Anti-Human ST3GAL1 Antibody Pair

Product Description: ST3 beta-galactoside alpha-2,3-sialyltransferase 1 (ST3GAL1) is a type II membrane glycoprotein enzyme belonging to glycosyltransferase family 29, catalyzing the transfer of sialic acid from CMP-Neu5Ac to galactose-containing substrates, primarily on glycoproteins and glycolipids. Structurally, ST3GAL1 contains conserved disulfide bonds critical for maintaining its active conformation, with key residues involved in donor and acceptor substrate binding and catalysis. The enzyme is predominantly localized in the Golgi apparatus but can be proteolytically processed to a soluble form. Functionally, ST3GAL1 regulates terminal sialylation of O-glycans, influencing cell adhesion and signaling pathways. Dysregulation of ST3GAL1 is implicated in cancer progression, notably promoting cell migration, invasion, and epithelial-mesenchymal transition (EMT) in ovarian and prostate cancers. It also contributes to tumor immune evasion by synthesizing sialoglycans that modulate the tumor microenvironment and confer resistance to chemotherapy agents like paclitaxel. Protein Function: A beta-galactoside alpha2->3 sialyltransferase involved in terminal sialylation of glycoproteins and glycolipids (PubMed:31784620, PubMed:8027041). Catalyzes the transfer of sialic acid (N-acetyl-neuraminic acid, Neu5Ac) from the nucleotide sugar donor CMP-Neu5Ac onto acceptor Galbeta-(1->3)-GalNAc-terminated glycoconjugates through an alpha2-3 linkage (PubMed:31784620, PubMed:8027041, PubMed:31719620). Adds sialic acid to the core 1 O-glycan, Galbeta-(1->3)-GalNAc-O-Ser/Thr, which is a major structure of mucin-type O-glycans. As part of a homeostatic mechanism that regulates CD8-positive T cell numbers, sialylates core 1 O-glycans of T cell glycoproteins, SPN/CD43 and PTPRC/CD45. Prevents premature apoptosis of thymic CD8-positive T cells prior to peripheral emigration, whereas in the secondary lymphoid organs controls the survival of CD8-positive memory T cells generated following a successful immune response (By similarity). Transfers sialic acid to asialofetuin, presumably onto Galbeta-(1->3)-GalNAc-O-Ser (By similarity). Sialylates GM1a, GA1 and GD1b gangliosides to form GD1a, GM1b and GT1b, respectively (By similarity) (PubMed:8027041) [The Uniprot Consortium]