|Detection of Human Phospho‑RPA2 (T21) by Western Blot. Western blot shows lysates of HeLa human cervical epithelial carcinoma cell line and U2OS human osteosarcoma cell line untreated (-) or treated (+) with 1 µM Camptothecin (CPT) for 1 hour. PVDF Membrane was probed with 0.5 µg/mL of Human Phospho-RPA2 (T21) Antigen Affinity-purified Polyclonal Antibody (Catalog # AF6654) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog # HAF008). A specific band was detected for Phospho-RPA2 (T21) at approximately 40 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
RPA2 (replication protein A 32 kDa subunit; also RFA2 and RPA p34) is a 32 kDa DNA-binding protein that constitutess one of three subunits comprising the PRA heterotrimer complex. In conjunction with 70 kDa RPA1 and 14 kDa RPA3, RPA2 participates in DNA replication, recombination and repair. Human RPA2 is 270 amino acids (aa) in length. It contains a Gly/Ser-rich N-terminus (aa 1-33), a DNA-binding domain (aa 43-171) and a protein-interaction C-terminus (aa 187-270). Phosphorylation of the N-terminus on Ser4/8/23/29/33, plus Thr21, regulates RPA complex interactions with DNA repair and replication complexes. There are multiple splice variants. Three contain N-terminal extensions: one shows an 88 aa insertion after Ser4, another shows a 12 aa substitution for aa 1-4, and a third shows a four aa insertion after Ser4. There is also a deletion of aa 93-98, and a potential truncation after Gln175. Over aa 141-270, human RPA2 shares 83% aa identity with mouse RPA2.
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