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Hsc70 anticorps

Il existe 7+ publications pour ce produit. L’anticorps anti-Hsc70 Monoclonal Souris est utilisé pour la détection de Hsc70 dans des échantillons de Humain, Rat, Souris, Boeuf (Vache), Poulet, Hamster, Chien, Mouton, Porc, Lapin, Cobaye, Singe, Drosophila melanogaster, Xenopus laevis, Beluga, Poisson, Plantes et C. elegans. Il a été validé pour WB, IP, FACS, IHC (fro) et EM.
N° du produit ABIN263939
1.055,38 €
Plus frais de livraison 40,00 € et TVA
0.2 mg
Destination: France
Envoi sous 17 jours ouvrables

Aperçu rapide pour Hsc70 anticorps (ABIN263939)

Antigène

Voir toutes Hsc70 (HSPA8) Anticorps
Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))

Reactivité

  • 104
  • 67
  • 62
  • 22
  • 17
  • 14
  • 12
  • 11
  • 10
  • 10
  • 10
  • 10
  • 8
  • 4
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  • 1
Humain, Rat, Souris, Boeuf (Vache), Poulet, Hamster, Chien, Mouton, Porc, Lapin, Cobaye, Singe, Drosophila melanogaster, Xenopus laevis, Beluga, Poisson, Plantes, C. elegans

Hôte

  • 97
  • 27
  • 9
  • 2
Souris

Clonalité

  • 82
  • 52
Monoclonal

Conjugué

  • 80
  • 20
  • 11
  • 3
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 2
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
Cet anticorp Hsc70 est non-conjugé

Application

  • 121
  • 74
  • 50
  • 43
  • 35
  • 34
  • 21
  • 15
  • 10
  • 10
  • 10
  • 4
  • 3
  • 2
  • 2
  • 2
Western Blotting (WB), Immunoprecipitation (IP), Flow Cytometry (FACS), Immunohistochemistry (Frozen Sections) (IHC (fro)), Electron Microscopy (EM)

Clone

N27F3-4
  • Specificité

    Detects 72 and 73 kDa proteins corresponding to the molecular mass of inducible hsp and hsc70 on SDS PAGE immunoblots.

    Attributs du produit

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

    Purification

    Affinity Chromatography on Protein G.

    Immunogène

    Recombinant hsp70/hsc70 (1)

    Isotype

    IgG1
  • Indications d'application

    Western blot (7,8,9): 1 μg/mL was sufficient for detection of HSP/HSC70 in 20 μg of HeLalysate. Immunoprecipitation (7). Immunohistochemistry (8). Flow Cytometry. Electron Microscopy (8).
    Other applications not tested.
    Optimal dilutions are dependent on conditions and should be determined by the user.

    Restrictions

    For Research Use only
  • Concentration

    1.0 mg/mL

    Buffer

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

    Agent conservateur

    Sodium azide

    Précaution d'utilisation

    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.

    Conseil sur la manipulation

    Avoid repeated freezing and thawing.

    Stock

    4 °C/-20 °C

    Stockage commentaire

    Store the antibody undiluted at 2-8 °C for one month or (in aliquots) at -28 °C for longer.
    Shelf life: one year from despatch.

    Date de péremption

    12 months
  • Silverstein, Ordanes, Wylie, Files, Milligan, Presley, Kavanagh: "Inducing Muscle Heat Shock Protein 70 Improves Insulin Sensitivity and Muscular Performance in Aged Mice." dans: The journals of gerontology. Series A, Biological sciences and medical sciences, Vol. 70, Issue 7, pp. 800-8, (2015) (PubMed).

    Hunter, OHagan, Kenyon, Dhanani, Prinsloo, Edkins: "Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells." dans: PLoS ONE, Vol. 9, Issue 1, pp. e86842, (2014) (PubMed).

    Ghemrawi, Pooya, Lorentz, Gauchotte, Arnold, Gueant, Battaglia-Hsu: "Decreased vitamin B12 availability induces ER stress through impaired SIRT1-deacetylation of HSF1." dans: Cell death & disease, Vol. 4, pp. e553, (2013) (PubMed).

    Sun, Prince, Manjarrez, Scroggins, Matts: "Characterization of the interaction of Aha1 with components of the Hsp90 chaperone machine and client proteins." dans: Biochimica et biophysica acta, Vol. 1823, Issue 6, pp. 1092-101, (2012) (PubMed).

    Modrow, Preusse-Prange, Meyer, Harder, Schwark, von Wurmb-Schwark: "Highly reliable quantification of proteins such as members of the HSP70 superfamily based on the grey scale index via immune detection stained bands on a Western blot." dans: Forensic science international, Vol. 222, Issue 1-3, pp. 256-8, (2012) (PubMed).

    Mutsvunguma, Moetlhoa, Edkins, Luke, Blatch, Knox: "Theiler's murine encephalomyelitis virus infection induces a redistribution of heat shock proteins 70 and 90 in BHK-21 cells, and is inhibited by novobiocin and geldanamycin." dans: Cell stress & chaperones, Vol. 16, Issue 5, pp. 505-15, (2011) (PubMed).

    Chen, Prior, Dargusch, Roberts, Riek, Eichmann, Chiruta, Akaishi, Abe, Maher, Schubert: "A novel neurotrophic drug for cognitive enhancement and Alzheimer's disease." dans: PLoS ONE, Vol. 6, Issue 12, pp. e27865, (2011) (PubMed).

  • Antigène

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

    Autre désignation

    HSPA8 / HSC70

    Sujet

    Hsp70 genes encode abundant heat-inducible 70- kDa hsps (hsp70s). In most eucaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eucaryotes 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: HSP70.1, HSP70.2, HSP73, HSPA10, HSPA1A, HSPA1B, HSPA8, Heat shock 70 kDa protein 1A/1B, Heat shock 70 kDa protein 8, Heat shock cognate 71 kDa protein

    ID gène

    3312

    UniProt

    P11142
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