产品名称
Anti-Heat Shock Protein 27 antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution
biological source
rabbit
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen 27 kDa
species reactivity
human
technique(s)
indirect immunofluorescence: 1:250-1:500 using HeLa cells
microarray: suitable
western blot: 1:4,000-1:8,000 using whole cell extract of human epitheloid carcinoma HeLa cell line or human epidermoid carcinoma A431 cell line
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... HSPB1(3315)
mouse ... Hspb1(15507)
rat ... Hspb1(24471)
Application
Anti-Heat Shock Protein 27 antibody produced in rabbit may be used in immunoblotting and immunofluorescence.
Biochem/physiol Actions
Anti- Heat Shock Protein 27 (HSP27) recognizes HSP27 (27 kDa).
Heat shock protein 27 (HSP27) accumulates in cells exposed to a short period of hyperthermia and contributes to the development of a transient state of thermotolerance. HSP27 can inhibit actin polymerization, thus modulating actin dynamics during stress. It is known to guard against apoptotic cell death activated by several stimuli, such as Fas ligand hyperthermia, oxidative stress and cytotoxic drugs. It can hinder the mitochondrial pathway of caspase-induced cell death by acting as a negative regulator of cytochrome c-dependent activation of caspase-3. The synthesis of HSP27 is stimulated by various cytokines, growth factors, hormones and chemicals. HSP27 shows a rapid phosphorylation, following exposure to stress stimuli. HSP27 is expressed in the cytoplasm and colocalizes to the nucleus upon stress stimuli. Mutation on this HSP27 gene is associated with Charcot-Marie-Tooth disease.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Heat shock protein 27 (HSP27) is an actin-binding protein, that is located on human chromosome 7q11.23. HSP27 (mouse HSP25) is a highly conserved oligomeric protein. This protein is expressed in various cell types and tissues during specific development and differentiation stages.
Immunogen
synthetic peptide corresponding to amino acids 186-205 located at the C-terminus of human HSP27, conjugated to KLH. This sequence is highly homologous in rat HSP27 (85% identity) and to a lesser extent in mouse HSP27/25 (65% identity).
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Preparation Note
For continuous use, store at 2-8°C for up to one month. For extended storage freeze in working aliquots. Repeated freezing and thawing is not recommended. Storage in "frost-free" freezers is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.
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J Landry et al.
Biochemistry and cell biology = Biochimie et biologie cellulaire, 73(9-10), 703-707 (1995-09-01)
HSP27, like other proteins of the heat-shock protein family, accumulates to high levels after exposure of cells to a short period of hyperthermia and contributes to the development of a transient state of thermoresistance. In vitro, HSP27 behaves as an
New HSP27 inhibitors efficiently suppress drug resistance development in cancer cells
Heinrich JC, et al.
Testing, 7(42), 68156-68156 (2016)
Heat shock protein 27 gene: chromosomal and molecular location and relationship to Williams syndrome
Stock AD, et al.
American Journal of Medical Genetics. Part A, 12, 320-325 (2003)
Targeting heat shock protein 27 in cancer: a druggable target for cancer treatment
Choi SK, et al.
Cancers, 11(8), 1195-1195 (2019)
Functional state of the Hsp27 chaperone as a molecular marker of an unfavorable course of larynx cancer
Kaigorodova EV, et al.
Cancer Biomarkers : Section A of Disease Markers, 17(2), 145-153 (2016)
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