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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 Kits (12) and many more products for this protein.
Showing 10 out of 19 products:
Human CLIC4 Protein expressed in Escherichia coli (E. coli) - ABIN2005157
Rønnov-Jessen, Villadsen, Edwards, Petersen: Differential expression of a chloride intracellular channel gene, CLIC4, in transforming growth factor-beta1-mediated conversion of fibroblasts to myofibroblasts. in The American journal of pathology 2002
Show all 3 references for ABIN2005157
Human CLIC4 Protein expressed in Escherichia coli (E. coli) - ABIN667889
Malik, Shukla, Amin, Niedelman, Lee, Jividen, Phang, Ding, Suh, Curmi, Yuspa: S-nitrosylation regulates nuclear translocation of chloride intracellular channel protein CLIC4. in The Journal of biological chemistry 2010
Show all 2 references for ABIN667889
in malignant pleural mesothelioma, the gene expressions of CLIC3 (show CLIC3 Proteins) and CLIC4 were significantly increased compared to controls
CLIC1 (show CLIC1 Proteins) 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 Proteins), and Smac/DIABLO (show DIABLO Proteins) 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 Proteins)-dependent manner.
In addition to CLIC1 (show CLIC1 Proteins) and TPM1 (show TPM1 Proteins), which were the proteins initially discovered in a xenograft mouse model, CLIC4, TPM2 (show TPM2 Proteins), TPM3 (show TPM3 Proteins), and TPM4 (show TPM4 Proteins) 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.
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 Proteins) pathway.
Data suggest that iNOS (show NOS2 Proteins)-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 Proteins)-induced product that can serve as a positive regulator of LPS (show TLR4 Proteins) 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 Proteins), is increased by DNA damage and participates in the apoptotic response to p53 (show TP53 Proteins).
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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