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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 Proteins (14) and Superoxide dismutase copper chaperone Kits (10) and many more products for this protein.
Showing 10 out of 57 products:
Arabidopsis thaliana Polyclonal Superoxide dismutase copper chaperone Primary Antibody for WB - ABIN190735
Abdel-Ghany, Burkhead, Gogolin, Andrés-Colás, Bodecker, Puig, Peñarrubia, Pilon: AtCCS is a functional homolog of the yeast copper chaperone Ccs1/Lys7. in FEBS letters 2005
Show all 2 references for ABIN190735
Human Monoclonal Superoxide dismutase copper chaperone Primary Antibody for IF, IHC (p) - ABIN523352
Spinazzi, Sghirlanzoni, Salviati, Angelini: Impaired copper and iron metabolism in blood cells and muscles of patients affected by copper deficiency myeloneuropathy. in Neuropathology and applied neurobiology 2014
Data indicate that transgenic plants expressing miR398-resistant forms of CSD1, CSD2 (show TGFB1 Antibodies) 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 Antibodies), 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 Antibodies), the human cytoplasm also contains Cu chaperones for loading of superoxide dismutase 1 (show SOD1 Antibodies) (i.e. CCS) and cytochrome c (show CYCS Antibodies) oxidase in mitochondria (i.e. Cox17 (show COX17 Antibodies)). [review]
Human cytoplasmic copper chaperones Atox1 (show ATOX1 Antibodies) and CCS exchange copper ions in vitro
Coexpression of hCCS (show HCCS Antibodies) in the presence of copper restores the correct maturation of the SOD1 (show SOD1 Antibodies) mutants and prevents the formation of the unstructured species, confirming that hCCS (show HCCS Antibodies) also acts as a molecular chaperone (show HSP90AA1 Antibodies).
CCS mRNA and protein levels in the serum are not correlated with inflammatory processes.
CTR1 (show SLC31A1 Antibodies) silencing increased the protein levels of copper chaperone ATOX1 (show ATOX1 Antibodies) and copper chaperone for superoxide dismutase 1 (show SOD1 Antibodies) (CCS-1), but decreased copper chaperone for cytochrome c (show CYCS Antibodies) oxidase (COX17 (show COX17 Antibodies)).
CCS1 serves as a specialized import receptor in mitochondria that facilitates the import and folding of SOD1 (show SOD1 Antibodies) 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 Antibodies) oxidase.
The CCS mutation, p.Arg163Trp, causes reduced SOD1 (show SOD1 Antibodies) activity and may impair other mechanisms important for normal Cu homeostasis.
analysis of human superoxide dismutase 1 (hSOD1 (show SOD1 Antibodies)) maturation through interaction with human copper chaperone for SOD1 (hCCS (show HCCS Antibodies))
results suggest that a SOD1 (show SOD1 Antibodies) 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 Antibodies)-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 Antibodies) in motor neurons, but it does not modify the onset and progression of motor neuron disease in SOD1 (show SOD1 Antibodies)-mutant mice.
CCS-independent activation of mammalian SOD1 (show SOD1 Antibodies) 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 Antibodies) is described, revealing a unique post-translational component of intracellular copper homeostasis.
These results establish that CCS/G93A SOD1 (show SOD1 Antibodies) mice manifest an isolated complex IV deficiency which may underlie a substantial part of mutant SOD1 (show SOD1 Antibodies)-induced mitochondrial cytopathy.
Study finds that as expected, CCS over-expression promotes oxidation of a wild-type SOD1 (show SOD1 Antibodies) disulfide; however, in the diseased G93A/CCS mouse, there was no increased oxidation of the mutant SOD1 (show SOD1 Antibodies) disulfide.
effects of copper chaperone for SOD1 on mitochondrial dysfunction are SOD1 (show SOD1 Antibodies) mutation dependent and correlate with SOD1 (show SOD1 Antibodies) 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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