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Hsp70 StressXpress® Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:Heat shock 70 kDa protein 1/2, HSP70-1/HSP70-2, HSP70.1/HSP70.2, HSPA1A, HSPA1, HSPA1B
  • Species:Human
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Cat. No. Size Price


RSKT-105-480R 5x 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Tissue extract, Cell lysate

Storage/Expiration

2–8°C

Calibration Curve

Calibration Range

0.781–50 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 6 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 (2). 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 (3). When hsc70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). 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 (6). 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.

References to Summary

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
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