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HSPD1 Antikörper

HSPD1 Reaktivität: Human WB, IHC, FACS, ELISA, IP Wirt: Maus Monoclonal LK1 unconjugated
Produktnummer ABIN361785
  • Target Alle HSPD1 Antikörper anzeigen
    HSPD1 (Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1))
    Reaktivität
    • 214
    • 126
    • 122
    • 74
    • 71
    • 69
    • 64
    • 62
    • 61
    • 60
    • 46
    • 41
    • 36
    • 26
    • 25
    • 21
    • 17
    • 17
    • 14
    • 14
    • 13
    • 11
    • 10
    • 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
    Human
    Wirt
    • 125
    • 117
    • 3
    Maus
    Klonalität
    • 128
    • 115
    Monoklonal
    Konjugat
    • 118
    • 19
    • 10
    • 7
    • 7
    • 7
    • 7
    • 6
    • 6
    • 6
    • 5
    • 5
    • 5
    • 5
    • 5
    • 5
    • 4
    • 3
    • 3
    • 2
    • 2
    • 2
    • 2
    • 2
    • 2
    Dieser HSPD1 Antikörper ist unkonjugiert
    Applikation
    • 194
    • 108
    • 99
    • 95
    • 68
    • 67
    • 27
    • 27
    • 25
    • 24
    • 12
    • 5
    • 5
    • 4
    • 3
    • 3
    • 2
    • 2
    • 2
    • 1
    • 1
    • 1
    • 1
    • 1
    Western Blotting (WB), Immunohistochemistry (IHC), Flow Cytometry (FACS), ELISA, Immunoprecipitation (IP)
    Spezifität
    Detects ~60 kDa.
    Kreuzreaktivität
    Bombyx mori, Huhn, Rind (Kuh), Hund, Drosophila melanogaster, Meerschweinchen, Hamster, Human, Affe, Maus, Schwein, Pflanzen, Kaninchen, Ratte, Schaf, Xenopus laevis
    Aufreinigung
    Protein G Purified
    Immunogen
    Recombinant human HSP60
    Klon
    LK1
    Isotyp
    IgG1
  • Applikationshinweise
    • WB (1:20000)
    • IHC (1:100)
    • ICC/IF (1:100)
    • IP (1:200)
    • optimal dilutions for assays should be determined by the user.
    Kommentare

    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.

    Beschränkungen
    Nur für Forschungszwecke einsetzbar
  • Format
    Liquid
    Konzentration
    1 mg/mL
    Buffer
    PBS, 50 % glycerol, 0.09 % sodium azide, Storage buffer may change when conjugated
    Konservierungsmittel
    Sodium azide
    Vorsichtsmaßnahmen
    This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
    Lagerung
    -20 °C
    Informationen zur Lagerung
    -20°C
  • Hangas, Kekäläinen, Potter, Michell, Aho, Rutanen, Spelbrink, Pohjoismäki, Goffart: "Top3α is the replicative topoisomerase in mitochondrial DNA replication." in: 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." in: 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." in: 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." in: 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." in: 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." in: Proteomics, Vol. 9, Issue 21, pp. 4889-907, (2009) (PubMed).

  • Target
    HSPD1 (Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1))
    Andere Bezeichnung
    HSP60 (HSPD1 Produkte)
    Synonyme
    CPN60 antikoerper, GROEL antikoerper, HLD4 antikoerper, HSP-60 antikoerper, HSP60 antikoerper, HSP65 antikoerper, HuCHA60 antikoerper, SPG13 antikoerper, chaperonin antikoerper, cpn60 antikoerper, groel antikoerper, hld4 antikoerper, hsp60 antikoerper, hsp65 antikoerper, spg13 antikoerper, 60kDa antikoerper, Hsp60 antikoerper, 12 antikoerper, BP5 antikoerper, CG12101 antikoerper, Cpn60 antikoerper, Dmel\\CG12101 antikoerper, Dmhsp60 antikoerper, G62 antikoerper, HSP60A antikoerper, Hsp60A antikoerper, IEF16 antikoerper, Mmp-P1 antikoerper, SSP 7506 antikoerper, d-hsp60 antikoerper, hsp60A antikoerper, l(1)10Ac antikoerper, l(1)BP5 antikoerper, l(1)G8 antikoerper, l(1)HM21 antikoerper, l(1)L12 antikoerper, l(1)dp025 antikoerper, cb863 antikoerper, fa04a05 antikoerper, fb22d10 antikoerper, fi27b05 antikoerper, id:ibd2197 antikoerper, sb:cb144 antikoerper, wu:fa04a05 antikoerper, wu:fb22d10 antikoerper, wu:fi04a12 antikoerper, wu:fi27b05 antikoerper, MIF4 antikoerper, MNA2 antikoerper, mopA antikoerper, groL antikoerper, crpA antikoerper, Hspd1-30p antikoerper, heat shock protein family D (Hsp60) member 1 antikoerper, heat shock protein family D (Hsp60) member 1 S homeolog antikoerper, 60 kDa heat shock protein, mitochondrial antikoerper, heat shock protein 1 (chaperonin) antikoerper, Heat shock protein 60A antikoerper, heat shock 60 protein 1 antikoerper, chaperone ATPase HSP60 antikoerper, molecular chaperone GroEL antikoerper, thermosome subunit antikoerper, chaperonin GroEL antikoerper, mitochondrial chaperonin antikoerper, heat shock protein family D member 1 antikoerper, HSPD1 antikoerper, hspd1.S antikoerper, hspd1 antikoerper, LOC100414401 antikoerper, Hspd1 antikoerper, Hsp60A antikoerper, HSP60 antikoerper, groEL antikoerper, MMP_RS07785 antikoerper, groEl antikoerper, LOC100136430 antikoerper
    Hintergrund
    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).
    Gen-ID
    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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