Hsp70 PLANT StressXpress® ELISA Kit

Cat. No.	Size	Price
RSKT-124R	96 wells (1 kit)

Technical Data

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Serum, Tissue extract, Cell lysate, Plasma

Storage/Expiration

2–8°C

Calibration Range

1.563–100 ng/mL

Limit of Detection

0.18 ng/mL

Summary

Features

ELISA kit used to quantitate hsp70 concentration in samples
The total assay time is less than 4 hours

Research topic

Diabetology - Other Relevant Products, Others

Summary

Hsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). In most eukaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments
of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and
the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at
least 5O% identity (1). The N-terminal two thirds of hsp70s are more conserved than the
C-terminal third. Hsp70 binds ATP with high affinity and possesses a weak ATPase activity
which can be stimulated by binding to unfolded proteins and synthetic peptides (2). When
hsc70 (constitutively expressed) present in mammalian cells was truncated, ATP binding
activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide
binding capacity. Polypeptide binding ability therefore resided within the C-terminal half
(3). The structure of this ATP binding domain displays multiple features of nucleotide
binding proteins (4).
All hsp70s, regardless of location, bind proteins, particularly unfolded ones. The molecular
chaperones of the hsp70 family recognize and bind to nascent polypeptide chains as well as
partially folded intermediates of proteins preventing their aggregation and misfolding. The
binding of ATP triggers a critical conformational change leading to the release of the bound
substrate protein (5). The universal ability of hsp70s to undergo cycles of binding to and
release from hydrophobic stretches of partially unfolded proteins determines their role in
a great variety of vital intracellular functions such as protein synthesis, protein folding and
oligomerization and protein transport.

Summary References (9)

References to Heat Shock 70kDa Protein 1A/1B

Boorstein WR, Ziegelhoffer T, Craig EA. Molecular evolution of the HSP70 multigene family. J Mol Evol. 1994 Jan;38 (1):1-17
Bork P, Sander C, Valencia A. An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins. Proc Natl Acad Sci U S A. 1992 Aug 15;89 (16):7290-4
DeLuca-Flaherty C, McKay DB, Parham P, Hill BL. Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis. Cell. 1990 Sep 7;62 (5):875-87
Fernandez-Funez P, Nino-Rosales ML, de Gouyon B, She WC, Luchak JM, Martinez P, Turiegano E, Benito J, Capovilla M, Skinner PJ, McCall A, Canal I, Orr HT, Zoghbi HY, Botas J. Identification of genes that modify ataxin-1-induced neurodegeneration. Nature. 2000 Nov 2;408 (6808):101-6
Fink AL. Chaperone-mediated protein folding. Physiol Rev. 1999 Apr;79 (2):425-49
Prapapanich V, Chen S, Toran EJ, Rimerman RA, Smith DF. Mutational analysis of the hsp70-interacting protein Hip. Mol Cell Biol. 1996 Nov;16 (11):6200-7
Rothman JE. Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell. 1989 Nov 17;59 (4):591-601
Smith DF, Sullivan WP, Marion TN, Zaitsu K, Madden B, McCormick DJ, Toft DO. Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70. Mol Cell Biol. 1993 Feb;13 (2):869-76
Zou J, Guo Y, Guettouche T, Smith DF, Voellmy R. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell. 1998 Aug 21;94 (4):471-80