|Detection of Human Protein O‑Glucosyltransferase 1/POGLUT1 by Western Blot. Western blot shows lysates of HepG2 human hepatocellular carcinoma cell line, Jurkat human acute T cell leukemia cell line, and IMR‑32 human neuroblastoma cell line. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human Protein O‑Glucosyltransferase 1/POGLUT1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6437) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for Protein O‑Glucosyltransferase 1/POGLUT1 at approximately 46 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
O-Glucosyltransferase1 (POGLUT1) is a homologue of Rumi from Drosophila, an endoplasmic reticulum (ER)-retaining glucosyltransferase, that adds glucose to serine residues within the consensus sequence of C1‑X‑S‑X‑P‑C2 in Notch EGF repeats, thereby regulating cell-fate decisions (1). It is also known as CAP10-like protein (2) and KTELC1 due to the highly conserved CAP10 domain and the presence of an ER-retaining motif, KTEL, at the C‑terminus. The human gene is reported to be involved in the pathogenesis of both acute myelogenous and T‑acute lymphoblastic leukemias (3). Recently, POGLUT1 has been demonstrated in a phosphatase-coupled glycosyltransferase assay to have hydrolase activity on UDP-Glc (4).
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