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Product Name
Hsp70: FITC Conjugate
Catalog #
SMC-103B
Alternative Names
Hsp70 1, Hsp70 2, Hsp70.1, Hsp72, Hsp73, HSPA1, HSPA1A, HSPA1B
Clone Number
C92F3A-5
Immunogen
Human Hsp70
Accession Number
NP_005336.3
Gene ID
3303
SwissProt
P08107
Applications
FACS, Flow cytometry
Host Species
Mouse
Isotype
IgG
Species Reactivity
Human, Mouse, Rat, Bovine, Canine, Chicken, Drosophila, Fish (carp), Guinea pig, Hamster, Monkey, Pig, Rabbit, Sheep
Recommended Dilutions
1:1000
Form
Protein G Purified
Storage Buffer
PBS pH7.2, 50% glycerol
Concentration
0.33mg/mL
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).
Conjugate
FITC
Package Size
200ug
Storage Temp
4°C
Shipping Temp
Blue Ice or 4°C
Datasheet
SMC 103 Heat Shock Protein 70 (Hsp70)
Research Area
Chaperones, Heat Shock, Trafficking
Certificate of Analysis
100 μg/mL of SMC-103 was sufficient for detection of Hsp70 in human Jurkat cells by FACS analysis.
Price
$314.00 USD Add to Cart

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 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.
References
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. 22(5): 547-555.
14. Banduseela V.C., et al. (2009) Physiol Genomics. 39(3): 141-159.

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