Hsc70 Protein (His tag)

N° du produit ABIN1686679

Cette protéine Recombinant Hsc70 est exprimée dans Escherichia coli (E. coli) et a été mentionnée dans 6+ publications.

Aperçu rapide pour Hsc70 Protein (His tag) (ABIN1686679)

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

Type de proteíne: Recombinant

Activité biologique: Active

Origine: Humain

Source: Escherichia coli (E. coli)

Application: Western Blotting (WB), SDS-PAGE (SDS), ELISA, Functional Studies (Func), Activity Assay (AcA)

Pureté: >90%

Détail du produit

Purification/Conjugué: Cette Hsc70 protéine est marqué à la His tag.

Specificité: ~70 kDa

Attributs du produit: 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.

Purification: Affinity Purified

Biological Activity Comment: ATPase active

Information d'application

Indications d'application: Optimal working dilution should be determined by the investigator.

Commentaires:

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.

Restrictions: For Research Use only

Stockage

Concentration: Lot specific

Buffer: 50 mM Tris/HCl, pH 8, 0.3M NaCl

Stock: -20 °C

Référence

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." dans: 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." dans: Journal of proteomics, (2015) (PubMed).

Ravindran, Bagchi, Inoue, Tsai: "A Non-enveloped Virus Hijacks Host Disaggregation Machinery to Translocate across the Endoplasmic Reticulum Membrane." dans: 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." dans: 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." dans: 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." dans: Journal of proteome research, Vol. 8, Issue 3, pp. 1540-54, (2009) (PubMed).

Détail du antigène

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

Autre désignation: Hsc70

Sujet: 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).

Poids moléculaire: approx. 70 kDa

ID gène: 3312

UniProt: P11142