Hsp70 Antibody Properties
Anti-Hsp70 (MOUSE) Monoclonal Antibody - 200-301-A27
human, bovine, mouse, rat, C.elegans, dog, chicken, Drosophila, carp, guinea pig, hamster, monkey, pig, rabbit, sheep
IF Microscopy : 1:200-1:1000
Western Blot : 1:500-1:2000
Immunochemistry: 10 µg/ml
Other Dilution: User Optimized
Liquid (sterile filtered)
1.0 mg/ml by UV absorbance at 280 nm
0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
Anti-Hsp 70 antibody is routinely used in cancer and signal transduction research. Hsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). In most eukaryotes, hsp70 genes exist as part of a multigene family. Hsp70s 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 50% identity (2). The N-terminal two-thirds of hsp70s are more conserved than the C-terminal one-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). 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.
Hsp70 monoclonal antibody was prepared using conventional hybridoma technology after repeated immunizations with a synthetic peptide from the region of amino acid residues 436-503 of human Hsp70 protein.