|Product Name||HSP70 Protein|
Human Recombinant HSP70 Full Length 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||Baculovirus/Hi5 cells|
|Amino Acid Sequence||MAKAAAVGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHWPFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTGASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVGYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSCIPPAPGVPQIEVTFDIDANGILNVTATKDSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGGSGSGPTIEEVD|
|Protein Length||Full Length|
|Storage Buffer||50mM Tris/HCl pH7.5, 0.3M NaCl, 10% glycerol, 0.1mM EDTA|
|Shipping Temperature||Blue Ice or 4ºC|
|Purification||Endotoxin-free, Multi-Step Purified|
|Cite This Product||Human Recombinant HSP70 Protein (StressMarq Biosciences Inc., Victoria BC CANADA, Catalog # SPR-117)|
|Certificate of Analysis||This product has been certified >90% pure using SDS-PAGE analysis. The protein tested positive for ATPase activity 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.
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.
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