Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) Antikörper

Details zu Produkt Nr. ABIN361784, Anbieter: Anmelden zum Anzeigen
Antigen
  • CPN60
  • GROEL
  • HLD4
  • HSP-60
  • HSP60
  • HSP65
  • HuCHA60
  • SPG13
  • chaperonin
  • cpn60
  • groel
  • hld4
  • hsp60
  • hsp65
  • spg13
  • 60kDa
  • Hsp60
  • 12
  • BP5
  • CG12101
  • Cpn60
  • Dmel\\CG12101
  • Dmhsp60
  • G62
  • HSP60A
  • Hsp60A
  • IEF16
  • Mmp-P1
  • SSP 7506
  • d-hsp60
  • hsp60A
  • l(1)10Ac
  • l(1)BP5
  • l(1)G8
  • l(1)HM21
  • l(1)L12
  • l(1)dp025
  • cb863
  • fa04a05
  • fb22d10
  • fi27b05
  • id:ibd2197
  • sb:cb144
  • wu:fa04a05
  • wu:fb22d10
  • wu:fi04a12
  • wu:fi27b05
  • MIF4
  • MNA2
  • mopA
  • groL
  • crpA
  • Hspd1-30p
  • heat shock protein family D (Hsp60) member 1
  • heat shock protein family D (Hsp60) member 1 S homeolog
  • 60 kDa heat shock protein, mitochondrial
  • heat shock protein 1 (chaperonin)
  • Heat shock protein 60A
  • heat shock 60 protein 1
  • chaperone ATPase HSP60
  • molecular chaperone GroEL
  • thermosome subunit
  • chaperonin GroEL
  • mitochondrial chaperonin
  • heat shock protein family D member 1
  • HSPD1
  • hspd1.S
  • hspd1
  • LOC100414401
  • Hspd1
  • Hsp60A
  • HSP60
  • groEL
  • MMP_RS07785
  • groEl
  • LOC100136430
Reaktivität
Huhn, Rind (Kuh), Hund, Fruchtfliege (Drosophila melanogaster), Meerschweinchen, Hamster, Human, Affe, Maus, Schwein, Pflanzen, Kaninchen, Ratte (Rattus), Schaf, Xenopus laevis
846
580
561
390
345
326
317
304
282
270
194
180
133
120
115
105
77
60
40
39
37
37
36
36
23
21
20
20
18
18
18
17
17
6
4
4
3
3
3
3
3
3
3
2
2
2
1
1
1
1
1
1
1
Wirt
Maus
571
349
10
Klonalität (Klon)
Monoklonal ()
Konjugat
Unkonjugiert
35
28
27
27
23
22
17
12
12
12
12
12
12
12
12
12
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8
8
8
5
5
5
5
5
5
5
5
5
5
5
5
5
4
4
4
3
Applikation
Flow Cytometry (FACS), Immunoprecipitation (IP), Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
777
439
410
383
320
278
231
187
85
63
42
41
8
7
6
6
2
2
1
1
Optionen
Hersteller
Anmelden zum Anzeigen
Hersteller Produkt- Nr.
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Immunogen Recombinant human HSP60
Klon LK1
Isotyp IgG1
Spezifität Detects ~60 kDa.
Reinigung Protein G Purified
Antigen Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1)
Andere Bezeichnung HSP60 (HSPD1 Antibody Abstract)
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
Applikations-hinweise
  • 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 SMC-110 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
Konservierungs-mittel Sodium azide
Vorsichtsmaßnahmen This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung -20 °C
Bilder des Herstellers
 image for anti-Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) antibody (ABIN361784) Hsp60 (LK 1), cell line mix.
Produkt verwendet in: 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).

Allgemeine Veröffentlichungen Verda, Kim, Ikehara, Statkute, Bronesky, Petrenko, Oyama, He, Link, Vahanian, Burt: "Hematopoietic mixed chimerism derived from allogeneic embryonic stem cells prevents autoimmune diabetes mellitus in NOD mice." in: Stem cells (Dayton, Ohio), Vol. 26, Issue 2, pp. 381-6, 2008 (PubMed).

Lai, Zhuang, Zhang: "[Stability of implants placed in different bone types]" in: Zhonghua kou qiang yi xue za zhi = Zhonghua kouqiang yixue zazhi = Chinese journal of stomatology, Vol. 42, Issue 5, pp. 292-3, 2007 (PubMed).

Lai, Liu, Ting, Yang, Huang, Wallace, Kaiser, Wang: "Regulation of IGF-I receptor signaling in diabetic cardiac muscle: dysregulation of cytosolic and mitochondria HSP60." in: American journal of physiology. Endocrinology and metabolism, Vol. 292, Issue 1, pp. E292-7, 2007 (PubMed).

Deocaris, Kaul, Wadhwa: "On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60." in: Cell stress & chaperones, Vol. 11, Issue 2, pp. 116-28, 2006 (PubMed).

Gupta, Knowlton: "HSP60, Bax, apoptosis and the heart." in: Journal of cellular and molecular medicine, Vol. 9, Issue 1, pp. 51-8, 2005 (PubMed).

Bason, Corrocher, Lunardi, Puccetti, Olivieri, Girelli, Navone, Beri, Millo, Margonato, Martinelli, Puccetti: "Interaction of antibodies against cytomegalovirus with heat-shock protein 60 in pathogenesis of atherosclerosis." in: Lancet (London, England), Vol. 362, Issue 9400, pp. 1971-7, 2003 (PubMed).

Hartl, Hayer-Hartl: "Molecular chaperones in the cytosol: from nascent chain to folded protein." in: Science (New York, N.Y.), Vol. 295, Issue 5561, pp. 1852-8, 2002 (PubMed).

Itoh, Komatsuda, Ohtani, Wakui, Imai, Sawada, Otaka, Ogura, Suzuki, Hamada: "Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration." in: European journal of biochemistry / FEBS, Vol. 269, Issue 23, pp. 5931-8, 2002 (PubMed).

LaVerda, Kalayoglu, Byrne: "Chlamydial heat shock proteins and disease pathology: new paradigms for old problems?" in: Infectious diseases in obstetrics and gynecology, Vol. 7, Issue 1-2, pp. 64-71, 1999 (PubMed).

Bukau, Horwich: "The Hsp70 and Hsp60 chaperone machines." in: Cell, Vol. 92, Issue 3, pp. 351-66, 1998 (PubMed).

Neuer, Lam, Tiller, Kiesel, Witkin: "Humoral immune response to membrane components of Chlamydia trachomatis and expression of human 60 kDa heat shock protein in follicular fluid of in-vitro fertilization patients." in: Human reproduction (Oxford, England), Vol. 12, Issue 5, pp. 925-9, 1997 (PubMed).

Hartl: "Molecular chaperones in cellular protein folding." in: Nature, Vol. 381, Issue 6583, pp. 571-9, 1996 (PubMed).

Gao, Brosnan, Raine: "Experimental autoimmune encephalomyelitis. Qualitative and semiquantitative differences in heat shock protein 60 expression in the central nervous system." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 154, Issue 7, pp. 3548-56, 1995 (PubMed).

Jindal, Dudani, Singh, Harley, Gupta: "Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen." in: Molecular and cellular biology, Vol. 9, Issue 5, pp. 2279-83, 1989 (PubMed).

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