|Detection of Human PUM2 by Western Blot. Western blot shows lysates of KG‑1 human acute myelogenous leukemia cell line and HeLa human cervical epithelial carcinoma cell line. PVDF membrane was probed with 0.2 µg/mL of Sheep Anti-Human PUM2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF7415) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). Specific bands were detected for PUM2 at approximately 115-130 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
PUM2 (Pumilio homolog 2/Pumilio-2) is a 121-125 kDa member of the PUF family of RNA-binding peoteins. It is expressed in a variety of cell types, including neurons, skeletal muscle cells, stem cells and germ cells, and plays a role in asymmetric cell division. PUM2 appears to bind to the 3' untranslated region of target mRNAs. By doing so, it causes a conformational change in the RNA, allowing for the subsequent binding of miRNAs and the silencing of protein translation. In germ cells, PUM2 is also reported to complex with NANOSI and SNAPIN, although its function in this complex is unclear. Human PUM2 is 1066 amino acids (aa) in length. It contains a SNAPIN interaction site (aa 1-260), one PUM-HD region (aa 706-1048) and eight consecutive pumilio repeats (aa 726-1022). There are six utilized Ser/Thr phosphorylation sites, and at least two isoform variants. One is 95-96 kDa in size and shows a deletion of aa 574-652, while another shows a deletion of two amino acids; Val829Ile830. Over aa 103-250, human PUM2 shares 95% aa sequence identity with mouse PUM2.
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