Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 40S subunit. The protein belongs to the S12P family of ribosomal proteins. It is located in the cytoplasm. The protein shares significant amino acid similarity with S. cerevisiae ribosomal protein S28. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. (provided by RefSeq)
Immunogen
RPS23 (NP_001016, 44 a.a. ~ 143 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Ribosomal protein S23 (RPS23) acts as a substrate for oxygenase domain containing protein 1 (OGFOD1), which is an enzyme involved in the regulation of protein translation and cellular growth. Abnormality in the regulation of RPS23 is associated with the pathogenesis of disc degeneration (DD). The protein has a potential application in diagnosis and treatment of DD.
Physical form
Solution in phosphate buffered saline, pH 7.4
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Bioinformatics analysis of published microarray data. This study aimed to reveal the possible genes and pathways related to the pathogenesis of disc degeneration (DD) by analyzing the microarray data. DD is one of the main causes of low back pain
Proceedings of the National Academy of Sciences of the United States of America, 111(11), 4031-4036 (2014-02-20)
2-Oxoglutarate (2OG) and Fe(II)-dependent oxygenase domain-containing protein 1 (OGFOD1) is predicted to be a conserved 2OG oxygenase, the catalytic domain of which is related to hypoxia-inducible factor prolyl hydroxylases. OGFOD1 homologs in yeast are implicated in diverse cellular functions ranging
Journal of translational medicine, 22(1), 248-248 (2024-03-08)
Acute ischemic stroke is a common neurological disease with a significant financial burden but lacks effective drugs. Hypoxia-inducible factor (HIF) and prolyl hydroxylases (PHDs) participate in the pathophysiological process of ischemia. However, whether FG4592, the first clinically approved PHDs inhibitor
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