- NCBI Gene Id:
- Official Gene Full Name:
- heat shock 70kDa protein 1A
- Protein G Purified
- WB, ELISA, ICC, IHC, FACS, IEM
- Tissue Tool:
- Find tissues and cell lines supported by DNA array analysis to express HSPA1A.
- RNA Seq:
- Find tissues and cell lines supported by RNA-seq analysis to express HSPA1A.
- Human Hsp70
- Reconstitution and Storage:
- Store at -20C. Shipping in Blue Ice or 4C.
- Printable datasheet for OASE00001
- 1ug/ml was sufficient for detection of Hsp70 in 20ug of Hela cell lysate
- Additional Information:
- Background Info: Detects a ~70kDa protein corresponding to the molecular mass of inducible Hsp70 on SDS PAGE immunoblots. The mapped epitope is in the region of amino acid residues 436-503. Does not cross-react with Hsc70 (Hsp73).
- 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 44 kDa 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.
- Certificate of Analysis: 1 ug/mL was sufficient for detection of Hsp70 in 20ug of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.
- Storage Buffer:
- PBS pH7.4, 50% glycerol, 0.1% sodium azide
- Target Reference:
- 1. Welch W.J. and Suhan J.P. (1986) J Cell Biol. 103: 2035-2050.
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. Galan A., et al. (2000) J. Biol. Chem. 275: 11418-11424.
8. Kondo T., et al. (2000) J. Biol. Chem. 275: 8872-8879.
9. Misaki T., et al. (1994) Clin. Exp. Immun. 98: 234-239.
10. Pockley A.G., et al. (1998) Immunol. Invest. 27: 367-377.
11. Moon I.S., et al. (2001) Cereb Cortex 11(3): 238-248.
12. Dressel et al. (2000) J. Immunol. 164: 2362-2371.
13. Verma A.K., et al. (2007) Fish and Shellfish Immunology.
14. Banduseela V.C., et al. (2009) Physiol Genomics. 39(3):