Anti-Human SULT1C2 Antibody Pair

Product Description: Sulfotransferase family 1C member 2 (SULT1C2) is a cytosolic enzyme encoded by the SULT1C2 gene, primarily involved in the sulfonation of hormones, neurotransmitters, drugs, and xenobiotics using 3'-phosphoadenosine 5'-phosphosulfate (PAPS) as a sulfate donor. This phase II detoxification enzyme facilitates the metabolism and excretion of various compounds, including potential carcinogens. SULT1C2 is structurally characterized by a conserved sulfotransferase domain and is expressed in fetal kidney and adult tissues like the stomach and thyroid. Its activity varies due to genetic polymorphisms, influencing individual responses to toxins and drugs. Dysregulation of SULT1C2 has been implicated in disease, particularly cancer. Overexpression in gastric and thyroid tissues is associated with increased susceptibility to carcinomas, potentially due to its role in activating procarcinogens or altering hormone signaling. For instance, elevated SULT1C2 levels may promote thyroid tumorigenesis by modifying estrogen metabolism. Additionally, genetic variants of SULT1C2 are linked to colorectal and hepatocellular cancer risks, highlighting its dual role in detoxification and carcinogen activation. Protein Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the sulfate conjugation of phenolic compounds (PubMed:10481272, PubMed:10783263, PubMed:9852044). Does not transfer sulfate to steroids, dopamine, acetaminophen, or alpha-naphthol (PubMed:10481272, PubMed:9852044). Except in mitochondria, where it can add sulfate to cholesterol producing cholesterol sulfate, which alters mitochondrial membrane organization, and impacts protein complex mobility increasing state-III respiration, thereby modulating mitochondrial respiration (By similarity). Catalyzes the sulfation of the carcinogenic N-hydroxy-2-acetylaminofluorene leading to highly reactive intermediates capable of forming DNA adducts, potentially resulting in mutagenesis (PubMed:9852044) [The Uniprot Consortium]