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

Details for Product No. ABIN863185, Supplier: Log in to see
Antigen
  • 12
  • 60kDa
  • BP5
  • cb863
  • CG12101
  • chaperonin
  • cpn60
  • CPN60
  • Cpn60
  • crpA
  • d-hsp60
  • Dmel\\CG12101
  • Dmhsp60
  • fa04a05
  • fb22d10
  • fi27b05
  • G62
  • groel
  • GROEL
  • groL
  • HLD4
  • hld4
  • HSP-60
  • HSP60
  • hsp60
  • Hsp60
  • Hsp60A
  • HSP60A
  • hsp60A
  • HSP65
  • hsp65
  • HSPD1
  • Hspd1-30p
  • HuCHA60
  • id:ibd2197
  • IEF16
  • l(1)10Ac
  • l(1)BP5
  • l(1)dp025
  • l(1)G8
  • l(1)HM21
  • l(1)L12
  • MIF4
  • Mmp-P1
  • MNA2
  • mopA
  • sb:cb144
  • SPG13
  • spg13
  • SSP 7506
  • wu:fa04a05
  • wu:fb22d10
  • wu:fi04a12
  • wu:fi27b05
Reactivity
Chicken, Cow (Bovine), Dog (Canine), Human, Mouse (Murine), Rabbit, Rat (Rattus)
623
334
319
203
198
161
160
142
122
122
120
98
95
76
75
70
39
35
24
22
22
22
20
18
4
3
3
3
2
2
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
Host
Rabbit
419
251
7
Clonality
Polyclonal
Conjugate
Un-conjugated
25
18
17
15
14
11
11
11
11
11
11
10
10
9
9
9
9
9
8
8
8
8
8
8
8
8
8
8
8
8
2
2
Application
Immunoprecipitation (IP), Immunohistochemistry (IHC), ELISA, Western Blotting (WB)
595
284
278
262
258
255
229
206
94
10
9
7
2
2
1
1
1
1
Supplier
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Immunogen Human HSP60 produced through recombinant DNA methods in E.coli
Specificity Detects ~60 kDa.
Purification Protein A Purified
Alternative Name HSP60 (HSPD1 Antibody Abstract)
Background 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). HSP60 has however been linked to a number of autoimmune diseases, as well as Alzheimer's, coronary artery diseases, MS, and diabetes (6-9).
Cellular Localization: Mitochondrion | Mitochondrion Matrix
Gene ID 3329
NCBI Accession NP_002147
UniProt P10809
Research Area Heat Shock Proteins
Application Notes Recommended Dilution: WB (1:1000), ICC/IF (1:100), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS, 50 % glycerol, 0.09 % sodium azide
Preservative Sodium azide
Precaution of Use This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Background publications Lai, Liu, Ting, Yang, Huang, Wallace, Kaiser, Wang: "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, Puccetti, Olivieri, Girelli, Navone, Beri, Millo, Margonato, Martinelli, Puccetti: "Interaction of antibodies against cytomegalovirus with heat-shock protein 60 in pathogenesis of atherosclerosis." in: Lancet (London, England), Vol. 362, Issue 9400, pp. 1971-7, 2003 (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, 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 (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, Kiesel, Witkin: "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, 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 (PubMed).