|Dot blot (DB)||1:500|
|Tested Species reactivity||Human|
|Host / Isotype||Rabbit / IgG|
|Immunogen||KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding S78 of human HSPB1|
|Purification||Antigen affinity chromatography|
|Contains||0.09% sodium azide|
|Storage conditions||-20° C, Avoid Freeze/Thaw Cycles|
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. HSBP1 exhibits rapid increased phosphorylation in response to various mitogens, tumor promoters (e.g. phorbol esters) and calcium ionophores, and high levels are associated with carcinoma of the breast and with endometrial adenocarcinomas. Heat shock of HeLa cell cultures, or treatment with arsenite, phorbol ester, or tumor necrosis factor, causes a rapid phosphorylation of preexisting HSBP1, with Ser82 as the major site and Ser78 the minor site of phosphorylation. HSBP1 may exert phosphorylation-activated functions linked with growth signaling pathways in unstressed cells. A homeostatic function at this level could protect cells from adverse effects of signal transduction systems which may be activated inappropriately during stress.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: 28 kDa heat shock protein; 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 beta-1; HSP 27; HSP25; HSP27; 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
Entrez Gene ID: (Human) 3315
Molecular Function: chaperone
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