anti-Bakterien Heat Shock 60kDa Protein 1 (Chaperonin) Antikörper für Immunofluorescence

Recommended Heat Shock 60kDa Protein 1 (Chaperonin) Antibody (geliefert von: Anmelden zum Anzeigen )

Antigen
Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) Antikörper
  • 12
  • BP5
  • CG12101
  • Cpn60
  • Dmel\\CG12101
  • Dmhsp60
  • G62
  • HSP60
  • HSP60A
  • Hsp60A
  • IEF16
  • Mmp-P1
  • SSP 7506
  • cpn60
  • d-hsp60
  • hsp60
  • hsp60A
  • l(1)10Ac
  • l(1)BP5
  • l(1)G8
  • l(1)HM21
  • l(1)L12
  • l(1)dp025
  • HSPD1
  • hld4
  • groel
  • hsp65
  • spg13
  • chaperonin
  • CPN60
  • MIF4
  • MNA2
  • mopA
  • groL
  • crpA
  • cb863
  • fa04a05
  • fb22d10
  • fi27b05
  • id:ibd2197
  • sb:cb144
  • wu:fa04a05
  • wu:fb22d10
  • wu:fi04a12
  • wu:fi27b05
  • GROEL
  • HLD4
  • HSP-60
  • HSP65
  • HuCHA60
  • SPG13
  • 60kDa
  • Hsp60
  • Hspd1-30p
  • Heat shock protein 60
  • heat shock 60kDa protein 1 (chaperonin)
  • chaperone ATPase HSP60
  • molecular chaperone GroEL
  • chaperonin GroEL
  • mitochondrial chaperonin
  • heat shock protein 60
  • heat shock 60kD protein 1 (chaperonin)
  • heat shock protein 1 (chaperonin)
  • Hsp60
  • HSPD1
  • hspd1
  • HSP60
  • groEL
  • hsp60
  • groEl
  • Hspd1
Reaktivität
Bakterien, Plasmodium falciparum
653
436
418
271
245
227
220
205
176
167
139
117
116
96
94
66
42
41
36
35
22
21
21
21
19
19
18
17
17
4
4
3
3
3
2
2
2
2
2
2
2
2
2
1
1
1
1
1
1
Wirt
Kaninchen
422
279
9
Klonalität
Polyklonal
Konjugat
Unkonjugiert
26
19
18
17
14
12
11
11
11
11
11
10
10
9
9
9
9
9
8
8
8
8
8
8
8
8
8
8
4
4
4
4
3
Applikation
Immunocytochemistry (ICC), Immunofluorescence (IF), Western Blotting (WB)
622
289
288
278
265
262
198
186
84
13
12
10
8
7
5
2
2
1
1
Optionen
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Bilder

Produktnummer ABIN361856
$ 383.90
Zzgl. Versandkosten $45.00
Relevance Score ABIN Application Konjugat Host Isotype Epitope Hersteller Clonality References Details
1 ABIN4320189 FACS ICC IF SimWes WB Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320190 FACS ICC IF SimWes WB Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320191 FACS ICC IF SimWes WB Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320241 ELISA FACS ICC IF IHC (fro) WB Alexa Fluor 488 Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320242 ELISA FACS ICC IF IHC (fro) WB Alexa Fluor 647 Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320254 ELISA FACS ICC IF IHC (fro) WB DyLight 350 Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320253 ELISA FACS ICC IF IHC (fro) WB DyLight 550 Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320255 ELISA FACS ICC IF IHC (fro) WB DyLight 405 Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320240 ELISA FACS ICC IF IHC (fro) WB Alexa Fluor 405 Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320247 ELISA FACS ICC IF IHC (fro) WB DyLight 680 Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320250 ELISA FACS ICC IF IHC (fro) WB DyLight 755 Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320243 ELISA FACS ICC IF IHC (fro) WB Alexa Fluor 700 Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320246 ELISA FACS ICC IF IHC (fro) WB DyLight 650 Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320248 ELISA FACS ICC IF IHC (fro) WB DyLight 488 Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320251 ELISA FACS ICC IF IHC (fro) IP WB PerCP Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320245 ELISA ICC IF IHC (fro) WB Biotin Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320202 CyTOF ELISA FACS ICC IF IHC (fro) IP WB Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN4320203 CyTOF ELISA FACS ICC IF IHC (fro) IP WB Mouse IgG1 kappa AA 383-419 Anmelden zum Anzeigen LK2
1 ABIN2741558 ELISA FACS IF IHC (fro) IP WB Mouse IgG1, kappa Anmelden zum Anzeigen LK2
1 ABIN2484789 ICC IF WB Atto 488 Rabbit Anmelden zum Anzeigen Polyclonal

General

Antigen Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) Antikörper
Reaktivität Bakterien, Plasmodium falciparum
(653), (436), (418), (271), (245), (227), (220), (205), (176), (167), (139), (117), (116), (96), (94), (66), (42), (41), (36), (35), (22), (21), (21), (21), (19), (19), (18), (17), (17), (4), (4), (3), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1)
Wirt Kaninchen
(422), (279), (9)
Klonalität
Polyklonal
Konjugat Unkonjugiert
(26), (19), (18), (17), (14), (12), (11), (11), (11), (11), (11), (10), (10), (9), (9), (9), (9), (9), (8), (8), (8), (8), (8), (8), (8), (8), (8), (8), (4), (4), (4), (4), (3)
Applikation Immunocytochemistry (ICC), Immunofluorescence (IF), Western Blotting (WB)
(622), (289), (288), (278), (265), (262), (198), (186), (84), (13), (12), (10), (8), (7), (5), (2), (2), (1), (1)
Pubmed 10 Publikationen vorhanden
Hersteller Anmelden zum Anzeigen

Produktdetails

Antigendetails Anwendungsinformationen Handhabung Referenzen Bilder
Spezifität Detects ~ 60 kDa. Cross-reacts with E.coli HSP60, GroEl.
Reinigung Protein A Purified
Immunogen Recombinant full length PfHSP60

Antigendetails

Produktdetails Anwendungsinformationen Handhabung Referenzen Bilder zurück nach oben
Antigen
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).
NCBI Accession XM_001347402
UniProt P34940
Forschungsgebiet Heat Shock Proteins
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

Anwendungsinformationen

Produktdetails Antigendetails Handhabung Referenzen Bilder zurück nach oben
Applikationshinweise
  • WB (1:2000)
  • optimal dilutions for assays should be determined by the user.
Kommentare

0.9 μg/ml of SPC-185 was sufficient for detection of PfHSP60 in 20 μg of P. falciparum lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

Beschränkungen Nur für Forschungszwecke einsetzbar

Handhabung

Produktdetails Antigendetails Anwendungsinformationen Referenzen Bilder zurück nach oben
Format Liquid
Konzentration 1.83 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
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

Referenzen

Produktdetails Antigendetails Anwendungsinformationen Handhabung Bilder zurück nach oben
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

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

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

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

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

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

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

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

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

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

Bilder

Produktdetails Antigendetails Anwendungsinformationen Handhabung Referenzen zurück nach oben
Bilder des Herstellers
 image for anti-Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) antibody (ABIN361856) PfHsp60, malarial parasite lysate.