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 (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 44kDa 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. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at more.
Certificate of analysis
This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.3µM phosphate liberated/hr/µg protein in a 200µl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.
Active Human Recombinant HSP70 Protein
HSP70 1 Protein, HSP70 2 Protein, HSP70.1 Protein, HSP72 Protein, HSP73 Protein, HSPA1 Protein, HSPA1A Protein, HSPA1B Protein
Primary research area
Cancer, Heat Shock
WB, SDS-PAGE, ATPase Activity Assay, Functional Assay, ELISA
Relevant bio activity
Protein expression model
See included datasheet.
>90% High purity
Recommended buffer for storage
Na-Phosphate, pH7.5 (20mM), 150mM NaCl, 10% glycerol, 200mM Imidazole
Lot/batch specific. See included datasheet.
Blue Ice or 4°C
Supplementary useful information
Please see included datasheet or contact us
Protein cell localization
1. Zho J. (1998) Cell. 94: 471-480. 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. Natl Acad. Sci. USA. 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Smith D.F., et al., (1993) Mol. Cell. Biol. 13(2): 869-876. 8. Prapapanich V., et al., (1996) Mol. Cell. Biol. 16(11): 6200-6207. 9. Fernandez-Funez et al., (2000) Nature. 408(6808): 101-106.
22496374, 21898234, 21423669, 19540092, 19503596, 19209902
Western Blot Control, ELISA, ELISA, Western Blot Inhibitor, Immunoprecipitation, Western Blot Control
Tested species reactivity
Mouse, Human, Drosophila melanogaster
Representative figure legend
SDS-PAGE of 70kDa Hsp70 protein (SPR-103). SDS-Page of human HSP70 Protein (SPR-103)
Total weight (kg)
Net weight (g)
Human proteins, cDNA and human recombinants are used in human reactive ELISA kits and to produce anti-human mono and polyclonal antibodies. Modern humans (Homo sapiens, primarily ssp. Homo sapiens sapiens). Depending on the epitopes used human ELISA kits can be cross reactive to many other species. Mainly analyzed are human serum, plasma, urine, saliva, human cell culture supernatants and biological samples.
Recombinants or rec. proteins