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Hsp70 (Hsc70) Monoclonal Antibody (Clone BB70)

Hsp70 (Hsc70) Monoclonal Antibody (Clone BB70)

Cat no: 10011425


Supplier: Cayman Chemical Company
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Antigen: chicken Hsp70/Hsp90 complex . Host: mouse, clone BB70 . Cross Reactivity: (+) human, mouse, rat, ovine, canine, beluga, bovine, fish (carp, rainbow trout, and chinook/chum salmon), pacific oyster, guinea pig, scallop, pig, hamster, rabbit, chicken, Artemia, Xenopus, Drosophila, and yeast Hsp70 . Applications: WB, IP, and IHC . Isotype: IgG2a .
Catalogue number: 10011425
Hosts: Mouse
Applications: Immunohistochemistry, Immunoprecipitation, Western Blot
Weight: 72
Form: 200 microg
Antigen: chicken Hsp70/Hsp90 complex{15525}
P type: Antibodies|Heat Shock Protein
Isotype: IgG2a
Shipping temp: -20
Storage temp: -20
Additional info: Hsp70 genes encode abundant heat-inducible 70 kDa Hsps (Hsp70s). In most eucaryotes Hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eukatyotes 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.

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