This Antibody was verified by Cell treatment to ensure that the antibody binds to the antigen stated. View Details
PA1-018 detects phosphorylated heat shock protein 27(hsp27) from rat and human tissue tissues.
PA1-018 has been successfully used in Western blot, immunoprecipitation, immunofluorscence, immunocytochemistry and immunohistochemistry procedures. Immunocytochemical staining of phospho-hsp27 (Ser15) in HeLa cells with this antibody results in cytoplasmic staining.
The PA1-018 immunogen is a synthetic phosphopeptide corresponding to the residues L(10) L R G P (pS) W D P F R C(21) of human HSP27. The immunizing peptide is 81% homologous in mice, rats, and hamsters. This peptide (Cat. # PEP-187) is available for use in neutralization and control experiments.
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.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: 28 kDa heat shock protein; DKFZp586P1322; epididymis secretory protein Li 102; Estrogen-regulated 24 kDa protein; Heat shock 27 kDa protein; heat shock 27kD protein 1; heat shock 27kDa protein 1; Heat shock protein; Heat shock protein beta-1; HS; HSP; HSP 27; HspB1; Phospho-HSP 27; SRP27; Stress-responsive protein 27
Gene Aliases: CMT2F; HEL-S-102; HMN2B; HS.76067; Hsp25; HSP27; HSP28; HSPB1; SRP27
UniProt ID: (Human) P04792
Molecular Function: chaperone