HSP70 Antikörper

Produktnummer ABIN361707

Produktdetails anti-HSP70 Antikörper

Target: HSP70 (Heat Shock Protein 70 (HSP70))

Reaktivität: Human

Wirt: Maus

Klonalität: Monoklonal

Konjugat: Dieser HSP70 Antikörper ist unkonjugiert

Applikation: Western Blotting (WB), ELISA, Immunohistochemistry (IHC), Immunofluorescence (IF), Immunocytochemistry (ICC), Flow Cytometry (FACS), Antibody Array (AA), Immunoelectron Microscopy (IEM), BioImaging (BI)

Spezifität: Detects ~70 kDa. Does not cross-react with HSC70 (HSP73).

Kreuzreaktivität: C. elegans, Karpfen, Huhn, Rind (Kuh), Hund, Drosophila melanogaster, Meerschweinchen, Hamster, Human, Affe, Maus, Schwein, Kaninchen, Ratte, Schaf

Aufreinigung: Protein G Purified

Immunogen: Human HSP70

Klon: C92F3A-5

Isotyp: IgG1

Anwendungsinformationen

Applikationshinweise:

• WB (1:1000)
• IHC (1:10000)
• ICC/IF (1:1000)
• FACS (1:1000)
• optimal dilutions for assays should be determined by the user.

Kommentare:

1 μg/ml of ABIN361707 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.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Konzentration: 1 mg/mL

Buffer: PBS pH 7.4, 50 % glycerol, 0.1 % sodium azide, Storage buffer may change when conjugated

Konservierungsmittel: Sodium azide

Vorsichtsmaßnahmen: This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

Lagerung: -20 °C

Informationen zur Lagerung: -20°C

Referenzen für anti-HSP70 Antikörper (ABIN361707)

Kuta, Larochelle, Fernandez, Pal, Minotti, Tibshirani, St Louis, Gentil, Nalbantoglu, Hermann, Durham et al.: "Depending on the stress, histone deacetylase inhibitors act as heat shock protein co-inducers in motor neurons and potentiate arimoclomol, exerting neuroprotection through multiple mechanisms in ALS ..." in: Cell stress & chaperones, Vol. 25, Issue 1, pp. 173-191, (2020) (PubMed).

Bhattacharya, Bernasconi, Picard: "Luminescence resonance energy transfer between genetically encoded donor and acceptor for protein-protein interaction studies in the molecular chaperone HSP70/HSP90 complexes." in: Scientific reports, Vol. 8, Issue 1, pp. 2801, (2019) (PubMed).

Qiao, Jin, Pang, Moskophidis, Mivechi: "The transcriptional regulator of the chaperone response HSF1 controls hepatic bioenergetics and protein homeostasis." in: The Journal of cell biology, Vol. 216, Issue 3, pp. 723-741, (2017) (PubMed).

Dayalan Naidu, Sutherland, Zhang, Risco, de la Vega, Caunt, Hastie, Lamont, Torrente, Chowdhry, Benjamin, Keyse, Cuenda, Dinkova-Kostova: "Heat Shock Factor 1 Is a Substrate for p38 Mitogen-Activated Protein Kinases." in: Molecular and cellular biology, Vol. 36, Issue 18, pp. 2403-17, (2017) (PubMed).

Ogilvie, Cacciani, Akkad, Larsson: "Targeting Heat Shock Proteins Mitigates Ventilator Induced Diaphragm Muscle Dysfunction in an Age-Dependent Manner." in: Frontiers in physiology, Vol. 7, pp. 417, (2016) (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).

Katoh, Kubota, Kita, Nakatsu, Aoki, Mori, Maenaka, Takeda, Kidokoro: "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).

Chittoor-Vinod, Lee, Judge, Notterpek: "Inducible HSP70 is critical in preventing the aggregation and enhancing the processing of PMP22." in: ASN neuro, Vol. 7, Issue 1, (2015) (PubMed).

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

Wijeratne, Xu, Scherz-Shouval, Marron, Rocha, Liu, Costa-Lotufo, Santagata, Lindquist, Whitesell, Gunatilaka: "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).

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).

Eroglu, Kimbler, Pang, Choi, Moskophidis, Yanasak, Dhandapani, Mivechi: "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).

Muralidharan, Ambade, Fulham, Deshpande, Catalano, Mandrekar: "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).

Kanegasaki, Matsushima, Shiraishi, Nakagawa, Tsuchiya: "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).

Berger, Ivanova, Gareau, Scherrer, Mazroui, Strub: "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).

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

Engels, Bilgic, Pinto, Vasquez, Wollschläger, Steinbrenner, Kellermann, Akhyari, Lichtenberg, Boeken: "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).

Richter, Viergutz, Schwerin, Weitzel: "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).

Seguin, Morelli, Vinet, Amore, De Biasi, Poletti, Rubinsztein, Carra: "Inhibition of autophagy, lysosome and VCP function impairs stress granule assembly." in: Cell death and differentiation, Vol. 21, Issue 12, pp. 1838-51, (2014) (PubMed).

Bauckman, Haller, Flores, Nanjundan: "Iron modulates cell survival in a Ras- and MAPK-dependent manner in ovarian cells." in: Cell death & disease, Vol. 4, pp. e592, (2013) (PubMed).

Details zu HSP70

Target: HSP70 (Heat Shock Protein 70 (HSP70))

Andere Bezeichnung: HSP70 (HSP70 Produkte)

Hintergrund: 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 50 % 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. For more information visit our HSP70 Scientific Resource Guide at http://www.HSP70.com.

Gen-ID: 3303

NCBI Accession: NP_005336

UniProt: P0DMV8, P0DMV9