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Hsc70 Antikörper

Der Maus Monoklonal Anti-Hsc70-Antikörper wurde für WB, IP, IF und IHC (fro) validiert. Er ist geeignet, Hsc70 in Proben von Human, Ratte, Maus, Rind (Kuh), Huhn, Hamster, Hund, Schaf, Kaninchen, Schwein, Meerschweinchen, Drosophila melanogaster, Xenopus laevis, Saccharomyces cerevisiae, Beluga, Fisch, Artemia sp. (Brine shrimp), Pinctada fucata (Pearl oyster) und Kammmuschel zu detektieren. Es sind 6+ Publikationen verfügbar.
Produktnummer ABIN263942

Kurzübersicht für Hsc70 Antikörper (ABIN263942)

Target

Alle Hsc70 (HSPA8) Antikörper anzeigen
Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))

Reaktivität

  • 90
  • 50
  • 43
  • 20
  • 16
  • 9
  • 8
  • 6
  • 6
  • 6
  • 5
  • 5
  • 5
  • 4
  • 4
  • 3
  • 3
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
Human, Ratte, Maus, Rind (Kuh), Huhn, Hamster, Hund, Schaf, Kaninchen, Schwein, Meerschweinchen, Drosophila melanogaster, Xenopus laevis, Saccharomyces cerevisiae, Beluga, Fisch, Artemia sp. (Brine shrimp), Pinctada fucata (Pearl oyster), Kammmuschel

Wirt

  • 92
  • 31
  • 5
  • 2
Maus

Klonalität

  • 87
  • 42
Monoklonal

Konjugat

  • 76
  • 22
  • 15
  • 4
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
Dieser Hsc70 Antikörper ist unkonjugiert

Applikation

  • 117
  • 80
  • 54
  • 42
  • 39
  • 38
  • 18
  • 10
  • 10
  • 10
  • 10
  • 5
  • 4
  • 2
  • 2
  • 2
Western Blotting (WB), Immunoprecipitation (IP), Immunofluorescence (IF), Immunohistochemistry (Frozen Sections) (IHC (fro))

Klon

BB70
  • Spezifität

    Detects 72 and 73 kDa proteins corresponding to the Molecular Mass of inducible HSP and HSC70 on SDS PAGE Immunoblots.

    Produktmerkmale

    Synonyms: HSP73, HSPA10, Heat shock cognate 71 kDa protein, Heat shock 70 kDa protein 8

    Aufreinigung

    Affinity Chromatography on Protein G

    Immunogen

    Chicken Hsp70/Hsp90 complex (1)

    Isotyp

    IgG2a
  • Applikationshinweise

    Western blot (7): 1 μg/mL was sufficient for detection of hsp70/Hsc70 in 20 g of HeLalysate.

    Beschränkungen

    Nur für Forschungszwecke einsetzbar
  • Konzentration

    1.0 mg/mL

    Buffer

    PBS pH 7.2, 0.09 % Sodium Azide, 50 % Glycerol

    Konservierungsmittel

    Sodium azide

    Vorsichtsmaßnahmen

    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.

    Handhabung

    Avoid repeated freezing and thawing.

    Lagerung

    4 °C/-20 °C

    Informationen zur Lagerung

    Store the antibody at 2 - 8 °C up to one month or (in aliquots) at -20 °C for longer.
    Shelf life: one year from despatch.

    Haltbarkeit

    12 months
  • Vavilis, Delivanoglou, Aggelidou, Stamoula, Mellidis, Kaidoglou, Cheva, Pourzitaki, Chatzimeletiou, Lazou, Albani, Kritis: "Oxygen-Glucose Deprivation (OGD) Modulates the Unfolded Protein Response (UPR) and Inflicts Autophagy in a PC12 Hypoxia Cell Line Model." in: Cellular and molecular neurobiology, Vol. 36, Issue 5, pp. 701-12, (2016) (PubMed).

    Stamoula, Vavilis, Aggelidou, Kaidoglou, Cheva, Mellidis, Lazou, Haitoglou, Albani, Kritis: "Low Dose Administration of Glutamate Triggers a Non-Apoptotic, Autophagic Response in PC12 Cells." in: Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, Vol. 37, Issue 5, pp. 1750-8, (2015) (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).

    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).

    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).

  • Target

    Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))

    Andere Bezeichnung

    HSPA8 / 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 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.Synonyms: HSP73, HSPA10, Heat shock 70 kDa protein 8, Heat shock cognate 71 kDa protein

    Gen-ID

    3312

    UniProt

    P11142
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