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rabbit anti-Hsp60 polyclonal antibody 2417


Antibody summary

  • Rabbit polyclonal to Hsp60
  • Suitable for: WB, ICC/IF, IHC
  • Reacts with: human, mouse, rat
  • Isotype: IgG
  • 100 µL, 25 µL, 1 mL
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SKU: 2417parent Categories: , Tags: , ,
Weight1 lbs
Dimensions9 × 5 × 2 in










available sizes

1 mL, 100 µL, 25 µL

Database link:
human P10809
mouse P63038
rat P63039
Tested applications
Recommended dilutions
WB: 1:5000-10000 ICC/IF and IHC: 1:5000
Recombinant full length human HSP60 expressed in and purified from E. coli
Size and concentration
25, 100, 1000µL and serum
Storage Instructions
2-8°C for short term, for longer term at -20°C. Avoid freeze / thaw cycles.
Storage buffer
serum, 0.04% NaN3 added
Compatible secondaries
goat anti-rabbit IgG, H&L chain specific, peroxidase conjugated, conjugated polyclonal antibody 9512
goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody 2079
goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody 7863
goat anti-rabbit IgG, H&L chain specific, Cross Absorbed polyclonal antibody 2371
goat anti-rabbit IgG, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1715
goat anti-rabbit IgG, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1720
Isotype control
Rabbit polyclonal - Isotype Control
target relevance
Heat shock protein 60 (HSP60), also known as chaperonin 60, is a highly conserved molecular chaperone in mitochondria that assists in the folding and assembly of newly synthesized proteins, particularly under conditions of cellular stress. This antibody can be used as a loading control when run alongside proteins, particularly mitochondrail proteins, of interest with different and resolvable molecular weights and ideally in combination with antibodies of same host and when using a secondary antibody.

Click for more on: loading controls and HSP60
Protein names
60 kDa heat shock protein, mitochondrial (EC (60 kDa chaperonin) (Chaperonin 60) (CPN60) (Heat shock protein 60) (HSP-60) (Hsp60) (HuCHA60) (Mitochondrial matrix protein P1) (P60 lymphocyte protein)
Gene names
Protein family
Chaperonin (HSP60) family
Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:1346131, PubMed:11422376). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable).
Catalytic activity
Reaction=ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide.; EC=; Evidence=;
Subellular location
Mitochondrion matrix.
Homoheptamer arranged in a ring structure (PubMed:1346131, PubMed:11422376, PubMed:25918392). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. Interacts with 2 heptameric Hsp10 rings to form the symmetrical football complex (PubMed:25918392). Interacts with HRAS (By similarity). Interacts with ATAD3A (PubMed:22664726). Interacts with ETFBKMT and EEF1AKMT3 (PubMed:23349634). Interacts with MFHAS1 (PubMed:24286120). ; (Microbial infection) Interacts with hepatitis B virus/HBV protein X. ; (Microbial infection) Interacts with HTLV-1 protein p40tax.
Target Relevance information above includes information from UniProt accession : P10809
The UniProt Consortium


Confocal immunofluorescent analysis of HeLa cells stained with rabbit pAb to HSP60, 2417, dilution 1:1,000, in red, and costained with chicken pAb to vimentindilution 1:1,000 in green. The blue is DAPI staining of nuclear DNA. The HSP60 antibody gives strong and specific staining of mitochondria while the vimentin antibody reveals cytoplasmic intermediate filaments.
Chromogenic immunostaining of a formalin fixed paraffin embedded mouse pons section with rabbit pAb to HSP60, 2417, dilution 1:1,000, detected with DAB (brown) using the Vector Labs ImmPRESS method and reagents with citra buffer retrieval. Hematoxylin (blue) was used as the counterstain. HSP60 antibody specifically detects mitochondria and produces a granular cytoplasmic staining pattern in most cells types. Mouse select image for larger view.
Western blot analysis of different tissue or cell lysates using rabbit pAb to HSP-60, 2417, dilution 1:5,000 in red. [1] protein standard, [2] rat brain, [3] mouse brain, [4] NIH-3T3, [5] HEK293, [6] HeLa, [7] SH-SY5Y cells. The strong 60kDa band present in all preparations corresponds to HSP60 protein. The blot was simultaneously probed with mouse mAb to HSP27 dilution 1:10,000, in green. Strong single band at ~27kDa corresponds to the HSP27 protein, detected only in human cell lines since this particular antibody does not recognize rodent HSP27.


Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.

22074436Heat shock protein-60 and risk for cardiovascular diseaseRizzo M, Macario AJ, de Macario EC, Gouni-Berthold I, Berthold HK, Rini GB, Zummo G, Cappello F.Curr Pharm Des. 2011 Nov;17(33):3662-8. doi: 10.2174/138161211798220981.
14597775A function for the mitochondrial chaperonin Hsp60 in the structure and transmission of mitochondrial DNA nucleoids in Saccharomyces cerevisiaeKaufman BA, Kolesar JE, Perlman PS, Butow RA.J Cell Biol. 2003 Nov 10;163(3):457-61. doi: 10.1083/jcb.200306132. Epub 2003 Nov 3.
14585136Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperonesRanford JC, Coates AR, Henderson B.Expert Rev Mol Med. 2000 Sep 15;2(8):1-17. doi: 10.1017/S1462399400002015.
10604986Cutting edge: heat shock protein (HSP) 60 activates the innate immune response: CD14 is an essential receptor for HSP60 activation of mononuclear cellsKol A, Lichtman AH, Finberg RW, Libby P, Kurt-Jones EA.J Immunol. 2000 Jan 1;164(1):13-7. doi: 10.4049/jimmunol.164.1.13.
10467106Identification of human heat shock protein 60 (Hsp60) and anti-Hsp60 antibodies in the peripheral circulation of normal individualsPockley AG, Bulmer J, Hanks BM, Wright BH.Cell Stress Chaperones. 1999 Mar;4(1):29-35. doi: 10.1054/csac.1998.0121.
9476895The Hsp70 and Hsp60 chaperone machinesBukau B, Horwich AL.Cell. 1998 Feb 6;92(3):351-66. doi: 10.1016/s0092-8674(00)80928-9.
1347713Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane spaceKoll H, Guiard B, Rassow J, Ostermann J, Horwich AL, Neupert W, Hartl FU.Cell. 1992 Mar 20;68(6):1163-75. doi: 10.1016/0092-8674(92)90086-r.


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