Anti-HSP27 [Clone 5D12.A12] - 100 μg

Hsp27 is an important heat shock protein found in normal and malignant human cells. The basic structure of most Hsps is a highly conserved amino acid sequence with an alpha-crystallin domain at the C-terminus and WD/EPF domain at the less conserved N- terminus. The N-terminus is essential for formation of high molecular weight oligomers. Hsp27 oligomers are formed by as many as 8-40 Hsp 27 monomers. The degree of oligomerization is associated with chaperone activity: large oligomers have high chaperone activity, whereas dimers have no chaperone activity. Hsp27 is localized in the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress where it may function to stabilize DNA and/or the nuclear membrane. Hsp27 is also involved in the apoptotic signaling pathway because it interferes with activation of cytochrome C / Apaf-1 / dATP complex, thereby inhibiting activation of procaspase-9.