Product: HSP60 Antibody
Catalog: AF5374
Description: Rabbit polyclonal antibody to HSP60
Application: WB IHC IF/ICC
Cited expt.: WB, IF/ICC
Reactivity: Human, Mouse, Rat, Monkey
Prediction: Zebrafish, Bovine, Horse, Sheep, Rabbit, Xenopus
Mol.Wt.: 60 kDa; 61kD(Calculated).
Uniprot: P10809
RRID: AB_2837859

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 100ul $280 In stock
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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat,Monkey
Prediction:
Zebrafish(88%), Bovine(100%), Horse(89%), Sheep(100%), Rabbit(100%), Xenopus(100%)
Clonality:
Polyclonal
Specificity:
HSP60 Antibody detects endogenous levels of total HSP60.
RRID:
AB_2837859
Cite Format: Affinity Biosciences Cat# AF5374, RRID:AB_2837859.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

60 kDa chaperonin; 60 kDa heat shock protein, mitochondrial; CH60_HUMAN; Chaperonin 60; Chaperonin, 60-KD; CPN60; fa04a05; GROEL; heat shock 60kDa protein 1 (chaperonin); Heat shock protein 1 (chaperonin); Heat shock protein 60; Heat shock protein 65; heat shock protein family D (Hsp60) member 1; HLD4; Hsp 60; HSP 65; HSP-60; HSP60; HSP65; HSPD1; HuCHA60; Mitochondrial matrix protein P1; P60 lymphocyte protein; short heat shock protein 60 Hsp60s1; SPG13;

Immunogens

Immunogen:

A synthesized peptide derived from human HSP60, corresponding to a region within C-terminal amino acids.

Uniprot:
Gene(ID):
Description:
Implicated in mitochondrial protein import and macromolecular assembly. May facilitate 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.
Sequence:
MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIATGGAVFGEEGLTLNLEDVQPHDLGKVGEVIVTKDDAMLLKGKGDKAQIEKRIQEIIEQLDVTTSEYEKEKLNERLAKLSDGVAVLKVGGTSDVEVNEKKDRVTDALNATRAAVEEGIVLGGGCALLRCIPALDSLTPANEDQKIGIEIIKRTLKIPAMTIAKNAGVEGSLIVEKIMQSSSEVGYDAMAGDFVNMVEKGIIDPTKVVRTALLDAAGVASLLTTAEVVVTEIPKEEKDPGMGAMGGMGGGMGGGMF

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Bovine
100
Sheep
100
Xenopus
100
Rabbit
100
Horse
89
Zebrafish
88
Chicken
70
Pig
0
Dog
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

Research Backgrounds

Function:

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. 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).

Subcellular Location:

Mitochondrion matrix.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Family&Domains:

Belongs to the chaperonin (HSP60) family.

Research Fields

· Genetic Information Processing > Folding, sorting and degradation > RNA degradation.

· Human Diseases > Endocrine and metabolic diseases > Type I diabetes mellitus.

· Human Diseases > Infectious diseases: Bacterial > Legionellosis.

· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.

References

1). Hsp60 exerts a tumor suppressor function by inducing cell differentiation and inhibiting invasion in hepatocellular carcinoma. Oncotarget, 2016 (PubMed: 27677587)

Application: WB    Species: human    Sample:

A-B. qRT-PCR and western blot analyses for the mRNA and protein expression of Hsp60 in tumor and paired peritumor tissues from HCC patients.

Application: IF/ICC    Species: human    Sample:

E. Immunofluorescence analysis of the Hsp60 expression in BEL-7402 cell (Scale bars, 10μm)

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Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
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