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Hsc70 Protein (Heat Shock 70kDa Protein 8) (His tag)

HSPA8 Spezies: Human Wirt: Escherichia coli (E. coli) Recombinant >90% AcA, ELISA, Func, SDS, WB Active
Pubmed (6 Referenzen)
Produktnummer ABIN1686679
Zzgl. Versandkosten $45.00
Lieferung in 3 bis 4 Werktagen
  • Target Alle Hsc70 (HSPA8) Proteine anzeigen
    Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))
    Biologische Aktivität
    • 7
    • 3
    • 3
    • 2
    • 2
    • 1
    • 14
    • 1
    • 1
    • 1
    • 1
    Escherichia coli (E. coli)
    Aufreinigungstag / Konjugat
    Dieses Hsc70 Protein ist gelabelt mit His tag.
    Activity Assay (AcA), ELISA, Functional Studies (Func), SDS-PAGE (SDS), Western Blotting (WB)
    ~70 kDa
    The protein has ATPase activity at the time of manufacture of 3.2 µM phosphate liberated/hr/μg protein in a 200 µL reaction at 37 °C (pH 8) in the presence of 20 µL of 1 mM ATP using a Malachite Green assay.
    Affinity Purified
    Biological Activity Comment
    ATPase active
  • Applikationshinweise
    Optimal working dilution should be determined by the investigator.

    This product has been certified >90% pure using SDS-PAGE analysis. The protein has ATPase activity at the time of manufacture of 3.2μM phosphate liberated/hr/μg protein in a 200μl reaction at 37°C (pH 8) in the presence of 20ul of 1mM ATP using a Malachite Green assay.

    Nur für Forschungszwecke einsetzbar
  • Konzentration
    Lot specific
    50 mM Tris/HCl, pH 8, 0.3M NaCl
    -20 °C
  • Liu, Vielhauer, Holzbeierlein, Zhao, Ghosh, Brown, Lee, Blagg: "KU675, a Concomitant Heat-Shock Protein Inhibitor of Hsp90 and Hsc70 that Manifests Isoform Selectivity for Hsp90α in Prostate Cancer Cells." in: Molecular pharmacology, Vol. 88, Issue 1, pp. 121-30, (2015) (PubMed).

    Kimura, Yoshikura, Koumura, Hayashi, Kobayashi, Kobayashi, Yano, Inuzuka: "Identification of target antigens of naturally occurring autoantibodies in cerebrospinal fluid." in: Journal of proteomics, (2015) (PubMed).

    Ravindran, Bagchi, Inoue, Tsai: "A Non-enveloped Virus Hijacks Host Disaggregation Machinery to Translocate across the Endoplasmic Reticulum Membrane." in: PLoS pathogens, Vol. 11, Issue 8, pp. e1005086, (2015) (PubMed).

    Fujiwara, Furuta, Kikuchi, Aizawa, Hatanaka, Konya, Uchida, Yoshimura, Tamai, Wada, Kabuta: "Discovery of a novel type of autophagy targeting RNA." in: Autophagy, Vol. 9, Issue 3, pp. 403-9, (2013) (PubMed).

    Takino, Kobayashi, Takeuchi: "The formation of intracellular glyceraldehyde-derived advanced glycation end-products and cytotoxicity." in: Journal of gastroenterology, Vol. 45, Issue 6, pp. 646-55, (2010) (PubMed).

    Zwang, Hoffert, Pisitkun, Moeller, Fenton, Knepper: "Identification of phosphorylation-dependent binding partners of aquaporin-2 using protein mass spectrometry." in: Journal of proteome research, Vol. 8, Issue 3, pp. 1540-54, (2009) (PubMed).

  • Target
    Hsc70 (HSPA8) (Heat Shock 70kDa Protein 8 (HSPA8))
    Andere Bezeichnung
    Hsc70 (HSPA8 Produkte)
    hsc54, hsc70, hsc71, hsp71, hsp73, hspa10, lap1, nip71, HSC54, HSC70, HSC71, HSP71, HSP73, HSPA10, LAP1, NIP71, Hsc70, 2410008N15Rik, Hsc71, Hsc73, Hsp73, Hspa10, wu:fb01g06, wu:fi48b06, heat shock protein family A (Hsp70) member 8 L homeolog, heat shock protein family A (Hsp70) member 8, heat shock 70kDa protein 8, heat shock protein 8, hspa8.L, HSPA8, Hspa8, hspa8
    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). When cells are subjected to metabolic stress (e.g., heat shock) a member of the HSP 70 family, HSP 70 (HSP72), is expressed, HSP 70 is highly related to HSC70 (>90 % sequence identity). Constitutively expressed HSC70 rapidly forms a stable complex with the highly inducible HSP70 in cells following heat shock. The interaction of HSC70 with HSP 70 is regulated by ATP. These two heat shock proteins move together in the cell experiencing stress. Furthermore, research on HSC70 has implicates it with a role in facilitating the recovery of centrosomal structure and function after heat shock (6).
    approx. 70 kDa
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