CDGSH iron sulfur domain 1 (CISD1), also known as mitoNEET, is an iron-sulfur outer mitochondrial membrane protein and member of the NEET protein family with roles in redox sensing, iron uptake, and respiratory capacity.{53739,53740} It is a homodimeric protein comprised of a B-cap domain and a cluster binding domain with each monomer consisting of an N-terminal in-organelle domain, a transmembrane domain, and a C-terminal cytosolic domain.{53739} The CISD1 C-terminal domain houses the [2Fe-2S] cluster binding site which has roles in tuning redox properties of the protein in response to environmental conditions. CISD1 mRNA expression is induced by the ferroptosis inducer erastin (Item No. 17754) in HepG2 cells in an iron-dependent manner and stabilization of the CISD1 [2Fe-2S] cluster by pioglitazone (Item Nos. 71745 | 22263 | 10028) inhibits mitochondrial iron uptake, lipid peroxidation, and subsequent ferroptosis in the same cells.{53740} Overexpression of CISD1 decreases oxidative stress-induced apoptosis in an HL-1 cardiomyocyte model of hypoxia and reoxygenation injury.{53738} Levels of CISD1 mRNA are decreased in subcutaneous and visceral adipose tissue isolated from patients with obesity and visceral adipose tissue levels of CISD1 mRNA are positively correlated with insulin sensitivity in patients with morbid obesity.{55227} Knockdown of Cisd1 in mice induces mitochondrial dysfunction and increased levels of mitochondrial reactive oxygen species (ROS), as well as a loss of striatal dopamine, shortened stride length in a gait analysis, and decreased latency to fall in the rotarod test, all of which serve as markers of a Parkinsonian phenotype.{53737} Cayman's CISD1 Cytosolic Domain (human, recombinant) protein consists of 95 amino acids and has a calculated molecular weight of 11.3 kDa. By SDS-PAGE, under reducing conditions, the apparent molecular mass is approximately 14 kDa.
20 ug
Cayman Chemical
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