Hsp70/Hsc70 (HSPA2) Antibody – Mouse Monoclonal

Background Info: Detects ~72 and ~73kDa proteins corresponding to the molecular mass of inducible Hsp and Hsc on SDS PAGE immunoblots.

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.

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1. Rodina, A. et al. (2013). Identification of an Allosteric Pocket on Human Hsp70 Reveals a Mode of Inhibition of This Therapeutically Important Protein. Cell Chemistry & Biology. doi: 10.1016/j.chembiol.2013.10.008
2. Kang, Y. et al. (2014). Heat Shock Protein 70 Inhibitors. 1. 2,5'-Thiodipyrimidine and 5-(Phenylthio)pyrimidine Acrylamides as Irreversible Binders to an Allosteric Site on Heat Shock Protein 70. J Med Chem. doi.org/10.1021/jm401551n
3. Taldone, T. et al. (2014). Heat Shock Protein 70 Inhibitors. 2. 2,5'-Thiodipyrimidines, 5-(Phenylthio)pyrimidines, 2-(Pyridin-3-ylthio)pyrimidines, and 3-(Phenylthio)pyridines as Reversible Binders to an Allosteric Site on Heat Shock Protein 70. J Med Chem. doi.org/10.1021/jm401552y
4. Rodina, A. et al. (2014). Affinity Purification Probes of Potential Use To Investigate the
Endogenous Hsp70 Interactome in Cancer. ACS Chem Biol. doi.org/10.1021/cb500256u

Small volumes of anti-HSPA2 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MBS802620 is an antibody targeting HSPA2. Also known as Hsp70/Hsc70 Antibody: ATTO 488. Reactive in Human, Mouse, Rat, Sheep, Dog, Beluga, Bovine, Fish, Guinea pig, Scallop pig, Hamster, Rabbit, Chicken, Xenopus, Drosophila, Yeast. Host: Mouse.