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

Details for Product No. ABIN263948, 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
Bacteria, Cow (Bovine), Dog (Canine), Chicken, Guinea Pig, Hamster, Human, Monkey, Mouse (Murine), Plant, Pig (Porcine), Rabbit, Rat (Rattus), Whitefly, Yeast
621
334
319
199
194
158
157
139
124
119
117
96
93
74
73
68
38
35
23
22
21
21
20
18
4
3
3
3
2
2
2
2
2
2
2
2
2
1
1
1
1
1
1
1
1
1
Host
Mouse
417
251
7
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
25
18
17
15
14
11
11
11
11
11
11
10
10
9
9
9
9
8
8
8
8
8
8
8
8
8
8
8
8
4
2
2
Application
Flow Cytometry (FACS), Immunohistochemistry (Frozen Sections) (IHC (fro)), Western Blotting (WB)
593
280
275
262
259
251
224
202
89
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
Clone LK2
Isotype IgG1
Specificity Recognizes amino acids 383-447. Recognizes a ~60 kDa protein, corresponding to the Molecular Mass of HSP60 on SDS-PAGE immunoblots.
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 (HSPD1 Antibody Abstract)
Background In both prokaryotic and eukarytic 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).Synonyms: 60 kDa chaperonin, 60 kDa heat shock protein mitochondrial, CPN60, Chaperonin 60, GROEL, GroEL Homolog, HSP-60, HSPD1, Heat shock protein 60, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein
Gene ID 3329
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
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
Supplier Images
Immunohistochemistry (Frozen Sections) (IHC (fro)) image for anti-Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) antibody (ABIN263948) Immunohistochemistry analysis of Listeria infected mice spleens 6 days after infectio...
Immunohistochemistry (IHC) image for anti-Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) antibody (ABIN263948) Hsp60 visualized using AM03145PU (Clone LK2), tested on Human colon cancer cells.
Western Blotting (WB) image for anti-Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) antibody (ABIN263948) Gels were loaded with 1, 2.5, 5.0 and 7.5 µg/lane of HeLa and Raw204.4 cell lysates. ...
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).

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

Product cited in: 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).