Product Name: HSP70

Product Number: AB-NN060-10

Size:	25 µg		Price:	89.00
			$US

Target Full Name: Heat shock 70 kDa protein 1A

Target Alias: HSP70 1; HSP70 2; HSP70.1; HSP72; HSP73; HSPA1; HSPA1A; HSPA1B

Product Type Specific: Heat shock/stress protein pan-specific antibody

Antibody Code: NN060-10

Antibody Target Type: Pan-specific

Protein UniProt: P0DMV8

Protein SigNET: P0DMV8

Antibody Type: Monoclonal

Antibody Host Species: Mouse

Antibody Ig Isotype Clone: IgG1

Antibody Immunogen Source: Human recombinant HSP70 overexpressed in E.coli

Production Method: Protein G purified

Antibody Modification: Unconjugated. Contact KInexus if you are interest in having the antibody biotinylated or coupled with fluorescent dyes.

Antibody Concentration: 1 mg/ml

Storage Buffer: Phosphate buffered saline pH7.2, 50% glycerol, 0.09% sodium azide

Storage Conditions: For long term storage, keep frozen at -40°C or lower. Stock solution can be kept at +4°C for more than 3 months. Avoid repeated freeze-thaw cycles.

Product Use: Western blotting | Immunohistochemistry | ICC/Immunofluorescence | Immunoprecipitation

Antibody Dilution Recommended: WB (1:5000), ICC/IF (1:500), IP (2µg); optimal dilutions for assays should be determined by the user.

Antibody Potency: Very high potency. Detects a ~70 kDa protein in cell and tissue lysates by Western blotting.

Antibody Species Reactivity: Human | Mouse | Rat | Amphibian | Chicken | Fish | S. cerevisiae | Drosophila | S. flexneri M90T

Antibody Positive Control: 0.2 µg/ml of SMC-164 was sufficient for detection of HSP70 in 20 µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Antibody Specificity: Very high

Antibody Cross Reactivity: May detect HSP70, HSC70, p75 and HSP72.

Related Product 1: HSP70/HSC70 pan-specific antibody (Cat. No.: AB-NN060-11)

Related Product 2: HSP70/HSC70 pan-specific antibody (Cat. No.: AB-NN060-12)

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 5O% identity (1). 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 (2). 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 (3). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (4). 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 (5). 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] Balashova N. et al. (2005) J Biol Chem 280:2186-9

[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. Nat Acad. Sci. USA 89: 7290-7294.

[6] Fink A.L. (1999) Physiol. Rev. 79: 425-449.