|Application ||WB, IF, IP|
|Calculated MW||22893 Da|
|Application & Usage||Western blotting (1-2 µg/ml), immunoprecipitation (5-10 µg/ml), immunocytochemistry (10-15 µg/ml), and ELISA (1 µg/ml). However, the optimal conditions should be determined individually. The antibody detects a 27 kDa protein, corresponding to the apparent molecular mass of Hsp27 on SDS-PAGE immunoblots, in samples from human, monkey, dog (weakly) and pig (weakly) origins.|
|Other Names||HSPB1, CMT2F, DKFZp586P1322, HS.76067, HSP27, HSP28, Hsp25|
|Formulation||100 µg (0.5 mg/ml) affinity purified rabbit polyclonal antibody in phosphate buffered saline (PBS), pH 7.2, containing 30% glycerol, 0.5% BSA, 0.01% thimerosal.|
|Handling||The antibody solution should be gently mixed before use.|
|Reconstitution & Storage||-20 °C|
|Precautions||Hsp27 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Involved in stress resistance and actin organization.|
|Cellular Location||Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, spindle Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles (By similarity).|
|Tissue Location||Expressed in a variety of tissues. High levels in lung, adrenal, xiphoid, adipose tissue, heart and striated and smooth muscle, lower levels in the CNS. Adult levels are much higher in the slow-twitch soleus muscle than in the fast-twitch rectus femoris and extensor digitorum muscles|
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Human Hsp27, mouse Hsp25 and αβ-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 8-40 Hsp27 protein monomers in cells and data s µggests 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. Hsp27 is 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. Recent findings indicate that Hsp27 is also a negative regulator of cytochrome c-dependent activation of procaspase-3.
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