|Detection of Human ATRIP by Western Blot. Western blot shows lysates of 293T human embryonic kidney cell line, MCF‑7 human breast cancer cell line and PC‑3 human prostate cancer cell line. PVDF membrane was probed with 1 µg/mL of Human ATRIP Antigen Affinity-purified Polyclonal Antibody (Catalog # AF1579) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for ATRIP at approximately 100 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
ATRIP (ATR interacting protein) is an 85‑90 kDa member of the ATRIP family of proteins. It is ubiquitously expressed, and recruits ATR to sites of DNA damage and replication stress. Human ATRIP is 791 amino acids (aa) in length. It contains a PRA-ssDNA binding region (aa 1‑107), a coiled-coil domain (aa 108‑217) and an ATR‑recruitment region (aa 641‑726). The coiled-coil region mediates ATRIP oligomerization, and multimerization with ATR, creating complexes of 1000 kDa. ATRIP undergoes phosphorylation at Ser224, Ser239 and Ser518 influencing its role in the DNA damage response. There is an alternate start site at Met94, plus a deletion of aa 658‑684 in a second isoform, and a deletion of aa 661‑687 in a third isoform. Over aa 461‑791, human ATRIP is 76% aa identical to mouse ATRIP.
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