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PA1-25984 detects Human HSP27 pSer82 and Mouse Phospho-HSP25 pSer86. The antibody has been negatively preadsorbed using a non-phosphopeptide corresponding to the site of phosphorylation to remove antibody that is reactive with non-phosphorylated HSP25 (the mouse homolog of human HSP27).
Specificity: NIH3T3 cell lysates were immunoblotted in the presence of non-phosphopeptide corresponding to the immunogen, a generic phosphoserine-containing peptide or the phosphopeptide immunogen. The data show that only the peptide corresponding to the mouse phospho S86 HSP25 blocks the antibody signal, thereby demonstrating the specificity of the antibody. The signal was completely removed by lambda phosphatase treatment demonstrating that the antibody interacts specifically with the phosphorylated protein.
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.
仅用于科研。不用于诊断过程。未经明确授权不得转售。