Hsp70 Polyclonal Antibody

Antigen: full length Hsp70 . Host: rabbit . Cross Reactivity: (+) human, mouse, rat, beluga, cow, canine, fish (carp), guinea pig, hamster, monkey, porcine, ovine, and coral Hsp70 . Application(s): WB, IP, ELISA, IHC, and ICC

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SPECIFICATIONS

Catalog Number

15481

Applications

ELISA, ICC, IHC, IP, WB

Hosts

Rabbit

Form

100 microL

P Type

Antibodies|Heat Shock Protein

Weight

0

Antigen

full length Hsp70

Storage Temp

-20

Shipping Temp

-20

Additional Info

Hsp70 genes encode abundant heat-inducible 70 kDa Hsps (Hsp70). 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 50% identity. 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. 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. The structure of this ATP binding domain displays multiple features of nucleotide binding proteins. 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 bound substrate protein. 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, oligomerization, and protein transport.