MW 225.3 Da. Superoxide dismutase (SOD) and NF-κB inhibitor. Nitric oxide (NO) spin-trapping reagent when complexed with Fe2+. Active in vivo and in vitro.
28 kDa heat shock protein, CMT2F, DKFZp586P1322, Estrogen-regulated 24 kDa protein, HEL-S-102, HMN2B, HS.76067, HSP 27, HSPB1_HUMAN, Heat Shock Protein 27, Heat shock 25kDa protein 1, Heat shock 27 kDa protein, Heat shock 27kD protein 1, Heat shock 27kDa protein 1, Heat shock 28kDa protein 1, Heat shock protein beta-1, Hsp 25, Hsp 28, SRP27, Stress-responsive protein 27, epididymis secretory protein Li 102, heat shock protein family B (small) member 1
MW 225.3 Da. Superoxide dismutase (SOD) and NF-κB inhibitor. Nitric oxide (NO) spin-trapping reagent when complexed with Fe2+. Active in vivo and in vitro.
Soluble in water to 75mM.
Superoxide dismutase (SOD) and NF-κB inhibitor. Nitric oxide (NO) spin-trapping reagent when complexed with Fe2+. Active in vivo and in vitro.
Hsp27 also known as HSPB1 is a small heat shock protein with a molecular weight of approximately 27 kilodaltons. This protein is expressed in various tissues including muscle heart and brain. It functions as a molecular chaperone that stabilizes unfolded proteins preventing their aggregation. Hsp27 undergoes phosphorylation at specific residues which modulates its chaperone activity and interaction with other proteins.
Hsp27 plays a critical role in cellular stress response by regulating actin cytoskeleton dynamics and inhibiting apoptosis. It forms part of a complex that includes other proteins such as alphaB-crystallin. This complex facilitates the reorganization of proteins under stress conditions enhancing cell survival during oxidative stress or thermal shock. Hsp27 also modulates inflammatory responses and has been shown to affect cell migration.
Hsp27 integrates into the apoptosis and inflammation pathways. It interacts with apoptotic machinery such as caspase proteins to protect cells by hindering apoptosome formation. Additionally Hsp27 can engage with pathways involving the nuclear factor-kappa B (NF-kB) impacting inflammatory signaling. CPTC (carboxyl-pyrene-trioctylamine) can modulate these pathways by altering Hsp27 function and interactions.
Hsp27 has connections to neurodegenerative diseases and cancer. In neurodegenerative conditions such as Alzheimer's disease its chaperone activity is thought to protect neurons from misfolded protein aggregates. In cancer Hsp27 supports tumor cell survival and resistance to chemotherapy by interacting with proteins like Akt and p53. These interactions highlight the complex role of Hsp27 in modulating cellular responses in various pathological states.
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2D chemical structure image of ab144752, Diethyldithiocarbamic acid sodium salt trihydrate, SOD and NF-kappaB inhibitor
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