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Product Name: Recombinant Human Hsp70
Catalog #: SPR-103A
Package size: 50ug
Price: $233.00 USD

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Alternate Product Sizes: SPR-103B, SPR-103C
Type: Recombinant Protein
Conjugate/Tag: His-tag
Datasheet: SPR 103 Heat Shock Protein 70 (Hsp70)
Description: Hsp70 Protein
Research Area: Chaperones, Heat Shock, Trafficking
Alternative Names: Hsp70 1, Hsp70 2, Hsp70.1, Hsp72, Hsp73, HSPA1, HSPA1A, HSPA1B
Species: Human
Applications: ATPase Assay, WB control, Binding Assay, ELISA reference standard, Lipid interaction assays
Accession Number: NM_005345
Gene ID: 3303
SwissProt: P08107
Expression System: E. coli
Background Info: Molecular weight of approximately 70kDa
Form: Multi-step Chromatographically purified.
Storage Buffer: Na-Phosphate, pH7.5 (20mM), 150mM NaCl, 10% glycerol, 200mM Imidazole
Concentration: 0.47mg/mL
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.
Storage Temp: -20°C
Shipping Temp: Dry ice, Blue Ice or 4°C

SDS PAGE of hsp70 protein.

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 (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.
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. Nut1 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.
Cited References: 1. Pedro Fernandez-Funez, Sergio Casas-Tinto, Yan Zhang, Melisa Gómez-Velazquez, Marco A. Morales-Garza, Ana C. Cepeda-Nieto, Joaquín Castilla, Claudio Soto, Diego E. Rincon-Limas. In Vivo Generation of Neurotoxic Prion Protein: Role for Hsp70 in Accumulation of Misfolded Isoforms. PLoS Genetics, June 2009, Volume 5, Issue 6, e1000507, pp1-14

2. Yoshio Ishibashia, Hiroshi Katoa, Yoko Asahia, Takashi Sugitab and Akemi Nishikawa. Identification of the major allergen of Malassezia globosa relevant for atopic dermatitis. Journal of Dermatological Science, Volume 55, Issue 3, September 2009, Pages 185-192. doi:10.1016/j.jdermsci.2009.05.005

3. Ireland, E.H. and Williams, J. H. H.. In Molecular Chaperones; Methods in Molecular Biology, 2011, Volume 787, 145-153. Measuring Hsp72 (HSPA1A) by Indirect Sandwich ELISA. doi: 10.1007/978-1-61779-295-3_12.

4. Nicholas A. Zwang, Jason D. Hoffert, Trairak Pisitkun, Hanne B. Moeller, Robert A. Fenton and Mark A. Knepper. Identification of Phosphorylation-Dependent Binding Partners of Aquaporin-2 Using Protein Mass Spectrometry. J. Proteome Res., 2009, 8 (3), pp 1540–1554. doi:10.1021/pr800894p

5. Guglielmo Sorci, Gloria Giovannini, Francesca Riuzzi, Pierluigi Bonifazi, Teresa Zelante, Silvia Zagarella, Francesco Bistoni, Rosario Donato, and Luigina Romani. The Danger Signal S100B Integrates Pathogen– and Danger–Sensing Pathways to Restrain Inflammation. PLoS Pathog. 2011 March; 7(3): e1001315. Published online 2011 March 10. doi: 10.1371/journal.ppat.1001315

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