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Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria.. De plus, nous expédions HSCB Anticorps (21) et HSCB Kits (4) et beaucoup plus de produits pour cette protéine.
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Cytosolic HSC20 is indispensable for cytoplasmic Fe-S assembly and delivery, which is initiated de novo in the cytosol.
Nfu is shown to bind to both chaperone proteins with binding affinities similar to those observed for IscU binding to the homologous HSPA9 and Hsc20, while Nfu can also stimulate the ATPase activity of HSPA9
The delivery of assembled Fe-S clusters to recipient proteins is a crucial step in the biogenesis of Fe-S proteins; review focuses on recent insights into the molecular mechanism of amino acid motif recognition and discrimination by the co-chaperone HSC20 and finds co-chaperone HSC20 binds to LYR motifs present in Fe-S recipient proteins or their binding partners. [Review]
the crucial role of HSC20 in the assembly of the mitochondrial respiratory chain, is reported.
NFS1 binds preferentially to the D-state of ISCU while mtHSP70 binds preferentially to the D-state of ISCU and HSC20 binds preferentially to the S-state of ISCU.
A cysteine-rich N-terminal domain, which clearly distinguishes hHSC20 from the specialized DnaJ type III proteins of fungi and most bacteria, was found to be important for the integrity and function of the human co-chaperone.
structural analysis of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain
Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria.
iron-sulfur cluster co-chaperone protein HscB, mitochondrial
, HscB iron-sulfur cluster co-chaperone homolog (E. coli)
, J-type co-chaperone HSC20
, DnaJ (Hsp40) homolog, subfamily C, member 20
, dnaJ homolog subfamily C member 20