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Heat Shock Protein Cognate 4 (HSC70-4) antibody

Details for Product No. ABIN361705, 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, Caenorhabditis elegans (C. elegans), Chicken, Cow (Bovine), Dog (Canine), Fish, Fruit Fly (Drosophila melanogaster), Guinea Pig, Hamster, Human, Monkey, Mouse (Murine), Pig (Porcine), Plant, Rabbit, Rat (Rattus), Sheep (Ovine), Xenopus laevis
Clonality (Clone)
Monoclonal ()
Immunoelectron Microscopy (IEM), Immunocytochemistry (ICC), Flow Cytometry (FACS), Immunofluorescence (IF), Immunoprecipitation (IP), Immunohistochemistry (IHC), Western Blotting (WB)
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Immunogen Recombinant HSP70/HSC70
Clone N27F3-4
Specificity Detects ~72 (HSP) and ~73 kDa (HSC).
Sensitivity 1 µg/mL of SMC-104 was sufficient for detection of Hsp70/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 3303
NCBI Accession NP_005336
UniProt P08107
Application Notes Recommended Dilution: WB (1:1000), IHC (1:100), ICC/IF (1:50), 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 (ABIN361705) Hsp70 (N27), cell lines.
Product cited in: Preusse-Prange, Modrow, Schwark et al.: "Detection of constitutive and inducible HSP70 proteins in formalin fixed human brain tissue." in: Forensic science international, Vol. 235, pp. 62-7, 2014 (PubMed).

Morshed, Ma, Latif et al.: "How one TSH receptor antibody induces thyrocyte proliferation while another induces apoptosis." in: Journal of autoimmunity, Vol. 47, pp. 17-24, 2013 (PubMed).

Modrow, Preusse-Prange, Meyer et al.: "Highly reliable quantification of proteins such as members of the HSP70 superfamily based on the grey scale index via immune detection stained bands on a Western blot." in: Forensic science international, Vol. 222, Issue 1-3, pp. 256-8, 2012 (PubMed).

Sun, Prince, Manjarrez et al.: "Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins." in: Biochimica et biophysica acta, Vol. 1823, Issue 6, pp. 1092-101, 2012 (PubMed).

Chen, Prior, Dargusch et al.: "A novel neurotrophic drug for cognitive enhancement and Alzheimer's disease." in: PLoS ONE, Vol. 6, Issue 12, pp. e27865, 2011 (PubMed).

Mutsvunguma, Moetlhoa, Edkins et al.: "Theiler's murine encephalomyelitis virus infection induces a redistribution of heat shock proteins 70 and 90 in BHK-21 cells, and is inhibited by novobiocin and geldanamycin." in: Cell stress & chaperones, Vol. 16, Issue 5, pp. 505-15, 2011 (PubMed).

Olkku, Leskinen, Lammi et al.: "Ultrasound-induced activation of Wnt signaling in human MG-63 osteoblastic cells." in: Bone, Vol. 47, Issue 2, pp. 320-30, 2010 (PubMed).

Background publications Kabakov, Budagova, Latchman et al.: "Stressful preconditioning and HSP70 overexpression attenuate proteotoxicity of cellular ATP depletion." in: American journal of physiology. Cell physiology, Vol. 283, Issue 2, pp. C521-34, 2002 (PubMed).

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

Polanowska-Grabowska, Simon, Falchetto et al.: "Platelet adhesion to collagen under flow causes dissociation of a phosphoprotein complex of heat-shock proteins and protein phosphatase 1." in: Blood, Vol. 90, Issue 4, pp. 1516-26, 1997 (PubMed).

Ricart, Egea, Izquierdo et al.: "Subcellular structure containing mRNA for beta subunit of mitochondrial H+-ATP synthase in rat hepatocytes is translationally active." in: The Biochemical journal, Vol. 324 ( Pt 2), pp. 635-43, 1997 (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).

Schnell, Kessler, Blobel: "Isolation of components of the chloroplast protein import machinery." in: Science (New York, N.Y.), Vol. 266, Issue 5187, pp. 1007-12, 1994 (PubMed).

Hang, Fox: "Expression of hsp70 induced in CHO cells by 45.0 degrees C hyperthermia is cell cycle associated and DNA synthesis dependent." in: Cytometry, Vol. 19, Issue 2, pp. 119-25, 1995 (PubMed).

Welch, Suhan: "Cellular and biochemical events in mammalian cells during and after recovery from physiological stress." in: The Journal of cell biology, Vol. 103, Issue 5, pp. 2035-52, 1987 (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).