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HSP70 Protein (His tag)

HSP70 Origin: Human Host: Escherichia coli (E. coli) Recombinant >90% SDS, WB, Func, AcA, ELISA Active
Catalog No. ABIN1686670
  • Target See all HSP70 Proteins
    HSP70 (Heat Shock Protein 70 (HSP70))
    Protein Type
    Recombinant
    Biological Activity
    Active
    Origin
    • 8
    • 2
    • 1
    • 1
    • 1
    • 1
    Human
    Source
    • 5
    • 3
    • 1
    • 1
    • 1
    Escherichia coli (E. coli)
    Purification tag / Conjugate
    This HSP70 protein is labelled with His tag.
    Application
    SDS-PAGE (SDS), Western Blotting (WB), Functional Studies (Func), Activity Assay (AcA), ELISA
    Sequence
    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
    Specificity
    ~70 kDa
    Characteristics
    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
    Purity
    >90%
    Biological Activity Comment
    ATPase active
  • Application Notes
    Optimal working dilution should be determined by the investigator.
    Comment

    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
  • Concentration
    Lot specific
    Buffer
    Na-Phosphate, pH 7.5 (20 mM), 150 mM NaCl, 10 % glycerol, 200 mM Imidazole
    Storage
    -20 °C
  • 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." in: 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." in: PLoS pathogens, Vol. 7, Issue 3, pp. e1001315, (2011) (PubMed).

    Ireland, Williams: "Measuring Hsp72 (HSPA1A) by indirect sandwich ELISA." in: 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." in: 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." in: 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." in: Journal of proteome research, Vol. 8, Issue 3, pp. 1540-54, (2009) (PubMed).

  • Target
    HSP70 (Heat Shock Protein 70 (HSP70))
    Alternative Name
    Hsp70 (HSP70 Products)
    Synonyms
    APG-2 Protein, HS24/P52 Protein, HSPH2 Protein, RY Protein, hsp70 Protein, hsp70RY Protein, CG31354 Protein, HSP70 Protein, Hsp70Bb Protein, hsp70B Protein, hsp70Bb-prime Protein, DmelCG5834 Protein, CG5834 Protein, HSPA1 Protein, HSP70B' Protein, HSPA6 Protein, ARABIDOPSIS HEAT SHOCK PROTEIN 70 Protein, ATHSP70 Protein, heat shock protein 70 Protein, LOC100305036 Protein, hsc70 Protein, Hsp70 Protein, Hsp70-1 Protein, Hsp70.1 Protein, hsp68 Protein, Hsp110 Protein, irp94 Protein, HSP70-2 Protein, HSPA1B Protein, HSPA2 Protein, hsp70-5 Protein, HSP70-1 Protein, HSP70.1 Protein, HSP70.2 Protein, heat shock protein family A (Hsp70) member 4 Protein, CG5834 gene product from transcript CG5834-RA Protein, heat shock protein 70 Protein, heat shock protein family A (Hsp70) member 6 Protein, heat shock 70kDa protein 2 Protein, heat shock 70 kD protein cognate Protein, Hsp70 family chaperone Protein, Heat shock protein 70 Protein, Heat shock protein 70, putative Protein, heat shock protein 1B Protein, heat shock protein family A member 4 Protein, heat shock 70kDa protein 1A Protein, heat shock protein 1 Protein, Heat Shock Protein Protein, heat shock cognate 70-kd protein Protein, Heat shock 70 kDa protein 1A Protein, HSPA4 Protein, Hsp70Bbb Protein, HSP70 Protein, HSPA6 Protein, HSPA2 Protein, PCC7424_2419 Protein, Isop_1041 Protein, CGB_C3390W Protein, Bacsa_1698 Protein, dnaK-B Protein, LOC100305036 Protein, Hspa1b Protein, Hspa4 Protein, HSPA1A Protein, hsp1 Protein, hsp-70 Protein, hsp70 Protein, LOC108348108 Protein
    Background
    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.
    Molecular Weight
    approx. 70 kDa
    Gene ID
    3303
    NCBI Accession
    NM_005345
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