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Hsc70 StressXpress® Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:Hsc70, Hsc54, Hsc71, Hsc73, Hsp71, Hsp73, HspA10, HspA8, LAP1, NIP71
  • Species:Human
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Cat. No. Size Price

SKT-106-480 5x 96 wells (1 kit)
PubMed Product Details
Technical Data

Cat # changed from RSKT-106-480R to SKT-106-480


Sandwich ELISA, Biotin-labelled antibody


Serum, Tissue extract, Cell lysate



Calibration Curve

Calibration Range

150–2.34 ng/mL

Limit of Detection

1.54 ng/mL



  • ELISA kit used to quantitate Hsc70 concentration in samples
  • The total assay time is less than 4 hours

Research topic



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 44 kDa 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).
When cells are subjected to metabolic stress (e.g., heat shock) a member of the hsp 70
family, hsp 70 (hsp72), is expressed; hsp 70 is highly related to hsc70 (>90% sequence
identity). Constitutively expressed hsc70 rapidly forms a stable complex with the highly
inducible hsp70 in cells following heat shock. The interaction of hsc70 with hsp 70 is
regulated by ATP. These two heat shock proteins move together in the cell experiencing
stress. Furthermore, research on hsc70 has implicates it with a role in facilitating the
recovery of centrosomal structure and function after heat shock (6).

Summary References (6)

References to Heat Shock 70kDa Cognate Protein

  • 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
  • Brown CR, Hong-Brown LQ, Doxsey SJ, Welch WJ. Molecular chaperones and the centrosome. A role for HSP 73 in centrosomal repair following heat shock treatment. J Biol Chem. 1996 Jan 12;271 (2):833-40
  • Brown CR, Martin RL, Hansen WJ, Beckmann RP, Welch WJ. The constitutive and stress inducible forms of hsp 70 exhibit functional similarities and interact with one another in an ATP-dependent fashion. J Cell Biol. 1993 Mar;120 (5):1101-12
  • 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
  • Rothman JE. Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells. Cell. 1989 Nov 17;59 (4):591-601
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