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Hsp27 StressXpress® Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:28kDa heat shock protein, CMT2F, Hsp25, Hsp27, Hsp28, HspB1, SRP27
  • Species:Human
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Cat. No. Size Price


RSKT-109R 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Serum, Cell lysate, Plasma

Storage/Expiration

2–8°C

Calibration Curve

Calibration Range

13–0.2 ng/mL

Limit of Detection

0.04 ng/mL

Summary

Features

  • ELISA kit used to quantitate Hsp27 concentration in samples
  • The total assay time is less than 4 hours

Research topic

Neural tissue markers, Others

Summary

Hsp27s belong to an abundant and ubiquitous family of small heat shock proteins (sHSP). It is an important HSP found in both normal human cells and cancer cells. The basic
structure of most sHsps is a homologous and highly conserved amino acid sequence,
with an alpha-crystallin-domain at the C-terminus and the WD/EPF domain at the less
conserved N-terminus. This N-terminus is essential for the development of high molecular
oligomers (1, 2). Hsp27-oligomers consist of stable dimers formed by as many as 8-40
Hsp27 protein monomers (3). The oligomerization status is connected with the chaperone
activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no
chaperone activity (4).
HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus
in response to stress, where it may function to stabilize DNA and/or the nuclear membrane.
Other functions include chaperone activity (as mentioned above), thermotolerance in
vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an
ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially
denatured proteins, which ensures refolding of the HSP70 complex. Hsp27 is also involved
in the apoptotic signaling pathway because it interferes with the activation of cytochrome
c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also
hypothesized that hsp27 may serve some role in cross-bridge formation between actin
and myosin (5). And finally, Hsp27 is also thought to be involved in the process of cell
differentiation. The up-regulation of Hsp27 correlates with the rate of phosphorylation
and with an increase of large oligomers. It is possible that Hsp27 may play a crucial role in
termination of growth (6)

References to Summary

References to Heat Shock 27kDa Protein

  • Arrigo AP. In search of the molecular mechanism by which small stress proteins counteract apoptosis during cellular differentiation. J Cell Biochem. 2005 Feb 1;94 (2):241-6
  • Ciocca DR, Oesterreich S, Chamness GC, McGuire WL, Fuqua SA. Biological and clinical implications of heat shock protein 27,000 (Hsp27): a review. J Natl Cancer Inst. 1993 Oct 6;85 (19):1558-70
  • Ehrnsperger M, Graber S, Gaestel M, Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 1997 Jan 15;16 (2):221-9
  • Kim KK, Kim R, Kim SH. Crystal structure of a small heat-shock protein. Nature. 1998 Aug 6;394 (6693):595-9
  • Sarto C, Binz PA, Mocarelli P. Heat shock proteins in human cancer. Electrophoresis. 2000 Apr;21 (6):1218-26
  • Van Montfort R, Slingsby C, Vierling E. Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones. Adv Protein Chem. 2001;59:105-56
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