antibody

Anti-Heat shock protein 60, HSP60 antibody

MBS355099

0.1 mg

285 USD

monoclonal

mouse

nonconjugated

H6-2

human, mouse, thale cress

western blot, immunohistochemistry, immunocytochemistry, immunohistochemistry - paraffin section

Antibody

Anti-Heat shock protein 60, HSP60 antibody

Heat shock protein 60, HSP60

Monoclonal Anti- Heat shock protein 60; HSP60

heat shock protein 60; Chaperonin CPN60, mitochondrial; heat shock protein 60; HSP60

HSP60

HSP60; CPN60; heat shock protein 60; HEAT SHOCK PROTEIN 60-3B; HSP60; HSP60-3B

CH60A_ARATH

Monoclonal

IgG1

H6-2

Mouse

Human, mouse

Protein A or Protein G purified

Liquid

Store at 4 degree C after thawing (1 week). Aliquot and store at -20 degree C for long term (at least one year). Avoid repeated freeze and thaw cycles

Western Blot (WB), Immunohistochemistry (IHC) Paraffin, Immunocytochemistry (ICC)

WB (1:5000)

Immunogen: A synthetic peptide (conjugated with KLH) corresponding to the C-terminal of HSP60.

Storage Buffer: In TBS (pH7.4), 0.5% BSA, 40% Glycerol and 0.05% Sodium Azide. Storage Buffer: In TBS (pH7.4), 0.5% BSA, 40% Glycerol and 0.05% Sodium Azide.

Heat shock protein 60 (HSP60) in the matrix of mitochondria is essential for the folding and assembly of newly imported proteins. Hsp60 belongs to a class of structurally related chaperonins found in organelles of endosymbiotic origin and in the bacterial cytosol.1 Members of the chaperonin class include the Escherichia coli, groEL protein and the Rubisco subunit-binding protein of chloroplasts.2 In both prokaryotic and eukaryotic systems, synthesis of these proteins is induced in response to stresses, such as heat shock.3 Under normal physiological conditions, HSP60 is a 60 KD oligomer composed of monomers that form a complex arranged as two stacked heptameric rings.1 HSP60 may be a very useful marker for patients with superficial bladder carcinoma and may be used for predicting disease progression. And low HSP60 expression levels may be usable as a prognostic marker to identify patients for whom local treatment would be insufficient.4 HSP60 also linked to diabetes, cancer and certain types of immunological disorders.

1. Cheng MY, Hartl FU, Horwich AL (November 1990). "The mitochondrial chaperonin hsp60 is required for its own assembly". Nature 348 (6300): 455-8. 2. Cheng, M. Y., Hartl, F.-U., Martin, J., Pollock, R. A., Kalousek, F., Neupert, W., Hallberg, E. M., Hallberg, R. L., Horwich, A. L. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337: 620-625, 1989. 3. Venner, T. J., Singh, B., Gupta, R. S. Nucleotide sequences and novel structural features of human and Chinese hamster hsp60 (chaperonin) gene families. DNA Cell Biol. 9: 545-552, 1990. 4. Lebret T, Watson RW, Molinié V, et al. (September 2003). "Heat shock proteins HSP27, HSP60, HSP70, and HSP90: expression in bladder carcinoma". Cancer 98 (5): 970-7.

15229559

NP_189041.1

NM_113304.4

P29197

61,281 Da

RNA Degradation Pathway (116162); RNA Degradation Pathway (116127)

mitochondrial chaperonin HSP. assist in rapid assembly of the oligomeric protein structures in the mitochondria.

Function: 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. Subcellular location: Mitochondrion. Induction: By heat shock. Sequence similarities: Belongs to the chaperonin (HSP60) family.

0.1 mg

285 USD