HSP70 Protein (His tag)

N° du produit ABIN1686670

Cette protéine Recombinant HSP70 est exprimée dans Escherichia coli (E. coli) et a été mentionnée dans 6+ publications.

Aperçu rapide pour HSP70 Protein (His tag) (ABIN1686670)

Antigène: HSP70 (Heat Shock Protein 70 (HSP70))

Type de proteíne: Recombinant

Activité biologique: Active

Origine: Humain

Source: Escherichia coli (E. coli)

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

Pureté: >90%

Détail du produit

Purification/Conjugué: Cette HSP70 protéine est marqué à la His tag.

Séquence: MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV D

Specificité: ~70 kDa

Attributs du produit: The protein has ATPase activity at the time of manufacture of 3.3 µM phosphate liberated/hr/μg protein in a 200 µL reaction at 37 °C (pH 7.5) 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 3.3μM phosphate liberated/hr/μg protein in a 200μl reaction at 37°C (pH7.5) in the presence of 20ul of 1mM ATP using a Malachite Green assay.

Restrictions: For Research Use only

Stockage

Concentration: Lot specific

Buffer: Na-Phosphate, pH 7.5 (20 mM), 150 mM NaCl, 10 % glycerol, 200 mM Imidazole

Stock: -20 °C

Référence

Chanoux, Robay, Shubin, Kebler, Suaud, Rubenstein: "Hsp70 promotes epithelial sodium channel functional expression by increasing its association with coat complex II and its exit from endoplasmic reticulum." dans: The Journal of biological chemistry, Vol. 287, Issue 23, pp. 19255-65, (2012) (PubMed).

Sorci, Giovannini, Riuzzi, Bonifazi, Zelante, Zagarella, Bistoni, Donato, Romani: "The danger signal S100B integrates pathogen- and danger-sensing pathways to restrain inflammation." dans: PLoS pathogens, Vol. 7, Issue 3, pp. e1001315, (2011) (PubMed).

Ireland, Williams: "Measuring Hsp72 (HSPA1A) by indirect sandwich ELISA." dans: Methods in molecular biology (Clifton, N.J.), Vol. 787, pp. 145-53, (2011) (PubMed).

Fernandez-Funez, Casas-Tinto, Zhang, Gómez-Velazquez, Morales-Garza, Cepeda-Nieto, Castilla, Soto, Rincon-Limas: "In vivo generation of neurotoxic prion protein: role for hsp70 in accumulation of misfolded isoforms." dans: PLoS genetics, Vol. 5, Issue 6, pp. e1000507, (2009) (PubMed).

Ishibashi, Kato, Asahi, Sugita, Nishikawa: "Identification of the major allergen of Malassezia globosa relevant for atopic dermatitis." dans: Journal of dermatological science, Vol. 55, Issue 3, pp. 185-92, (2009) (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: HSP70 (Heat Shock Protein 70 (HSP70))

Autre désignation: Hsp70

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). 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. Looking for more information on HSP70? Visit our new HSP70 Scientific Resource Guide at http://www.HSP70.com.

Poids moléculaire: approx. 70 kDa

ID gène: 3303

NCBI Accession: NM_005345