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Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria.. Additionally we are shipping HSCB Antibodies (16) and and many more products for this protein.
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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 (show CDH2 Proteins) 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 (show NFS1 Proteins) binds preferentially to the D-state of ISCU (show ISCU Proteins) while mtHSP70 (show HSPA9 Proteins) binds preferentially to the D-state of ISCU (show ISCU Proteins) and HSC20 binds preferentially to the S-state of ISCU (show ISCU Proteins).
A cysteine-rich N-terminal domain, which clearly distinguishes hHSC20 from the specialized DnaJ (show DNAJB6 Proteins) 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