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抗Human Superoxide dismutase copper chaperone 抗体:
抗Mouse (Murine) Superoxide dismutase copper chaperone 抗体:
抗Rat (Rattus) Superoxide dismutase copper chaperone 抗体:
Human Monoclonal Superoxide dismutase copper chaperone Primary Antibody for IP, ELISA - ABIN532559
Weisiger, Fridovich: Superoxide dismutase. Organelle specificity. in The Journal of biological chemistry 1973
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Human Monoclonal Superoxide dismutase copper chaperone Primary Antibody for ELISA, WB - ABIN532562
Kuninaka, Ichinose, Koja, Toh: Suppression of manganese superoxide dismutase augments sensitivity to radiation, hyperthermia and doxorubicin in colon cancer cell lines by inducing apoptosis. in British journal of cancer 2000
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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 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, 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, the human cytoplasm also contains Cu chaperones for loading of superoxide dismutase 1 (i.e. CCS) and cytochrome c oxidase in mitochondria (i.e. Cox17). [review]
Human cytoplasmic copper chaperones Atox1 and CCS exchange copper ions in vitro
Coexpression of hCCS in the presence of copper restores the correct maturation of the SOD1 mutants and prevents the formation of the unstructured species, confirming that hCCS also acts as a molecular chaperone.
CCS mRNA and protein levels in the serum are not correlated with inflammatory processes.
CTR1 silencing increased the protein levels of copper chaperone ATOX1 and copper chaperone for superoxide dismutase 1 (CCS-1), but decreased copper chaperone for cytochrome c oxidase (COX17).
CCS1 serves as a specialized import receptor in mitochondria that facilitates the import and folding of SOD1 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 oxidase.
The CCS mutation, p.Arg163Trp, causes reduced SOD1 activity and may impair other mechanisms important for normal Cu homeostasis.
analysis of human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)
Loss of copper chaperone for superoxide dismutase (CCS) increases amyloid-beta production in both CCS knockout neurons and CCS small-interfering (si)RNA-treated cultured tumor cells.
The results of the present study reveal the plasticity of this multi-domain chaperone in solution and are consistent with an indispensable flexibility necessary for executing its dual functions of metal binding and transfer.
CCS reduces, under non-oxidative conditions, yet facilitates in the presence of H(2)O(2), mitochondrial translocation of inactive SOD1 mutants.
Results describe the identification of the copper chaperone for superoxide dismutase as a mediator of copper delivery to XIAP in cells.
No causative mutations for amyotrophic lateral sclerosis (ALS) gene have been detected in the CCS gene in 20 sporadic ALS patients analyzed, but an intragenic single nucleotide polymorphism has been identified.
Study of site-directed cysteine-to-serine mutants of CCS suggests the formation of a domain III copper cluster within a dimeric or tetrameric protein and further suggest that this cluster may be an important element of CCS copper transfer machinery.
The copper chaperone CCS is responsible for copper insertion into apo-superoxide dismutasse 1.
A mechanism determining the abundance of CCS that is competitive with the process of copper delivery to SOD1 is described, revealing a unique post-translational component of intracellular copper homeostasis.
copper chaperone mRNA levels were reduced in peripheral mononuclear cells after copper supplementation
Measurements of hCCS-induced SOD1 activation were used to show that the C-terminal CXC sequence is both necessary and sufficient for EZn-SOD maturation.
results suggest that a SOD1 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-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 in motor neurons, but it does not modify the onset and progression of motor neuron disease in SOD1-mutant mice.
CCS-independent activation of mammalian SOD1 involves glutathione
Associated with copper deficiency were higher levels of Ccs in erythrocytes.
These results establish that CCS/G93A SOD1 mice manifest an isolated complex IV deficiency which may underlie a substantial part of mutant SOD1-induced mitochondrial cytopathy.
Study finds that as expected, CCS over-expression promotes oxidation of a wild-type SOD1 disulfide; however, in the diseased G93A/CCS mouse, there was no increased oxidation of the mutant SOD1 disulfide.
effects of copper chaperone for SOD1 on mitochondrial dysfunction are SOD1 mutation dependent and correlate with SOD1 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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