The AKR1C1 and AKR1C2 proteins belong to the aldo-keto reductase (AKR) superfamily, which catalyzes NADPH-dependent reduction of carbonyl groups in various substrates, including steroids, prostaglandins, and xenobiotics. These cytosolic enzymes share ~86% sequence homology and are part of the AKR1C subfamily, which also includes AKR1C3 and AKR1C4. AKR1C1 (20α-hydroxysteroid dehydrogenase) and AKR1C2 (3α-hydroxysteroid dehydrogenase) play critical roles in steroid hormone metabolism, particularly in regulating the balance between active and inactive forms of androgens, estrogens, and progesterone. Their dysregulation has been implicated in hormone-dependent cancers (e.g., prostate, breast), metabolic disorders, and drug resistance. Antibodies targeting AKR1C1/C2 are essential tools for studying their expression patterns, subcellular localization, and functional roles in both physiological and pathological contexts. Due to high structural similarity among AKR1C isoforms, antibody specificity must be rigorously validated using knockout controls or recombinant proteins. These antibodies are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to investigate tissue-specific expression, cancer progression biomarkers, and therapeutic targeting strategies. Recent studies also explore their involvement in inflammatory responses and detoxification pathways, expanding their potential clinical relevance.