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Hsp70 Antibody (OASE00332)

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Predicted Species Reactivity:
Human, Mouse, Rat, Beluga, Cow, Dog, Fish (carp), Guinea Pig, Hamster, Monkey, Pig, Sheep, Coral, Tomato, Tobacco, Spiny Dogfish Shark (Squalus acanthias), Atlantic Hagfish (Myxine glutinosa)
Product Format:
Liquid. PBS with 50% glycerol and 0.09% sodium azide.
Cellular Location: Cytoplasm.
Reconstitution and Storage:
Store at -20C for up to one year. Shipping in Blue Ice or 4C. Avoid freeze/thaw cycles.
Replacement Item:
This antibody may replace item sc-1060 from Santa Cruz Biotechnology.
Full length protein Hsp70.
Protein A purification.
1 mg/ml
Printable datasheet for OASE00332
Detects a ~70kDa. May cross-react with HSC70 at lower dilutions.
Application Info:
WB: 1:10000
IP: 1:100
Target Reference:
1. Welch W.J. and Suhan J.P. (1986) J.Cell Biol. 103: 2035-2050.
2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J.
Mol. Evol. 38(1): 1-17.
3. Rothman J. (1989) Cell 59: 591 -601.
4. DeLuca-Flaherty et al. (1990) Cell 62: 875-887.
5. Bork P., Sander C. & Valencia A. (1992) Proc. Nut1 Acad.
Sci. USA 89: 7290-7294.
6. Fink A.L. (1999) Physiol. Rev. 79: 425-449.
7. Hung T.H., et al. (2001) Am J Pathol. 159: 1031-1043.
8. Locke M. (2000) Cell Stress & Chaperones 5: 45-51.
9. Ianaro A., et al. (2001) FEBS Lett. 508: 61-66.
10.Trentin G.A. et al. (2001) J Biol Chem. 276: 13087-
Gene Symbol:
Official Gene Full Name:
heat shock 70kDa protein 1A
NCBI Gene Id:
Description of Target:
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 50% identity (1, 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 ATPbinding 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.
Swissprot Id:
Protein Accession #:
Tissue Tool:
Find tissues and cell lines supported by DNA array analysis to express HSPA1A.
RNA Seq:
Find tissues and cell lines supported by RNA-seq analysis to express HSPA1A.

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