|Detection of Human and Mouse HSP27 by Western Blot. Western blot shows lysates of Jurkat human acute T cell leukemia cell line and NIH‑3T3 mouse embryonic fibroblast cell line untreated (-) or treated (+) with a 42 °C heat shock for 30 minutes with a 3 hour recovery. PVDF membrane was probed with 0.1 µg/mL of Goat Anti-Human/Mouse/Rat HSP27 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF15801), followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). A specific band was detected for HSP27 at approximately 27 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 2.|
Detection of Human HSP27 by Simple WesternTM. Simple Western lane view shows lysates of Jurkat human acute T cell leukemia cell line, loaded at 0.2 mg/mL. A specific band was detected for HSP27 at approximately 33 kDa (as indicated) using 5 µg/mL of Goat Anti-Human/Mouse/Rat HSP27 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF15801) followed by 1:50 dilution of HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF109). This experiment was conducted under reducing conditions and using the|
12-230 kDa separation system.
Heat shock proteins (HSPs) are a family of highly conserved stress response proteins. Heat shock proteins function primarily as molecular chaperones by facilitating the folding of other cellular proteins, preventing protein aggregation or targeting improperly folded proteins to specific degradative pathways. HSPs are typically expressed at low levels under normal physiological conditions but are dramatically up-regulated in response to cellular stress. Elevated levels of HSPs have been observed in association with ischemia/reperfusion, cancer, and chronic heart failure. HSP27, also known as HSPB1, is a member of the small heat shock protein family, which also includes HSP25 and the alpha -crystallins. HSP27 forms a large oligomer and the extent of phosphorylation plays a role in determining specific functions. HSP27 also functions as an anti-apoptotic molecule, regulating apoptosis through direct interaction with key components of the apoptotic pathway. HSP27 binds and sequesters cytochrome c released from the mitochondria in response to an apoptotic stimulus. This prevents the proper assembly of the apoptosome and subsequently, the activation of procaspase-9 and procaspase-3.
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