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You are here:Home » Antibodies » Antibodies-Heat Shock Proteins » Anti -Heat Shock Protein 27 (HSP27)

Anti -Heat Shock Protein 27 (HSP27)


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Clone Host Grade Applications
Polyclonal Rabbit E B IP IH IC
Human Hsp27, mouse Hsp25 and alpha-beta-crystallin are part of a diverse family of small heat shock proteins which are produced in all organisms. They function as chaperone-like proteins by binding unfolded polypeptides and preventing uncontrolled protein aggregation. Hsp27 is believed to exist mainly as oligomers of as many as 840 Hsp27 protein monomers in cells and data suggests that the large oligomers of Hsp27 have a chaperone-like activity by serving as a site where unfolding proteins may bind until ATP and Hsp70-dependent refolding can occur (1). The state of phosphorylation and oligomerization of Hsp27 has been suggested to regulate microfilament organization because data demonstrates that only the nonphosphorylated lower molecular weight forms of Hsp27 bind actin barbed ends and inhibit polymerization (2). Hsp27 is also believed to protect cells by enhancing cellular glutathione levels and elevated glutathione levels have been measured in cells overexpressing hsp27. Data from studies using wild-type Hsp27 and mutant forms in which the serine phosphorylation sites were mutated to alanines, glycines or aspartates, have shown that cellular glutathione levels depend on the oligomerization of Hsp27 (3). Recent findings indicate a novel function for Hsp27 which is that HSp27 is a negative regulator of cytochrome c-dependent activation of procaspase-3 (4).
Western Blot (Colorimetric) (7,8): 1:5,000
Immunoprecipitation (6): 1:100
Immunocytochemistry: 1:300
Immunohistochemistry (9): 1:200
ELISA: 1:1,000
Optimal dilutions to be determined by researcher.PC-Personal Communication
Catalog #H1834-05B
Positive ControlsRecombinant Human Hsp27 Protein
HeLa Heat Shocked Cell Lysate
Clone TypePolyclonal
FormSupplied as a liquid in PBS containing 50% glycerol and 0.09% sodium azide.
ImmunogenHsp27 produced through recombinant DNA methods in E. coli. The
purification of Hsp27 closely follows the method described in
previously published reports
SpecificityDetects a ~27kD protein, corresponding to the apparent molecular mass of Hsp27 on SDS-PAGE immunoblots, in samples from human, monkey, guinea pig and porcine (weakly).
Important NoteThis product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

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