| Cat. No. | Size |
Price |
|
|---|---|---|---|
| SKT-124-96 | 96 wells (1 kit) |
Cat # changed from RSKT-124R to SKT-124-96
Sandwich ELISA, Biotin-labelled antibody
Serum, Tissue extract, Cell lysate, Plasma
2–8°C
1.563–100 ng/mL
0.18 ng/mL
Diabetology - Other Relevant Products, Others
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.