Heat Shock Protein 60 (HSP60) antibody

Antigen: Heat Shock Protein 60 (HSP60)

Synonyms: HLD4, CPN60, GROEL, HSP60, HSP65, SPG13, HuCHA60, 60kDa, Hsp60, 12, BP5, Cpn60, Dmhsp60, G62, Hsp60A, Mmp-P1, l(1)10Ac, l(1)BP5, l(1)G8, l(1)HM21, l(1)L12, l(1)dp025, DmelCG12101, CG12101, HEAT SHOCK PROTEIN 60, HEAT SHOCK PROTEIN 60-3B, HSP60-3B, 23.m06276

Clonality: Monoclonal (LK1)

Host: Mouse

Reactivity: Human, Mouse (Murine), Rat (Rattus), Cow (Bovine), Dog (Canine), Chicken, Fruit Fly (Drosophila melanogaster), Guinea Pig, Hamster, Monkey, Pig (Porcine), Rabbit, Sheep (Ovine), Xenopus laevis

Application: Western Blotting (WB), Immunoprecipitation (IP), ELISA, Flow Cytometry (FACS), Immunohistochemistry (IHC)

Catalog no.: ABIN361784

Additional Information

Alternative name: Hsp60

Immunogen: Recombinant human hsp60

Format: Protein G purified

Isotype: IgG1  (Matching secondary antibodies)

Clone: LK1

Description: 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).

Specificity: Recognizes a ~60kDa protein, corresponding to the molecular mass of hsp60 on SDS-PAGE immunoblots. Species cross-reactivity: Human, Mouse, Rat, Bovine, Canine, Chicken, Drosophilia, Guinea pig, Hamster, Monkey, Pig, Rabbit, Sheep, Xenopus.

Synonyms: HLD4, CPN60, GROEL, HSP60, HSP65, SPG13, HuCHA60, 60kDa, Hsp60, 12, BP5, Cpn60, Dmhsp60, G62, Hsp60A, Mmp-P1, l(1)10Ac, l(1)BP5, l(1)G8, l(1)HM21, l(1)L12, l(1)dp025, DmelCG12101, CG12101, HEAT SHOCK PROTEIN 60, HEAT SHOCK PROTEIN 60-3B, HSP60-3B, 23.m06276

Application Details

Application Notes: 0.05 ug/mL for western blot analysis

Concentration: 1.0mg/mL

Buffer: Mouse immunoglobulin in PBS, 0.09% azide and 50% glycerol

Storage: -20°C, 1 year+, shipped on cold packs or ambient

Research Area: Signaling, Heat Shock Proteins

Restrictions: For Research Use only

Images

Hsp60 (LK-1) 1 IN 100 000 Human Colon Cancer, Amplifer

Hsp60 (LK1), Rat tissue lysates

Hsp60 (LK1) Human skin fibroblast cells, control+24h later

Publications

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).

Neuer, Lam, Tiller et al.: "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).

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

Verda, Kim, Ikehara et al.: "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).

Ahsan, Donnart, Nouri et al.: "Tissue-Specific Defense and Thermo-Adaptive Mechanisms of Soybean Seedlings under Heat Stress Revealed by Proteomic Approach." in: Journal of proteome research, 2010 (PubMed).