Art Nr.: SPC-103D, StressMarq
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Product Name
Hsp70 Antibody
Catalog #
Package size
View Conjugates
Bulk Quote
Alternate Product Sizes
SPC 103 Heat Shock Protein 70 (Hsp70)
Research Area
Chaperones, Heat Shock, Trafficking
Alternative Names
Hsp70 1, Hsp70 2, Hsp70.1, Hsp72, Hsp73, HSPA1, HSPA1A, HSPA1B
Clone Number
Host Species
Full length human protein Hsp70
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), Rainbow Trout
Accession Number
Gene ID
Background Info
Detects a ~70kDa protein corresponding to the molecular mass of inducible Hsp70 on SDS PAGE immunoblots. May cross-react with Hsc70 at lower dilutions.
Recommended Dilutions
1:25,000 (ECL) (WB), 1:100 (IP)
Rabbit antiserum
Storage Buffer
Rabbit antiserum
Certificate of Analysis
A 1:10,000 dilution of SPC-103 was sufficient for detection of hsp70 in 20μg of HeLa cell lysate by ECL immunoblot analysis.
Storage Temp
Shipping Temp
Blue Ice or 4°C

This antibody is available conjugated to several dyes. Please select one of the conjugates from the lists below or contact your distributor directly about these conjugation options:

ATTO Conjugates:


Enzyme & Fluorescent Conjugates:

hsp70 antibody Western blot analysis of Hsp70 in Pam212 cells using a 1:1000 dilution of SPC-103. Western blot analysis of Hsp70 in multiple human and rat brain cell lysates using a 1:1000 dilution of SPC-103. Hsp70 visualized using SPC-103, tested on Bouin's fixed paraffin-embedded backskin sections of transgenic mice. Courtesy of Dr. Turksen, Ottawa  Hospital Research Institute, Canada.
Inducing Muscle Heat Shock Protein 70 Improves Insulin Sensitivity and Muscular Performance in Aged Mice. J Gerontol A Biol Sci Med Sci. [Epub ahead of print] 2014. Silverstein, M.G. et al. PubMed ID: 25123646     Reactivity: Mouse     Applications: Western Blot
Research Background
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, 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. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at
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- 13095.

This product is offered by Biomol for research purposes only. Not for diagnostic purposes or human use. It may not be resold or used to manufacture commercial products without written approval of Biomol GmbH.