ISOC2 Antibody / Isochorismatase domain-containing protein 2

ISOC2 antibody recognizes Isochorismatase domain-containing protein 2, a cytoplasmic enzyme that belongs to the isochorismatase family of hydrolases. Encoded by the ISOC2 gene on chromosome 19p13.12, this protein contains a conserved catalytic isochorismatase domain that hydrolyzes amide bonds in small-molecule substrates, although its physiological substrates in mammalian cells remain incompletely defined. Structural and proteomic studies indicate that ISOC2 may participate in amino acid metabolism, mitochondrial function, and redox homeostasis. The protein localizes to the cytosol and mitochondrial matrix, where it interacts with metabolic enzymes and stress-response factors. Its expression is ubiquitous but highest in metabolically active tissues such as liver, heart, and skeletal muscle.

ISOC2 is evolutionarily conserved from bacteria to humans, suggesting an ancestral enzymatic role in intermediate metabolism. While the bacterial isochorismatases catalyze the hydrolysis of isochorismate to 2,3-dihydroxybenzoate in siderophore biosynthesis, mammalian ISOC2 lacks this function but retains the characteristic aspartate and cysteine residues that form the catalytic dyad. Structural modeling implies that ISOC2 might act on endogenous metabolites involved in oxidative stress pathways or NAD-dependent reactions. Transcriptomic profiling has linked ISOC2 expression to mitochondrial biogenesis and adaptive responses to nutrient deprivation.

The ISOC2 antibody is used to study mitochondrial metabolism, oxidative stress, and protein-protein interactions involving metabolic enzymes. Western blot analysis detects a 30 kilodalton band corresponding to the mature ISOC2 protein, while immunofluorescence shows diffuse cytoplasmic and mitochondrial staining. Elevated ISOC2 expression has been reported in various cancers, including hepatocellular and colorectal carcinoma, where it may contribute to metabolic reprogramming and proliferation. Silencing of ISOC2 in cancer cell lines reduces ATP production and induces apoptosis, indicating its potential role in maintaining energy homeostasis under stress conditions.

In developmental contexts, ISOC2 expression increases during myogenesis and cardiogenesis, reflecting its involvement in energy-demanding differentiation processes. The protein may interact with metabolic regulators such as PGC-1alpha and AMPK to coordinate mitochondrial turnover and antioxidant defense. Because of these broad metabolic implications, the ISOC2 antibody is valuable for basic and translational research in metabolism, oncology, and mitochondrial biology.