Recombinant Human CLIC4 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1322

Recombinant Human CLIC4 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-1322
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Product Overview

Tag His
Host Species Human
Accession Q9Y696
Synonym CLIC4L, H1, huH1, MTCLIC, p64H1
Background Chloride intracellular channel protein 4, also known as Intracellular chloride ion channel protein p64H1 and CLIC4, is a member of the chloride channel CLIC family. It contains oneGST C-terminal domain. CLIC4 is a member of a family of intracellular chloride channels. It is regulated by p53, c-Myc, and tumor necrosis factor-alpha. CLIC4 is detected in epithelial cells from colon, esophagus and kidney (at protein level). CLIC4 has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. CLIC4 could promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis). Expression of CLIC4 is prominent in heart, kidney, placenta and skeletal muscle. Overexpression of CLIC4 in cancer cells inhibits tumor growth. Conversely, overexpression of CLIC4 in tumor stromal cells stimulates tumor growth. Thus, CLIC4 participates in normal and pathological processes and may serve as a useful target for therapies in disturbances of homeostasis and neoplastic transformation. Loss of CLIC4 in tumor cells and gain in tumor stroma is common to many human cancers and marks malignant progression. Up-regulation of CLIC4 in tumor stroma is coincident with myofibroblast conversion, generally a poor prognostic indicator. Reactivation and restoration of CLIC4 in tumor cells or the converse in tumor stromal cells could provide a novel approach to inhibit tumor growth.
Description A DNA sequence encoding the human CLIC4 (Q9Y696-1) (Ala 2-Lys 253) was expressed, with a His tag at the N-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Ala 2-Lys 253
Molecular Weight The recombinant human CLIC4 consisting of 263 a.a. and migrates as an 30 kDa band in SDS-PAGE under reducing conditions as predicted.
Purity >97% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Can insert into membranes and form poorly selective ion channels that may also transport chloride ions. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Promotes cell-surface expression of HRH3. Has alternate cellular functions like a potential role in angiogenesis or in maintaining apical-basolateral membrane polarity during mitosis and cytokinesis. Could also promote endothelial cell proliferation and regulate endothelial morphogenesis (tubulogenesis).
Subcellular Location Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasmic vesicle membrane; Single-pass membrane protein. Nucleus matrix. Cell membrane; Single-pass membrane protein. Mitochondrion. Cell junction. Note=Colocalized with AKAP9 at the centrosome and midbody. Exists both as soluble cytoplasmic protein and as membrane protein with probably a single transmembrane domain. Present in an intracellular vesicular compartment that likely represent trans-Golgi network vesicles.
Protein Families Chloride channel CLIC family
Database References
Tissue Specificity Detected in epithelial cells from colon, esophagus and kidney (at protein level). Expression is prominent in heart, kidney, placenta and skeletal muscle.

Gene Functions References

  1. Results provide evidence that the G4 structure formed in the CLIC4 promoter region may act as a regulatory element in regulating CLIC4 gene transcription. PMID: 30201851
  2. CLIC4 and Ihh could serve as biological markers for the progression, metastasis and/or invasiveness of pancreatic ductal adenocarcinoma. PMID: 28205343
  3. in malignant pleural mesothelioma, the gene expressions of CLIC3 and CLIC4 were significantly increased compared to controls PMID: 26445368
  4. CLIC1 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) PMID: 25546839
  5. CLIC4 knockdown decreases cell-matrix adhesion, cell spreading and integrin signaling, whereas it increases cell motility. PMID: 25344254
  6. This study investigated the proteome modulated by oncogenic KRAS in immortalized airway epithelial cells. PMID: 24503901
  7. Increased CLIC4 expression is an early manifestation and mediator of endothelial dysfunction in pulmonary hypertension. PMID: 24503951
  8. CLIC4 increases tumor cell migration and invasion in a TGF-beta-dependent manner. PMID: 23416981
  9. In addition to CLIC1 and TPM1, which were the proteins initially discovered in a xenograft mouse model, CLIC4, TPM2, TPM3, and TPM4 were present in ovarian cancer patient sera at significantly elevated levels compared with controls. PMID: 23792823
  10. Our data indicate that CLIC4 protein may be a key element in the apoptotic response to oxidative stress. PMID: 23380911
  11. These results demonstrate that CLIC4 nuclear translocation is an integral part of the cellular response to starvation. PMID: 22761775
  12. 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 resistance and enhances tumor development. PMID: 22387366
  13. CLIC4 may not be responsible for benign familial infantile seizures (BFIS) in a Chinese family affected with BFIS. PMID: 20374090
  14. Data suggest that CLIC4 is regulated by RhoA to be targeted to the plasma membrane, where it may function not as an inducible chloride channel but rather by displaying Cys-dependent transferase activity toward a yet unknown substrate. PMID: 19776349
  15. CLIC4 functions to promote endothelial cell proliferation and to regulate endothelial morphogenesis, and is thus involved in multiple steps of in vitro angiogenesis. PMID: 19247789
  16. CLIC4 is differentially regulated in fibroblasts and its expression contributes to a myofibroblast phenotype PMID: 12163372
  17. CLIC4 has alternate cellular functions that are distinct from their proposed roles as chloride channels PMID: 14569596
  18. subcellular localization of CLIC4 in endothelial cells was dependent on whether cells were engaged in proliferation or tube formation PMID: 16239224
  19. up-regulation of mitochondrial CLIC4, together with a reduction in Bcl-2 and Bcl-xL, sensitizes Myc-expressing cells to the proapoptotic action of Bax. PMID: 16316993
  20. preliminary crystallographic analysis PMID: 16842122
  21. CLIC4 in tumor stroma has a role in myofibroblast conversion in human neoplasms PMID: 17200346
  22. Nuclear CLIC4, possibly by altering the Cl(-) and pH of the nucleus, contributes to cell cycle arrest and the specific gene expression program associated with keratinocyte terminal differentiation. PMID: 17636002
  23. Data showed that CLIC1 and CLIC5, but not CLIC4, were strongly and reversibly inhibited (or inactivated) by F-actin. PMID: 18028448
  24. ROS-initiated CLIC4 up-regulation is required for TGF-beta1-induced fibroblast-to-myofibroblast transdifferentiaton in ovarian cancer. PMID: 19639201
  25. S100A4 and bone morphogenetic protein-2 codependently induce vascular smooth muscle cell migration via phospho-extracellular signal-regulated kinase and chloride intracellular channel 4. PMID: 19713532


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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