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

Details for Product No. ABIN361856, Supplier: Log in to see
  • 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
  • HLD4
  • HSP-60
  • HSP65
  • HuCHA60
  • SPG13
  • 60kDa
  • Hsp60
  • Hspd1-30p
Bacteria, Plasmodium falciparum
Immunocytochemistry (ICC), Immunofluorescence (IF), Western Blotting (WB)
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Immunogen Recombinant full length PfHSP60
Specificity Detects ~ 60 kDa. Cross-reacts with E.coli HSP60, GroEl.
Purification Protein A Purified
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). 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).
Cellular Localization: Mitochondrion | Mitochondrion Matrix
NCBI Accession XM_001347402
UniProt P34940
Research Area Heat Shock Proteins
Application Notes Recommended Dilution: WB (1:2000), optimal dilutions for assays should be determined by the user.
Restrictions For Research Use only
Format Liquid
Concentration 1.83 mg/mL
Buffer PBS pH 7.4, 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
Supplier Images
 image for anti-Heat Shock 60kDa Protein 1 (Chaperonin) (HSPD1) antibody (ABIN361856) PfHsp60, malarial parasite lysate.
Background publications 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).

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).

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).

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