Product Name: HSP70 (Crab)

Product Number: AB-NN060-5

Size:	25 µg		Price:	89.00
			$US

Target Full Name: Heat shock-related 70 kDa protein

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

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

Antibody Code: NN060-5

Antibody Target Type: Pan-specific

Protein UniProt: P08107

Protein SigNET: P08107

Antibody Type: Polyclonal

Antibody Host Species: Rabbit

Antibody Ig Isotype Clone: N/A

Antibody Immunogen Source: Crab protein peptide: NDQGNRTTPSYVA, 100% identical to a wide variety of species including Mouse, Rat, Drosophilia, Rice, Arabidopsis, Bovine, Nematode, Bonobos.

Production Method: Protein A 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: 1X Phosphate buffered saline pH7.4, 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

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

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

Antibody Species Reactivity: Crab

Antibody Positive Control: 1 µg/ml of SPC-318 was sufficient for detection of HSP70 in 20 µg of crab muscle lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

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)

Related Product 3: 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, 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] 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] Hung T.H. et al. (2001) Am J Pathol. 159: 1031-1043.

[8] Locke M. (2000) Cell Stress & Chaperones 5: 45-51.

[9] Ianaro A. et al. (2001) FEBS Lett. 508: 61-66.

[10] Trentin G.A. et al. (2001) J Biol Chem. 276: 13087-13095.