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HSP70 antibody (Heat Shock Protein 70)

Details for Product anti-HSP70 Antibody No. ABIN361707, Supplier: Login to see New
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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)
(556), (256), (255), (110), (109), (98), (93), (70), (62), (59), (58), (57), (53), (48), (47), (39), (38), (35), (34), (24), (24), (23), (21), (18), (18), (18), (8), (6), (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)
(359), (296), (40), (18)
Clonality (Clone)
Monoclonal ()
This HSP70 antibody is un-conjugated
(32), (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), (2), (1), (1), (1)
BioImaging (BI), Immunoelectron Microscopy (IEM), Immunocytochemistry (ICC), Flow Cytometry (FACS), Immunofluorescence (IF), Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
(624), (275), (253), (250), (238), (222), (90), (83), (55), (51), (28), (17), (13), (9), (3), (2), (2), (1), (1), (1)
Pubmed 21 references available
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Quantity 50 μg
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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 Heat Shock Proteins
Application Notes Recommended Dilution: WB (1:1000), IHC (1:10000), ICC/IF (1:1000), FACS (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
 image for anti-HSP70 antibody (Heat Shock Protein 70) (ABIN361707) Hsp70 (C92) Mouse Melanoma.
 image for anti-HSP70 antibody (Heat Shock Protein 70) (ABIN361707) Hsp70 (C92), cell lines.
Product cited in: Katoh, Kubota, Kita et al.: "Heat shock protein 70 regulates degradation of the mumps virus phosphoprotein via the ubiquitin-proteasome pathway." in: Journal of virology, Vol. 89, Issue 6, pp. 3188-99, 2015 (PubMed).

Richter, Viergutz, Schwerin et al.: "Prostaglandin E synthase interacts with inducible heat shock protein 70 after heat stress in bovine primary dermal fibroblast cells." in: Cytometry. Part A : the journal of the International Society for Analytical Cytology, Vol. 87, Issue 1, pp. 61-7, 2014 (PubMed).

Engels, Bilgic, Pinto et al.: "A cardiopulmonary bypass with deep hypothermic circulatory arrest rat model for the investigation of the systemic inflammation response and induced organ damage." in: Journal of inflammation (London, England), Vol. 11, pp. 26, 2014 (PubMed).

Dang, Tanabe, Tanaka et al.: "Fasting enhances TRAIL-mediated liver natural killer cell activity via HSP70 upregulation." in: PLoS ONE, Vol. 9, Issue 10, pp. e110748, 2014 (PubMed).

Ishikawa, Sakurai: "Heat-induced expression of the immediate-early gene IER5 and its involvement in the proliferation of heat-shocked cells." in: The FEBS journal, Vol. 282, Issue 2, pp. 332-40, 2015 (PubMed).

Berger, Ivanova, Gareau et al.: "Direct binding of the Alu binding protein dimer SRP9/14 to 40S ribosomal subunits promotes stress granule formation and is regulated by Alu RNA." in: Nucleic acids research, Vol. 42, Issue 17, pp. 11203-17, 2014 (PubMed).

Kanegasaki, Matsushima, Shiraishi et al.: "Macrophage inflammatory protein derivative ECI301 enhances the alarmin-associated abscopal benefits of tumor radiotherapy." in: Cancer research, Vol. 74, Issue 18, pp. 5070-8, 2014 (PubMed).

Muralidharan, Ambade, Fulham et al.: "Moderate alcohol induces stress proteins HSF1 and hsp70 and inhibits proinflammatory cytokines resulting in endotoxin tolerance." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 193, Issue 4, pp. 1975-87, 2014 (PubMed).

Eroglu, Kimbler, Pang et al.: "Therapeutic inducers of the HSP70/HSP110 protect mice against traumatic brain injury." in: Journal of neurochemistry, Vol. 130, Issue 5, pp. 626-41, 2014 (PubMed).

Akkad, Corpeno, Larsson: "Masseter muscle myofibrillar protein synthesis and degradation in an experimental critical illness myopathy model." in: PLoS ONE, Vol. 9, Issue 4, pp. e92622, 2014 (PubMed).

Wijeratne, Xu, Scherz-Shouval et al.: "Structure-activity relationships for withanolides as inducers of the cellular heat-shock response." in: Journal of medicinal chemistry, Vol. 57, Issue 7, pp. 2851-63, 2014 (PubMed).

Sheppard, Sun, Khammash et al.: "Overexpression of heat shock protein 72 attenuates NF-κB activation using a combination of regulatory mechanisms in microglia." in: PLoS computational biology, Vol. 10, Issue 2, pp. e1003471, 2014 (PubMed).

Aare, Radell, Eriksson et al.: "Effects of corticosteroids in the development of limb muscle weakness in a porcine intensive care unit model." in: Physiological genomics, Vol. 45, Issue 8, pp. 312-20, 2013 (PubMed).

Larkins, Murphy, Lamb: "Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers." in: American journal of physiology. Cell physiology, Vol. 303, Issue 6, pp. C654-65, 2012 (PubMed).

Abisambra, Jinwal, Suntharalingam et al.: "DnaJA1 antagonizes constitutive Hsp70-mediated stabilization of tau." in: Journal of molecular biology, Vol. 421, Issue 4-5, pp. 653-61, 2012 (PubMed).

Santagata, Xu, Wijeratne et al.: "Using the heat-shock response to discover anticancer compounds that target protein homeostasis." in: ACS chemical biology, Vol. 7, Issue 2, pp. 340-9, 2012 (PubMed).

Aare, Ochala, Norman et al.: "Mechanisms underlying the sparing of masticatory versus limb muscle function in an experimental critical illness model." in: Physiological genomics, Vol. 43, Issue 24, pp. 1334-50, 2011 (PubMed).

Wood, Pring, Eveson et al.: "Co-overexpression of Bag-1 and heat shock protein 70 in human epidermal squamous cell carcinoma: Bag-1-mediated resistance to 5-fluorouracil-induced apoptosis." in: British journal of cancer, Vol. 104, Issue 9, pp. 1459-71, 2011 (PubMed).

Batista-Nascimento, Neef, Liu et al.: "Deciphering human heat shock transcription factor 1 regulation via post-translational modification in yeast." in: PLoS ONE, Vol. 6, Issue 1, pp. e15976, 2011 (PubMed).

Fernández-Llama, Khositseth, Gonzales et al.: "Tamm-Horsfall protein and urinary exosome isolation." in: Kidney international, Vol. 77, Issue 8, pp. 736-42, 2010 (PubMed).

Xu, Marron, Seddon et al.: "2,3-Dihydrowithaferin A-3beta-O-sulfate, a new potential prodrug of withaferin A from aeroponically grown Withania somnifera." in: Bioorganic & medicinal chemistry, Vol. 17, Issue 6, pp. 2210-4, 2009 (PubMed).

Catalog No. ABIN361707
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