Heat Shock 70kDa Protein 4 (HSPA4) antibody

Antigen: Heat Shock 70kDa Protein 4 (HSPA4)

Synonyms: DKFZp459F0933

Clonality: Monoclonal (3A3)

Host: Mouse

Reactivity: Human, Mouse (Murine), Rat (Rattus), Amphibian, Chicken, Fish, Saccharomyces cerevisiae (S. cerevisiae), Fruit Fly (Drosophila melanogaster)

Conjugate: Un-conjugated

Application: Immunocytochemistry (ICC), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blotting (WB)

Catalog no.: ABIN361737

Additional Information

Alternative name: Hsp70

Gene ID: 3303

UniProt: P08107

Immunogen: Human Recombinant Hsp70 overexpressed in E.coli

Isotype: IgG1

Clone: 3A3

Description: 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. 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. 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. The structure of this ATP binding domain displays multiple features of nucleotide binding proteins. 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. 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.

Synonyms: Hsp70 1, Hsp70 2, Hsp70.1, Hsp72, Hsp73, HSPA1, HSPA1A, HSPA1B

Characteristics: Accession Number: NP_005336.3

Specificity: Detects several members of the heat shock protein 70kDa gene family including Hsp70, Hsc70, p75 and following heat shock, Hsp72 from yeast, Drosophila, fish, mouse, avian, amphibian and human samples.

Sensitivity: 0.2 µg/mL of SMC-164 was sufficient for detection of Hsp70 in 20µg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody.

Application Details

Application Notes: ICC: 1/500, WB: 1/5000 by ECL, IP: 1-2ug

Concentration: 1mg/mL

Purification: Protein G Purified

Buffer: PBS pH7.2, 50% glycerol

Storage: Store at -20° C. Shipping Conditions: Blue Ice or 4° C

Storage Shipping Temp Max: Blue Ice or 4 °C

Research Area: Heat Shock Proteins, Cancer, Signaling

Restrictions: For Research Use only

Images

Hsp70 (3A3), Artemia franciscanna Picture courtesy of Alison King.

Publications

Bork, Sander, Valencia: "An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, Issue 16, pp. 7290-4, 1992 (PubMed).

DeLuca-Flaherty, McKay, Parham et al.: "Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis." in: Cell, Vol. 62, Issue 5, pp. 875-87, 1990 (PubMed).

Rothman: "Polypeptide chain binding proteins: catalysts of protein folding and related processes in cells." in: Cell, Vol. 59, Issue 4, pp. 591-601, 1990 (PubMed).

Boorstein, Ziegelhoffer, Craig: "Molecular evolution of the HSP70 multigene family." in: Journal of molecular evolution, Vol. 38, Issue 1, pp. 1-17, 1994 (PubMed).

Fink: "Chaperone-mediated protein folding." in: Physiological reviews, Vol. 79, Issue 2, pp. 425-49, 1999 (PubMed).