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Details for Product No. ABIN263949

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

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CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13, hld4, cpn60, groel, hsp60, hsp65, spg13, chaperonin, cb863, fa04a05, fb22d10, fi27b05, sb:cb144, id:ibd2197, wu:fa04a05, wu:fb22d10, wu:fi04a1 ... show more
»Alternatives Bacillus, Cow (Bovine), Dog (Canine), Chicken, Guinea Pig, Hamster, Human, Monkey, Mouse (Murine), Plant, Pig (Porcine), Rabbit, Rat (Rattus), Yeast
»Alternatives Mouse
Clonality (Clone) Monoclonal ()
»Alternatives Un-conjugated
»Alternatives Immunohistochemistry (Frozen Sections) (IHC (fro)), Western Blotting (WB), Flow Cytometry (FACS)
Pubmed 11 references available
Catalog no. ABIN263949
Quantity 50 µg
242.00 $   Plus shipping costs $45.00
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Availability Will be delivered in 6 to 8 Business Days
Immunogen Human Hsp60 produced through recombinant DNA methods in E. coli
Clone LK2
Isotype IgG1
Characteristics Synonyms: HSP-60, HSPD1, Heat shock protein 60, Chaperonin 60, HuCHA60, GROEL, GroEL Homolog,CPN60, 60 kDa heat shock protein mitochondrial, 60 kDa chaperonin, Mitochondrialmatrix protein P1, P60 lymphocyte protein
Purification Purified
Alternative Name HSP60
Background In both prokaryotic and eukarytic cells, the misfolding and aggregation of proteins duringbiogenesis 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 characterizedchaperones. Hsp60, also known as Cpn60 or GroEl, is an abundant protein synthesizedconstitutively in the cell that is induced to a higher concentration after brief cell shock. It ispresent in many species and exhibits a remarkable sequence homology among variouscounterparts in bacteria, plants, and mammals with more than half of the residuesidentical between bacterial and mammalian Hsp60 (1-3). Whereas mammalian Hsp60 islocalized within the mitochondria, plant Hsp60, or otherwise known as Rubisco-bindingprotein, is located in plant chloroplasts. It has been indicated that these proteins carry outa very important biological function due to the fact that Hsp60 is present in so manydifferent species. The common characteristics of the Hsp60s from the divergent speciesare 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 thepresence of Mg2+ and ATP, iv) ATPase activity and v) a role in folding and assembly ofoligomeric protein structures (4). These similarities are supported by recent studies wherethe single-ring human mitochondrial homolog, Hsp60 with its co-chaperonin, Hsp10 wereexpressed in a E. coli strain, engineered so that the groE operon is under strict regulatorycontrol. This study has demonstrated that expression of Hsp60-Hsp10 was able to carry outall essential in vivo functions of GroEL and its co-chaperonin, GroES (5). Another importantfunction of Hsp60 and Hsp10 is their protective functions against infection and cellularstress. Hsp60 has however been linked to a number of autoimmune diseases, as well asAlzheimer's, coronary artery diseases, MS, and diabetes (6-9).
UniProt P10809
Research Area Heat Shock Proteins
Application Notes Western blot (10): 0.25 µg/ml. Immunohistochemistry on Frozen Sections. This Clone is reported to work on Paraffin Sections. Flow Cytometry (12). Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1.0 mg/mL
Buffer PBS containing 0.1 mM PMSF and 50% Glycerol.
Storage 4 °C/-20 °C
Storage Comment Store the antibody undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer. Avoid repeated freezing and thawing. Shelf life: one year from despatch.
Expiry Date 12 months
Background publications 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).

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).

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

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

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 et al.: "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).

Bason, Corrocher, Lunardi et al.: "Interaction of antibodies against cytomegalovirus with heat-shock protein 60 in pathogenesis of atherosclerosis." in: Lancet, Vol. 362, Issue 9400, pp. 1971-7, 2003 (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).

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).

Lai, Liu, Ting et al.: "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).

Alternatives for antigen "Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1)", type "Antibodies"
Hosts (132), (119), (4)
Reactivities (226), (83), (81), (35), (34), (25), (21), (13), (8), (8), (7), (6), (6), (6), (6), (5), (4), (4), (4), (3), (3), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Applications (222), (82), (79), (54), (52), (50), (35), (20), (19), (10), (8), (5), (4), (3), (3), (1), (1)
Conjugates (8), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Epitopes (11), (7), (7), (6), (5), (4), (4), (4), (4), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1)