|Detection of Human/Mouse HSF2 by Western Blot. Western blot shows lysates of NIH‑3T3 mouse embryonic fibroblast cell line, human HeLa human cervical epithelial carcinoma cell line, and 293T human embryonic kidney cell line. PVDF membrane was probed with 2 µg/mL of Human/Mouse HSF2 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF5227) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for HSF2 at approximately 60 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 3.|
HSF2 (Heat shock transcription factor 2; also HSTF2) is a 60 kDa member of the HSF family of proteins. It is widely expressed and serves as a transcriptional activator of HSPs. In quiescent cells, HSF2 is a cytoplasmic homodimer; upon exposure to stress or differentiation, it homo- or hetero-trimerizes with HSF-1, and translocates to the nucleus where it impacts gene transcription. Human HSF2 is 536 amino acids (aa) in length and contains a DNA binding region (aa 7‑107), two NLSs (aa 108‑122 and 195‑210) and an HR (hydrophobic repeat) domain that mediates trimerization (aa 119‑192). There are three potential splice variants. One shows a Leu substitution for aa 260‑536, a second shows an IlePhe substitution for aa 229‑536, and a third shows a deletion of aa 393‑410. Over aa 411‑536, human HSF2 is 92% aa identical to mouse HSF2.
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