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Heat Shock Protein Cognate 4 (HSC70-4) antibody

Details for Product No. ABIN361709, Supplier: Log in to see
  • BAP74
  • CG4264
  • Dmel\\CG4264
  • E(csp)1545
  • E(nd)195
  • HSC-70
  • HSC4
  • HSC70
  • HSC70-4
  • Hsc-4
  • Hsc4
  • Hsc4p
  • Hsc70
  • Hsp-c4
  • Hsp70
  • anon-WO0118547.237
  • bs17d06.y1
  • dhsc70
  • hsc4
  • hsc70
  • hsc70-4
  • hsp70
  • i190
  • l(3)03550
  • l(3)L3929
  • l(3)j7A4
  • scd
Beluga, Chicken, Cow (Bovine), Dog (Canine), Fish, Fruit Fly (Drosophila melanogaster), Guinea Pig, Hamster, Human, Mouse (Murine), Pig (Porcine), Rabbit, Rat (Rattus), Sheep (Ovine), Xenopus laevis, Yeast
Clonality (Clone)
Monoclonal ()
Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blotting (WB)
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Immunogen Chicken HSP70/HSP90 complex
Clone BB70
Specificity Detects ~72 (HSP) and ~73 kDa (HSC).
Sensitivity 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.
Purification Protein G Purified
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.
Cellular Localization: Cytoplasm
Gene ID 423504
NCBI Accession NP_001006686
UniProt P08106
Application Notes Recommended Dilution: WB (1:1000), IHC (1:200), ICC/IF (1:200), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
 image for anti-Heat Shock Protein Cognate 4 (HSC70-4) antibody (ABIN361709) Hsp70 Hsc70 ( BB70), rat nuclear smears and liver sections (top control).
Product cited in: Rodina, Taldone, Kang et al.: "Affinity purification probes of potential use to investigate the endogenous Hsp70 interactome in cancer." in: ACS chemical biology, Vol. 9, Issue 8, pp. 1698-705, 2014 (PubMed).

Taldone, Kang, Patel et al.: "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 ..." in: Journal of medicinal chemistry, Vol. 57, Issue 4, pp. 1208-24, 2014 (PubMed).

Kang, Taldone, Patel et al.: "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." in: Journal of medicinal chemistry, Vol. 57, Issue 4, pp. 1188-207, 2014 (PubMed).

Rodina, Patel, Kang et al.: "Identification of an allosteric pocket on human hsp70 reveals a mode of inhibition of this therapeutically important protein." in: Chemistry & biology, Vol. 20, Issue 12, pp. 1469-80, 2013 (PubMed).

Background publications Fernandez-Funez, Nino-Rosales, de Gouyon et al.: "Identification of genes that modify ataxin-1-induced neurodegeneration." in: Nature, Vol. 408, Issue 6808, pp. 101-6, 2000 (PubMed).

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

Zou, Guo, Guettouche et al.: "Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1." in: Cell, Vol. 94, Issue 4, pp. 471-80, 1998 (PubMed).

Prapapanich, Chen, Toran et al.: "Mutational analysis of the hsp70-interacting protein Hip." in: Molecular and cellular biology, Vol. 16, Issue 11, pp. 6200-7, 1996 (PubMed).

Smith, Sullivan, Marion et al.: "Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70." in: Molecular and cellular biology, Vol. 13, Issue 2, pp. 869-76, 1993 (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).

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).

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).

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).