|Application ||WB, IHC|
|Calculated MW||22783 Da|
|Other Names||Heat shock protein beta-1, HspB1, 28 kDa heat shock protein, Estrogen-regulated 24 kDa protein, Heat shock 27 kDa protein, HSP 27, Stress-responsive protein 27, SRP27, HSPB1, HSP27, HSP28|
|Target/Specificity||A synthetic peptide corresponding to residues near the N-terminus of human Hsp 27 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|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|
|Tissue Location||Detected in all tissues tested: skeletal muscle, heart, aorta, large intestine, small intestine, stomach, esophagus, bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue, kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal fluid. Highest levels are found in the heart and in tissues composed of striated and smooth muscle|
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Provided below are standard protocols that you may find useful for product applications.
Heat shock protein (HSP) 27 is one of the small HSPs, and is involved in stress resistance and actin organization. HSP27 is expressed in response to environmental stresses such as heat shock, or estrogen stimulation in MCF-7 cells (1,2). HSP27 is phosphorylated at serines 15, 78 and 82 by MAPKAP kinase 2 as a result of the activation of the p38 MAP kinase pathway (3,4).
1. Mendelsohn, M.E., et al. Proc Natl Acad Sci U S A. 88: 112-126 (1991).
2. Faucher,C.,et al..J.Biol Chem. 268:15168-73
3. Landry, J., et al. J. Biol. Chem. 267: 794-803 (1992)
4. Rouse, J., et al.. Cell 78: 1027-1037 (1994)
5. Latour, S et al. (1996) J. Biol. Chem. 271, 22782-90
6. Schymeinsky J, et al. PLos ONE 2(11), 2007
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