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Copper chaperone for superoxide dismutase specifically delivers Cu to copper/zinc superoxide dismutase and may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor. Additionally we are shipping Superoxide dismutase copper chaperone Antibodies (57) and Superoxide dismutase copper chaperone Kits (10) and many more products for this protein.
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Human Superoxide dismutase copper chaperone Protein expressed in Escherichia coli (E. coli) - ABIN667211
Romerius, Ståhl, Moëll, Relander, Cavallin-Ståhl, Gustafsson, Löfvander Thapper, Jepson, Spanò, Wiebe, Lundberg Giwercman, Giwercman: Sperm DNA integrity in men treated for childhood cancer. in Clinical cancer research : an official journal of the American Association for Cancer Research 2010
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Data indicate that transgenic plants expressing miR398-resistant forms of CSD1, CSD2 (show TGFB1 Proteins) and CCS under the control of their native promoters are more sensitive to heat stress.
miR398 links expression of the three major chloroplast copper proteins, plastocyanin, CCS1 and Csd2 (show TGFB1 Proteins), to copper availability.
CCS1 gene encodes both a cytosolic and a chloroplastic form of CCS1. miR398 directs the post-transcriptional regulation of CCS1 mRNAs by cleavage and AGO10-mediated translational repression. [CCS1]
Arabidopsis thaliana gene AtCCS encodes a functional homolog to yeast Ccs1p/Lys7p, a copper chaperone for SOD [AtCCS]
The structure and function of the CCS gene of A. thaliana, including its copper and protein binding domains, are reported.
In addition to Atox1 (show ATOX1 Proteins), the human cytoplasm also contains Cu chaperones for loading of superoxide dismutase 1 (show SOD1 Proteins) (i.e. CCS) and cytochrome c (show CYCS Proteins) oxidase in mitochondria (i.e. Cox17 (show COX17 Proteins)). [review]
Human cytoplasmic copper chaperones Atox1 (show ATOX1 Proteins) and CCS exchange copper ions in vitro
Coexpression of hCCS (show HCCS Proteins) in the presence of copper restores the correct maturation of the SOD1 (show SOD1 Proteins) mutants and prevents the formation of the unstructured species, confirming that hCCS (show HCCS Proteins) also acts as a molecular chaperone (show HSP90AA1 Proteins).
CCS mRNA and protein levels in the serum are not correlated with inflammatory processes.
CTR1 (show SLC31A1 Proteins) silencing increased the protein levels of copper chaperone ATOX1 (show ATOX1 Proteins) and copper chaperone for superoxide dismutase 1 (show SOD1 Proteins) (CCS-1), but decreased copper chaperone for cytochrome c (show CYCS Proteins) oxidase (COX17 (show COX17 Proteins)).
CCS1 serves as a specialized import receptor in mitochondria that facilitates the import and folding of SOD1 (show SOD1 Proteins) and CCS1.
CCS-dependent copper acquisition and distribution largely occur at membrane interfaces and that this emerging role of the bilayer may reflect a general mechanistic aspect of cellular transition metal ion acquisition.
CCS-1 facilitates copper trafficking to the mitochondria, but does not affect the transfer of copper to the cytochrome c (show CYCS Proteins) oxidase.
The CCS mutation, p.Arg163Trp, causes reduced SOD1 (show SOD1 Proteins) activity and may impair other mechanisms important for normal Cu homeostasis.
analysis of human superoxide dismutase 1 (hSOD1 (show SOD1 Proteins)) maturation through interaction with human copper chaperone for SOD1 (hCCS (show HCCS Proteins))
results suggest that a SOD1 (show SOD1 Proteins) supplement to healthy mice may not be necessary to modulate cell proliferation and neuroblast differentiation in the dentate gyrus
Small interfering RNA (siRNA) targeting CCS was introduced into metallothionein (show MT Proteins)-knockout mouse fibroblasts (MT-KO cells) and their wild type cells (MT-WT cells) to reveal the interactive role of CCS with other Cu-regulating proteins.
CCS is necessary for the efficient incorporation of copper into SOD1 (show SOD1 Proteins) in motor neurons, but it does not modify the onset and progression of motor neuron disease in SOD1 (show SOD1 Proteins)-mutant mice.
CCS-independent activation of mammalian SOD1 (show SOD1 Proteins) involves glutathione
Associated with copper deficiency were higher levels of Ccs in erythrocytes.
A mechanism determining the abundance of CCS that is competitive with the process of copper delivery to SOD1 (show SOD1 Proteins) is described, revealing a unique post-translational component of intracellular copper homeostasis.
These results establish that CCS/G93A SOD1 (show SOD1 Proteins) mice manifest an isolated complex IV deficiency which may underlie a substantial part of mutant SOD1 (show SOD1 Proteins)-induced mitochondrial cytopathy.
Study finds that as expected, CCS over-expression promotes oxidation of a wild-type SOD1 (show SOD1 Proteins) disulfide; however, in the diseased G93A/CCS mouse, there was no increased oxidation of the mutant SOD1 (show SOD1 Proteins) disulfide.
effects of copper chaperone for SOD1 on mitochondrial dysfunction are SOD1 (show SOD1 Proteins) mutation dependent and correlate with SOD1 (show SOD1 Proteins) redox susceptibility
Copper chaperone for superoxide dismutase specifically delivers Cu to copper/zinc superoxide dismutase and may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.
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