|Product Name||HSP70 Protein|
Active Human Recombinant HSP70 Protein
|Applications||, WB , SDS-PAGE , ATPase Activity Assay , Functional Assay , ELISA|
|Concentration||Lot/batch specific. See included datasheet.|
AP (Alkaline Phosphatase)
HRP (Horseradish peroxidase)
|Expression System||E. coli|
|Amino Acid Sequence||MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD|
|Biological Activity||ATPase active|
|Storage Buffer||Na-Phosphate, pH7.5 (20mM), 150mM NaCl, 10% glycerol, 200mM Imidazole|
|Shipping Temperature||Blue Ice or 4ºC|
|Cite This Product||Human Recombinant HSP70 Protein (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPR-103)|
|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.|
|Alternative Names||HSP70 1 Protein, HSP70 2 Protein, HSP70.1 Protein, HSP72 Protein, HSP73 Protein, HSPA1 Protein, HSPA1A Protein, HSPA1B Protein|
|Research Areas||Cancer, Heat Shock|
|Scientific 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 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 http://www.HSP70.com.|
|References||1. Zho J. (1998) Cell. 94: 471-480.
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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.
Fernandez-Funez, P. et al. (2009) PLoS Genet. 5(6): e1000507.
PubMed ID: 19503596 Applications: Immunoprecipitation
Ireland, H.E. and Williams, J.H.H. (2011) Methods Mol Biol. 787, 145-153.
PubMed ID: 21898234 Applications: ELISA
Sorci, G. et al. (2011) PLoS Pathog. 7(3): e1001315.
PubMed ID: 21423669 Applications: ELISA
Lee, S.L. et al. (2017) Cell Stress Chaperones. [Epub ahead of print]
PubMed ID: 28255900 Applications: Western Blot Control
Chanoux, R.A. et al. (2012) J Biol Chem. 287.19255-19265.
PubMed ID: 22496374 Applications: Western Blot Control
Ishibashi, Y., Kato, H., Asahi, Y., Suqita, T. and Nishikawa, A. (2009) J Dermatol Sci. 55 (3): 185-192.
PubMed ID: 19540092 Applications: Western Blot Inhibitor
Zwang, N.A. et al. (2009) J Proteome Res. 8 (3): 1540-1554.
PubMed ID: 19209902 Applications: Western Blot Control