Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) (AA 31-547) antibody

Details for Product No. ABIN121328
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Antigen
Epitope
AA 31-547
(21), (18), (17), (13), (11), (9), (5), (4), (3), (3), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Reactivity
Insect, Snake, Trout, Fruit Fly (Drosophila melanogaster), Mammalian
(288), (85), (83), (29), (28), (21), (20), (18), (10), (8), (8), (6), (6), (6), (6), (6), (4), (4), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1)
Host
Mouse
(167), (162), (4)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(12), (6), (5), (4), (4), (4), (4), (4), (4), (4), (4), (4), (4), (4), (4), (4), (3), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Enzyme Immunoassay (EIA), Immunocytochemistry (ICC), Immunofluorescence (IF), Immunoprecipitation (IP), Western Blotting (WB), Flow Cytometry (FACS)
(290), (118), (112), (85), (82), (73), (69), (20), (19), (13), (11), (10), (8), (4), (3), (1), (1)
Pubmed 6 references available
Quantity 0.1 mL
Shipping to United States (Change)
Availability Discontinued
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Catalog No. ABIN121328
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Immunogen Recombinant human Hsp60 protein, amino acids 31-547 (6)
Clone Mab11-13
Isotype IgG2a
Purification Purified
Alternative Name HSP60
Background The human Hsp60 is a member of a highly conserved family which includes molecular chaperones from several species such as plant Hsp60 (known as Rubisco binding protein), GroEL, the E.coli Hsp60 and 65 kDa major antigen of mycobacteria. In eukaryotes, Hsp60 is localized in the mitochondrial matrix and the plant Hsp60 is localized in the chloroplast. Mitochondria, chloroplasts and bacteria have a common ancestry (>1 billion years) and this fact together with the high degree of homology between the divergent Hsp60s would indicate that these proteins carry out a primitive but important function which is similar to all of these 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 (1). 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 (2). Consistent with their functions as chaperones, Hsp60 and Hsp10 have been suggested to act as docking molecules with a passive role in the maturation of caspase processing. Data demonstrates that recombinant Hsp60 and Hsp10 have been shown to accelerate the activation of procaspase-3 by cytochrome C and dATP in an ATP-dependent manner (3). Hsps are intracellular proteins which are thought to serve protective functions against infection and cellular stress, however several recent studies indicate that members of the Hsp60 family are linked to a number of autoimmune diseases, artherosclerosis and chlamydial disease. Although overexpression of self Hsp60 in the synovial tissue of rheumatoid artheritic (RA) patients and cellular as well as humoral reactivities against Hsp60 molecules in RA have been demonstrated, a role for these activities remains to be elucidated (4). The chlamydial heat shock protein, Hsp60, a homolog of E. coli, GroEL, has been identified as capable of eliciting macrophage activation and several studies have revealed a correlation between Hsp60 responses and the immunopathologic manifestations of human chlamydial disease. Another prime candidate is the chlamydial GroES homolog, Hsp10 which is genetically and physiologically linked to Hsp60. Recent data indicates that immune reactivity to Hsp10 is significantly associate with tubal infertility in a chlamydiae-exposed population (5).
UniProt P10809
Research Area Heat Shock Proteins
Application Notes Western blot analysis: 1/10000. Immunoprecipitation: please see references (7,8) for details. Immunofluorescence/Immunocytochemistry: please see references (6,10) for details. Flow (Intracellular): please see references (8,10) for details. Electron microscopy studies (7,9). Neutralization: please see reference (8) for details. Recommended positive control: HeLa heat shock cell lysate. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Format Liquid
Handling Advice Avoid repeated freezing and thawing.
Centrifuge vial before opening.
Storage -20 °C
Storage Comment Store the antibody (in aliquots) at -20 °C. Can be shipped at 2 - 8 °C. Shelf Life: One year from despatch.
Expiry Date 12 months
Supplier Images
anti-Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) (AA 31-547) antibody Western blot analysis of purified human Hsp60 protein (1), HeLa (2) and mouse L929 (3) cell lysates probed with ABIN121328.
General Jindal, Dudani, Singh et al.: "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).

Kaur, Voss, Gupta et al.: "Human peripheral gamma delta T cells recognize hsp60 molecules on Daudi Burkitt's lymphoma cells." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 150, Issue 5, pp. 2046-55, 1993 (PubMed).

Soltys, Gupta: "Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells." in: Experimental cell research, Vol. 222, Issue 1, pp. 16-27, 1996 (PubMed).

Soltys, Gupta: "Cell surface localization of the 60 kDa heat shock chaperonin protein (hsp60) in mammalian cells." in: Cell biology international, Vol. 21, Issue 5, pp. 315-20, 1997 (PubMed).

Samali, Cai, Zhivotovsky et al.: "Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells." in: The EMBO journal, Vol. 18, Issue 8, pp. 2040-8, 1999 (PubMed).

Nielsen, McLennan, Masters et al.: "A single-ring mitochondrial chaperonin (Hsp60-Hsp10) can substitute for GroEL-GroES in vivo." in: Journal of bacteriology, Vol. 181, Issue 18, pp. 5871-5, 1999 (PubMed).

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