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HSPD1 anticorps

HSPD1 Reactivité: Humain WB, IHC, FACS, ELISA, IP Hôte: Souris Monoclonal LK1 unconjugated
N° du produit ABIN361785
  • Antigène Voir toutes HSPD1 Anticorps
    HSPD1 (Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1))
    Reactivité
    • 208
    • 123
    • 118
    • 74
    • 70
    • 69
    • 64
    • 63
    • 61
    • 61
    • 46
    • 41
    • 36
    • 26
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    • 17
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    • 14
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    • 13
    • 10
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    • 10
    • 10
    • 10
    • 4
    • 4
    • 4
    • 4
    • 4
    • 4
    • 3
    • 3
    • 3
    • 2
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    Humain
    Hôte
    • 120
    • 114
    • 3
    Souris
    Clonalité
    • 123
    • 112
    Monoclonal
    Conjugué
    • 113
    • 19
    • 10
    • 7
    • 7
    • 7
    • 7
    • 6
    • 6
    • 6
    • 5
    • 5
    • 5
    • 5
    • 5
    • 5
    • 4
    • 3
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    Cet anticorp HSPD1 est non-conjugé
    Application
    • 186
    • 102
    • 97
    • 90
    • 64
    • 62
    • 27
    • 27
    • 24
    • 24
    • 12
    • 5
    • 4
    • 4
    • 3
    • 3
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    • 1
    Western Blotting (WB), Immunohistochemistry (IHC), Flow Cytometry (FACS), ELISA, Immunoprecipitation (IP)
    Specificité
    Detects ~60 kDa.
     Réactivité croisée
    Bombyx mori, Poulet, Boeuf (Vache), Chien, Drosophila melanogaster, Cobaye, Hamster, Humain, Singe, Souris, Porc, Plantes, Lapin, Rat, Mouton, Xenopus laevis
    Purification
    Protein G Purified
    Immunogène
    Recombinant human HSP60
    Clone
    LK1
    Isotype
    IgG1
    Top Product
    Discover our top product HSPD1 Anticorps primaire
  • Indications d'application
    • WB (1:20000)
    • IHC (1:100)
    • ICC/IF (1:100)
    • IP (1:200)
    • optimal dilutions for assays should be determined by the user.
    Commentaires

    0.05 μg/ml of ABIN361784 was sufficient for detection of HSP60 in 20 μg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using goat anti-mouse IgG as the secondary antibody.

    Restrictions
    For Research Use only
  • Format
    Liquid
    Concentration
    1 mg/mL
    Buffer
    PBS, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated
    Agent conservateur
    Sodium azide
    Précaution d'utilisation
    This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
    Stock
    -20 °C
    Stockage commentaire
    -20°C
  • Hangas, Kekäläinen, Potter, Michell, Aho, Rutanen, Spelbrink, Pohjoismäki, Goffart: "Top3α is the replicative topoisomerase in mitochondrial DNA replication." dans: Nucleic acids research, Vol. 50, Issue 15, pp. 8733-8748, (2022) (PubMed).

    Schuster, Anton, Simões, Altin, den Brave, Hermanns, Hospenthal, Komander, Dittmar, Dohmen, Escobar-Henriques: "Dual role of a GTPase conformational switch for membrane fusion by mitofusin ubiquitylation." dans: Life science alliance, Vol. 3, Issue 1, (2020) (PubMed).

    Hangas, Aasumets, Kekäläinen, Paloheinä, Pohjoismäki, Gerhold, Goffart: "Ciprofloxacin impairs mitochondrial DNA replication initiation through inhibition of Topoisomerase 2." dans: Nucleic acids research, Vol. 46, Issue 18, pp. 9625-9636, (2019) (PubMed).

    Dogan, Pujol, Maiti, Kukat, Wang, Hermans, Senft, Wibom, Rugarli, Trifunovic: "Tissue-specific loss of DARS2 activates stress responses independently of respiratory chain deficiency in the heart." dans: Cell metabolism, Vol. 19, Issue 3, pp. 458-69, (2014) (PubMed).

    Ahsan, Donnart, Nouri, Komatsu: "Tissue-specific defense and thermo-adaptive mechanisms of soybean seedlings under heat stress revealed by proteomic approach." dans: Journal of proteome research, Vol. 9, Issue 8, pp. 4189-204, (2010) (PubMed).

    Ahsan, Komatsu: "Comparative analyses of the proteomes of leaves and flowers at various stages of development reveal organ-specific functional differentiation of proteins in soybean." dans: Proteomics, Vol. 9, Issue 21, pp. 4889-907, (2009) (PubMed).

  • Antigène
    HSPD1 (Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1))
    Autre désignation
    HSP60 (HSPD1 Produits)
    Synonymes
    anticorps CPN60, anticorps GROEL, anticorps HLD4, anticorps HSP-60, anticorps HSP60, anticorps HSP65, anticorps HuCHA60, anticorps SPG13, anticorps chaperonin, anticorps cpn60, anticorps groel, anticorps hld4, anticorps hsp60, anticorps hsp65, anticorps spg13, anticorps 60kDa, anticorps Hsp60, anticorps 12, anticorps BP5, anticorps CG12101, anticorps Cpn60, anticorps Dmel\\CG12101, anticorps Dmhsp60, anticorps G62, anticorps HSP60A, anticorps Hsp60A, anticorps IEF16, anticorps Mmp-P1, anticorps SSP 7506, anticorps d-hsp60, anticorps hsp60A, anticorps l(1)10Ac, anticorps l(1)BP5, anticorps l(1)G8, anticorps l(1)HM21, anticorps l(1)L12, anticorps l(1)dp025, anticorps cb863, anticorps fa04a05, anticorps fb22d10, anticorps fi27b05, anticorps id:ibd2197, anticorps sb:cb144, anticorps wu:fa04a05, anticorps wu:fb22d10, anticorps wu:fi04a12, anticorps wu:fi27b05, anticorps MIF4, anticorps MNA2, anticorps mopA, anticorps groL, anticorps crpA, anticorps Hspd1-30p, anticorps heat shock protein family D (Hsp60) member 1, anticorps heat shock protein family D (Hsp60) member 1 S homeolog, anticorps 60 kDa heat shock protein, mitochondrial, anticorps heat shock protein 1 (chaperonin), anticorps Heat shock protein 60A, anticorps heat shock 60 protein 1, anticorps chaperone ATPase HSP60, anticorps molecular chaperone GroEL, anticorps thermosome subunit, anticorps chaperonin GroEL, anticorps mitochondrial chaperonin, anticorps heat shock protein family D member 1, anticorps HSPD1, anticorps hspd1.S, anticorps hspd1, anticorps LOC100414401, anticorps Hspd1, anticorps Hsp60A, anticorps HSP60, anticorps groEL, anticorps MMP_RS07785, anticorps groEl, anticorps LOC100136430
    Sujet
    In both prokaryotic and eukaryotic cells, the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones. Members of the HSP60 family of heat shock proteins are some of the best characterized chaperones. HSP60, also known as Cpn60 or GroEl, is an abundant protein synthesized constitutively in the cell that is induced to a higher concentration after brief cell shock. It is present in many species and exhibits a remarkable sequence homology among various counterparts in bacteria, plants, and mammals with more than half of the residues identical between bacterial and mammalian HSP60 (1-3). Whereas mammalian HSP60 is localized within the mitochondria, plant HSP60, or otherwise known as Rubisco-binding protein, is located in plant chloroplasts. It has been indicated that these proteins carry out a very important biological function due to the fact that HSP60 is present in so many different species. The common characteristics of the HSP60s from the divergent species are i) high abundance, ii) induction with environmental stress such as heat shock, iii) homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP, iv) ATPase activity and v) a role in folding and assembly of oligomeric protein structures (4). These similarities are supported by recent studies where the single-ring human mitochondrial homolog, HSP60 with its co-chaperonin, HSP10 were expressed in a E. coli strain, engineered so that the groE operon is under strict regulatory control. This study has demonstrated that expression of HSP60-HSP10 was able to carry out all essential in vivo functions of GroEL and its co-chaperonin, GroES (5). Another important function of HSP60 and HSP10 is their protective functions against infection and cellular stress. HSP60 has however been linked to a number of autoimmune diseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9).
    ID gène
    3329
    NCBI Accession
    NP_002147
    UniProt
    P10809
    Pathways
    Activation of Innate immune Response, Regulation of Leukocyte Mediated Immunity, Positive Regulation of Immune Effector Process, Production of Molecular Mediator of Immune Response, Positive Regulation of Endopeptidase Activity
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