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The protein encoded by ISCA2 is an A-type iron-sulfur cluster (ISC) protein found in mitochondria. Additionally we are shipping Iron-Sulfur Cluster Assembly 2 Homolog (S. Cerevisiae) Antibodies (47) and and many more products for this protein.
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We identified a homoallelic missense founder mutation in ISCA2 leading to mitochondrial depletion and reduced complex I activity as well as decreased ISCA2, ISCA1 and IBA57 expression in fibroblasts.
The structural plasticity of the dimeric state of the [2Fe-2S] bound form of human GRX5 is the crucial factor that allows an efficient cluster transfer to the partner proteins human ISCA1 and ISCA2 by a specific protein-protein recognition mechanism.
ISCA1, ISCA2, and IBA57 were depleted by RNA interference. Depleted cells contained massively swollen and enlarged mitochondria that were virtually devoid of cristae membranes, demonstrating the importance of these proteins for mitochondrial biogenesis.
The data suggest that cellular processes with different requirements for ISCA1, ISCA2 and ISCA1-ISCA2 complex seem to exist.
Data suggest that miR-210 induced repression of ISCU1/2 may contribute to HIF-1alpha-triggered alterations in neuronal energy metabolism after nickel exposure.
The protein encoded by this gene is an A-type iron-sulfur cluster (ISC) protein found in mitochondria. The encoded protein appears to be involved in the maturation of mitochondrial iron-sulfur proteins. Two transcript variants encoding different isoforms have been found for this gene.
HESB-like domain-containing protein 1
, iron-sulfur cluster assembly 2 homolog, mitochondrial
, HESB like domain containing 1
, iron-sulfur cluster assembly 2 homolog