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HSP70 antibody (Heat Shock Protein 70) FITC

Details for Product anti-HSP70 Antibody No. ABIN361671, Supplier: Login to see New
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Chicken, Cow (Bovine), Crab, Dog (Canine), Fruit Fly (Drosophila melanogaster), Guinea Pig, Hamster, Human, Monkey, Pig (Porcine), Rabbit, Rat (Rattus), Sheep (Ovine)
(568), (258), (257), (111), (110), (96), (94), (71), (62), (59), (59), (58), (54), (49), (48), (40), (39), (35), (35), (25), (24), (23), (21), (18), (18), (18), (9), (8), (5), (4), (4), (4), (4), (4), (3), (3), (3), (3), (3), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1)
(367), (302), (40), (18)
Clonality (Clone)
Monoclonal ()
This HSP70 antibody is conjugated to FITC
(34), (32), (24), (21), (21), (19), (19), (19), (19), (19), (19), (19), (19), (19), (19), (19), (17), (7), (6), (5), (5), (5), (5), (5), (5), (5), (3), (1), (1), (1)
Flow Cytometry (FACS)
(636), (281), (256), (254), (243), (222), (94), (89), (55), (52), (31), (18), (16), (9), (3), (2), (2), (1), (1), (1)
Pubmed 14 references available
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Quantity 50 μg
Shipping to United States ( )
Immunogen Human Hsp70
Clone C92F3A-5
Isotype IgG1
Specificity Detects a approx. 70 kDa protein corresponding to the molecular mass of inducible Hsp70 on SDS PAGE immunoblots. The mapped epitope is in the region of AA 436-503.
Cross-Reactivity (Details) Does not cross-react with Hsc70 (Hsp73).
Sensitivity 100 µg/mL of SMC-103 was sufficient for detection of Hsp70 in human Jurkat cells by FACS analysis.
Purification Protein G Purified
Alternative Name Hsp70 (HSP70 Antibody Abstract)
Background Synonyms:
Hsp70 1, Hsp70 2, Hsp70.1, Hsp72, Hsp73, HSPA1, HSPA1A, HSPA1B
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 proteinsand 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.
Gene ID 3303
NCBI Accession NP_005336
UniProt P08107
Research Area Cancer, Heat Shock Proteins, Signaling
Application Notes Recommended Dilution: 1:1000
Restrictions For Research Use only
Concentration 0.33 mg/mL
Buffer PBS pH 7.2, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use WARNING: Reagents contain sodium azide. Sodium azide is very toxic if ingested or inhaled. Avoid contact with skin, eyes, or clothing. Wear eye or face protection when handling. If skin or eye contact occurs, wash with copious amounts of water. If ingested or inhaled, contact a physician immediately. Sodium azide yields toxic hydrazoic acid under acidic conditions. Dilute azide-containing compounds in running water before discarding to avoid accumulation of potentially explosive deposits in lead or copper plumbing.
Handling Advice Avoid repeated freezing and thawing. This product is photosensitive and should be protected from light.
Storage 4 °C
Supplier Images
Flow Cytometry (FACS) image for anti-HSP70 antibody (Heat Shock Protein 70)  FITC (ABIN361671) FACS Hsp70 copy.
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).

Catalog No. ABIN361671

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