Product Name: HSP70/HSC70

Product Number: AB-NN060-12

Size:	50 µg		Price:	89.00
			$US

Target Full Name: Heat shock-related 70 kDa protein 2

Target Alias: HSC54; HSC70; HSC71; HSP70 1; HSP701/HSP70 2; HSP70.1; HSP71; HSP72; HSP73; HSPA1; HSPA10; HSPA1A; HSPA1B; LAP1; NIP71

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

Antibody Code: NN060-12

Antibody Target Type: Pan-specific

Protein UniProt: P54652

Protein SigNET: P54652

Antibody Type: Monoclonal

Antibody Host Species: Mouse

Antibody Ig Isotype Clone: IgG2a

Antibody Immunogen Source: Chicken HSP70/HSP90 complex

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 | Immunoprecipitation

Antibody Dilution Recommended: WB (1:1000), ICC/IF (1:200); optimal dilutions for assays should be determined by the user.

Antibody Potency: Very high potency. Detects a ~72 (HSP) and ~73 kDa protein (HSC) in cell and tissue lysates by Western blotting.

Antibody Species Reactivity: Human | Mouse | Rat | Bovine | Sheep | Dog | Beluga | Fish | Guinea pig | Scallop pig | Hamster | Rabbit | Chicken | Xenopus | Drosophila | Yeast

Antibody Positive Control: 1 µg/ml of SMC-106 was sufficient for detection of HSP70 and HSC70 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

Related Product 1: HSP70 pan-specific antibody (Cat. No.: AB-NN060-10)

Related Product 2: HSP70/HSC70 pan-specific antibody (Cat. No.: AB-NN060-11)

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 (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. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.

References

[1] Zho J. (1998) Cell 94 : 471-480.

[2] Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J.

[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.

[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.