Product Name: HSP70

Product Number: AB-NN060-3

Size:	25 µl		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: NN060-3

Antibody Target Type: Pan-specific

Protein UniProt: P0DMV8

Protein SigNET: P0DMV8

Antibody Type: Polyclonal

Antibody Host Species: Rabbit

Antibody Immunogen Source: Full length human protein Hsp70

Production Method: Rabbit antiserum

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

Storage Buffer: Rabbit antiserum

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, Immunoprecipitation, ELISA, Immunohistochemistry, ICC, Immunofluorescence

Antibody Dilution Recommended: 1:25,000 (ECL) (WB), 1:100 (IP)

Antibody Potency: Detects a ~70kDa protein corresponding to the molecular mass of inducible Hsp70 on SDS-PAGE immunoblots.

Antibody Species Reactivity: Human, Mouse, Rat, Beluga, Cow, Dog, Fish (carp), Guinea Pig, Hamster, Monkey, Pig, Sheep, Coral, Tomato, Tobacco, Spiny dogfish shark (Squalus acanthias), Atlantic Hagfish (Myxine glutinosa), Rainbow Trout

Antibody Positive Control: A 1:10,000 dilution of SPC-103 was sufficient for detection of hsp70 in 20μg of HeLa cell lysate by ECL immunoblot analysis.

Antibody Cross Reactivity: May cross-react with Hsc70 at lower dilutions.

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)

Related Product 4: HSP70/HSC70 (pan) pan-specific antibody (Cat. No.: AB-NN060-13)

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 ATPbinding 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.

Figure 1. Immunoblotting of various cell lines with AB-NN059-3 antibody at a 1000 X final dilution. The target protein Hsp70 is indicated. Each lane was loaded with 15 µg of cell lysate protein. The max signal count was 65535.

Figure 2. Immunoblotting of various tissue lines with AB-NN059-3 antibody at a 1000 X final dilution. The target protein Hsp70 is indicated. Each lane was loaded with 15 µg of tissue lysate protein. The max signal count was 30407.

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.