is expressed in many tissues and exhibits a intracellular vesicular pattern in Panc-1 cells (pancreatic cancer cells).
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