HSP70/HSC70 Antikörper

Produktnummer ABIN361710

Der Maus Monoklonal Anti-HSP70/HSC70-Antikörper wurde für WB, IP, IHC, ICC und IF validiert. Er ist geeignet, HSP70/HSC70 in Proben von Huhn zu detektieren. Es sind 4+ Publikationen verfügbar.

Kurzübersicht für HSP70/HSC70 Antikörper (ABIN361710)

Target: HSP70/HSC70 (HSC70-4) (Heat Shock Protein Cognate 4 (HSC70-4))

Reaktivität: Huhn

Wirt: Maus

Klonalität: Monoklonal

Konjugat: Dieser HSP70/HSC70 Antikörper ist unkonjugiert

Applikation: Western Blotting (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC), Immunocytochemistry (ICC), Immunofluorescence (IF)

Klon: BB70

Produktdetails anti-HSP70/HSC70 Antikörper

Spezifität: Detects ~72 (HSP) and ~73 kDa (HSC).

Kreuzreaktivität: Beluga, Huhn, Rind (Kuh), Hund, Drosophila melanogaster, Fisch, Meerschweinchen, Hamster, Human, Maus, Schwein, Kaninchen, Ratte, Saccharomyces cerevisiae, Schaf, Xenopus laevis

Aufreinigung: Protein G Purified

Immunogen: Chicken HSP70/HSP90 complex

Isotyp: IgG2a

Anwendungsinformationen

Applikationshinweise:

• WB (1:1000)
• IHC (1:200)
• ICC/IF (1:200)
• optimal dilutions for assays should be determined by the user.

Kommentare:

1 μg/ml of ABIN361709 was sufficient for detection of HSP70 and HSC70 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 7.2, 50 % glycerol, 0.09 % 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/HSC70 Antikörper (ABIN361710)

Kang, Taldone, Patel, Patel, Rodina, Gozman, Maharaj, Clement, Patel, Brodsky, Young, Chiosis: "Heat shock protein 70 inhibitors. 1. 2,5'-thiodipyrimidine and 5-(phenylthio)pyrimidine acrylamides as irreversible binders to an allosteric site on heat shock protein 70." in: Journal of medicinal chemistry, Vol. 57, Issue 4, pp. 1188-207, (2014) (PubMed).

Taldone, Kang, Patel, Patel, Patel, Rodina, Patel, Gozman, Maharaj, Clement, Lu, Young, Chiosis et al.: "Heat shock protein 70 inhibitors. 2. 2,5'-thiodipyrimidines, 5-(phenylthio)pyrimidines, 2-(pyridin-3-ylthio)pyrimidines, and 3-(phenylthio)pyridines as reversible binders to an allosteric site on ..." in: Journal of medicinal chemistry, Vol. 57, Issue 4, pp. 1208-24, (2014) (PubMed).

Rodina, Taldone, Kang, Patel, Koren, Yan, DaGama Gomes, Yang, Patel, Shrestha, Ochiana, Santarossa, Maharaj, Gozman, Cox, Erdjument-Bromage, Hendrickson, Cerchietti, Melnick, Guzman, Chiosis: "Affinity purification probes of potential use to investigate the endogenous Hsp70 interactome in cancer." in: ACS chemical biology, Vol. 9, Issue 8, pp. 1698-705, (2014) (PubMed).

Rodina, Patel, Kang, Patel, Baaklini, Wong, Taldone, Yan, Yang, Maharaj, Gozman, Patel, Patel, Chirico, Erdjument-Bromage, Talele, Young, Chiosis: "Identification of an allosteric pocket on human hsp70 reveals a mode of inhibition of this therapeutically important protein." in: Chemistry & biology, Vol. 20, Issue 12, pp. 1469-80, (2013) (PubMed).

Details zu HSP70/HSC70

Target: HSP70/HSC70 (HSC70-4) (Heat Shock Protein Cognate 4 (HSC70-4))

Andere Bezeichnung: HSP70/HSC70

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: 423504

NCBI Accession: NP_001006686

UniProt: P08106