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

Details for Product No. ABIN361784
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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, hld ... show more
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 show less
Human, Rat (Rattus), Cow (Bovine), Dog (Canine), Chicken, Fruit Fly (Drosophila melanogaster), Guinea Pig, Hamster, Monkey, Pig (Porcine), Rabbit, Sheep (Ovine), Xenopus laevis
(353), (81), (80), (24), (23), (20), (19), (19), (12), (12), (10), (10), (8), (7), (6), (6), (6), (4), (3), (3), (3), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1)
(207), (184), (8)
Clonality (Clone)
Monoclonal ()
(11), (7), (5), (5), (5), (4), (4), (4), (4), (4), (4), (4), (4), (4), (4), (4), (2), (2), (1)
Western Blotting (WB), Immunoprecipitation (IP), ELISA, Flow Cytometry (FACS), Immunohistochemistry (IHC)
(360), (167), (140), (115), (96), (91), (81), (20), (20), (13), (12), (12), (8), (4), (3), (3), (1), (1), (1), (1), (1)
Pubmed 15 references available
Quantity 50 μg
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Catalog No. ABIN361784
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Immunogen Recombinant human Hsp60
Clone LK1
Isotype IgG1
Specificity Detects an approx. 60 kDa protein corresponding to the molecular mass of Hsp60 on SDS PAGE immunoblots.
Sensitivity 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.
Purification Protein G Purified
Alternative Name Hsp60
Background Synonyms:
CPN60, GROEL, HLD4, Hsp 60, Hsp65, HSPD1, HuCHA60, SPG 13
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. 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. 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. 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.
Gene ID 3329
NCBI Accession NP_002147
UniProt P10809
Research Area Signaling, Heat Shock Proteins
Application Notes Recommended Dilution: 0.05 µg/mL (WB)
Restrictions For Research Use only
Concentration 1 mg/mL
Buffer PBS, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use WARNING: Reagents contain sodium azide. Sodium azide is very toxic if ingested or inhaled. Avoid contact with skin, eyes, or clothing. Wear eye or face protection when handling. If skin or eye contact occurs, wash with copious amounts of water. If ingested or inhaled, contact a physician immediately. Sodium azide yields toxic hydrazoic acid under acidic conditions. Dilute azide-containing compounds in running water before discarding to avoid accumulation of potentially explosive deposits in lead or copper plumbing.
Storage -20 °C
Supplier Images
anti-Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) antibody Hsp60 (LK 1), cell line mix.
Background publications 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).

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 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).

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).

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).

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 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).

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 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).

General 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).

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).

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).

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