anti-HSP70 antibody (Heat Shock Protein 70)

Details for Product anti-HSP70 Antibody No. ABIN361707
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HSP70, HEAT SHOCK PROTEIN 70, HEAT SHOCK PROTEIN 70-7, HSC70-7, K9P8.5, K9P8_5, chloroplast heat shock protein 70-2, cpHsc70-2, F19K16.12, F19K16_12, LOC100305036, hsc70, CG31354, Hsp70Bb, hsp70B, hsp ... show more
HSP70, HEAT SHOCK PROTEIN 70, HEAT SHOCK PROTEIN 70-7, HSC70-7, K9P8.5, K9P8_5, chloroplast heat shock protein 70-2, cpHsc70-2, F19K16.12, F19K16_12, LOC100305036, hsc70, CG31354, Hsp70Bb, hsp70B, hsp70Bb-prime, DmelCG5834, CG5834, APG-2, HS24/P52, HSPH2, RY, hsp70, hsp70RY, hsc71, Hsp70, Hsp70-1, Hsp70.1, hsp68, Hsp110, irp94, HSPA1, HSP70B', HSPA6, ARABIDOPSIS HEAT SHOCK PROTEIN 70, ATHSP70, heat shock protein 70, hsp70-5 show less
Caenorhabditis elegans (C. elegans), Carp, Chicken, Cow (Bovine), Dog (Canine), Fruit Fly (Drosophila melanogaster), Guinea Pig, Hamster, Human, Monkey, Mouse (Murine), Pig (Porcine), Rabbit, Rat (Rattus), Sheep (Ovine)
(587), (269), (255), (116), (112), (103), (96), (70), (65), (60), (56), (55), (55), (50), (49), (41), (40), (35), (33), (25), (24), (22), (20), (20), (19), (19), (19), (12), (11), (8), (6), (5), (5), (4), (4), (4), (4), (4), (3), (3), (3), (3), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
(383), (313), (40), (18)
Clonality (Clone)
Monoclonal ()
This HSP70 antibody is un-conjugated
(37), (34), (26), (21), (21), (19), (19), (19), (19), (19), (19), (19), (19), (19), (19), (19), (18), (7), (6), (6), (6), (6), (6), (6), (6), (3), (1), (1)
BioImaging (BI), ELISA, Flow Cytometry (FACS), Immunocytochemistry (ICC), Immunoelectron Microscopy (IEM), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blotting (WB)
(658), (277), (265), (265), (246), (232), (94), (87), (60), (52), (30), (18), (16), (9), (4), (3), (2), (1), (1), (1)
Pubmed 18 references available
Quantity 50 μg
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Request Want additional data for this product?

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Immunogen Human HSP70
Clone C92F3A-5
Specificity Detects a ~70 kDa. Does not cross-react with HSC70 (HSP73).
Sensitivity 1 µg/mL of SMC-100 was sufficient for detection of Hsp70 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
Alternative Name HSP70 (HSP70 Antibody Abstract)
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
Research Area Cancer, Heat Shock Proteins, Signaling
Application Notes Recommended Dilution: WB (1:1000) IHC (1:10,000), ICC/IF (1:1000)
Optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.1 % 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
anti-Heat Shock Protein 70 (HSP70) antibody Hsp70 (C92) Mouse Melanoma.
anti-Heat Shock Protein 70 (HSP70) antibody (2) Hsp70 (C92), cell lines.
Product cited in: Bauckman, Haller, Flores et al.: "Iron modulates cell survival in a Ras- and MAPK-dependent manner in ovarian cells." in: Cell death & disease, Vol. 4, pp. e592, 2013 (PubMed).

Patterson, Ward, Combs et al.: "Heat Shock Protein 70 Prevents both Tau Aggregation and the Inhibitory Effects of Preexisting Tau Aggregates on Fast Axonal Transport." in: Biochemistry, 2011 (PubMed). Further details: 0.2 ug/ml

Larkins, Murphy, Lamb: "Absolute amounts and diffusibility of HSP72, HSP25 and {alpha}B-crystallin in fast- and slow-twitch skeletal muscle fibers of rat." in: American journal of physiology. Cell physiology, 2011 (PubMed). (1:500).

Mitsuhashi, Yamaguchi, Kojima et al.: "Effects of HSP70 on the compression force-induced TNF-α and RANKL expression in human periodontal ligament cells." in: Inflammation research : official journal of the European Histamine Research Society ... [et al.], Vol. 60, Issue 2, pp. 187-94, 2011 (PubMed).

Background publications Banduseela, Ochala, Chen et al.: "Gene expression and muscle fiber function in a porcine ICU model." in: Physiological genomics, Vol. 39, Issue 3, pp. 141-59, 2009 (PubMed).

Verma, Pal, Manush et al.: "Persistent sub-lethal chlorine exposure augments temperature induced immunosuppression in Cyprinus carpio advanced fingerlings." in: Fish & shellfish immunology, Vol. 22, Issue 5, pp. 547-55, 2007 (PubMed).

Moon, Park, Schenker et al.: "Presence of both constitutive and inducible forms of heat shock protein 70 in the cerebral cortex and hippocampal synapses." in: Cerebral cortex (New York, N.Y. : 1991), Vol. 11, Issue 3, pp. 238-48, 2001 (PubMed).

Galán, García-Bermejo, Troyano et al.: "Stimulation of p38 mitogen-activated protein kinase is an early regulatory event for the cadmium-induced apoptosis in human promonocytic cells." in: The Journal of biological chemistry, Vol. 275, Issue 15, pp. 11418-24, 2000 (PubMed).

Kondo, Matsuda, Tashima et al.: "Suppression of heat shock protein-70 by ceramide in heat shock-induced HL-60 cell apoptosis." in: The Journal of biological chemistry, Vol. 275, Issue 12, pp. 8872-9, 2000 (PubMed).

Dressel, Elsner, Quentin et al.: "Heat shock protein 70 is able to prevent heat shock-induced resistance of target cells to CTL." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 164, Issue 5, pp. 2362-71, 2000 (PubMed).

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

Pockley, Shepherd, Corton: "Detection of heat shock protein 70 (Hsp70) and anti-Hsp70 antibodies in the serum of normal individuals." in: Immunological investigations, Vol. 27, Issue 6, pp. 367-77, 1999 (PubMed).

Misaki, Takeuchi, Miyamoto et al.: "Induction in vitro of 72-kD heat shock protein in a continuous culture of rat thyroid cells, FRTL5." in: Clinical and experimental immunology, Vol. 98, Issue 2, pp. 234-9, 1994 (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).

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

Validation Images
Catalog No. ABIN361707
225.50 $
Plus shipping costs $45.00
50 μg
225.50 $

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