HSP27 Monoclonal Antibody (STRSN), eBioscience™, Invitrogen™

Description

• Description The MAb STRSN recognizes human heat shock protein 27 (HSP27)
• The heat shock proteins are a large family of proteins that are induced in response to stressors such as changing temperatures, cytokine levels, and presence of various chemicals
• Heat shock proteins serve as molecular chaperones, binding to other proteins to maintain proper protein structure or by folding denatured proteins and preventing activation of caspases that could lead to apoptosis
• Unlike the larger HSP proteins, HSP27 belongs to a unique subgroup that is involved in apoptosis regulation
• Expression of HSP27 is constitutive, but upon stress HSP27 is upregulated and can relocate from the cytoplasm to the nucleus
• Increased HSP27 expression with certain carcinomas has been observed
• In breast cancer, HSP27 expression has been shown to be responsive to estrogen levels
• In both breast cancer and melanoma, high levels of HSP27 correlate with more aggressive tumors and decreased survival
• Increased levels of HSP27 in the serum of patients with Chronic Obstructive Pulmonary Disease (COPD), breast cancer and melanoma may serve as a potential diagnostic marker
• No crossreactivity is observed with HSP70, 90, 104 or 110
• In response to adverse changes in their environment, cells from many organisms increase the expression of a class of proteins referred to as heat shock or stress proteins
• HSPB1 (heat shock protein beta-1 or HSP27) is a small heat shock protein which functions as a molecular chaperone that maintains denatured proteins in a folding-competent state
• It plays a role in stress resistance and actin organization
• Through its molecular chaperone activity, HSP27 regulates numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins
• Mutations in the gene can result in Charcot-Marie-Tooth disease 2F and Neuronopathy distal hereditary motor 2B.