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Product Name: Hsp70 (Recombinant, Human, Baculovirus expressed, His-tag)
Catalog #: SPR-115C
Alternative Names: Hsp70 1, Hsp70 2, Hsp70.1, Hsp72, Hsp73, HSPA1, HSPA1A, HSPA1B
Type: Recombinant Protein
Accession Number: NM_005345
Gene ID: 3303
SwissProt: P08107
Applications: ATPase Assay, WB control, Binding Assay, ELISA reference standard
Species: Human
Conjugate/Tag: His-tag
Form: Affinity Purifiied using His tag
Storage Buffer: 20mM Tris, 150mM NaCl and 10% glycerol.
Concentration: 0.5mg/mL
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.
Background Info: Molecular weight of approximately 70kD
Package Size: 2x 100ug
Other Information: ATPase active
Storage Temp: -20°C
Shipping Temp: Dry ice, Blue Ice or 4°C
Datasheet: SPR 115 Heat Shock Protein 70 (Hsp70)
Research Area: Chaperones, Heat Shock, Trafficking
Price: $742.00 USD Add to Cart

SDS PAGE of endotoxin-free, his-tagged human 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: Tal Mizrahi, Joseph Heller, Shoshana Goldenberg and Zeev Arad. Heat shock proteins and resistance to desiccation in congeneric land snails. Cell Stress and Chaperones Volume 15, Number 4, 351-365

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