electron microscopy: suitable immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable indirect ELISA: suitable western blot: 1:400 using cultured human foreskin fibroblast extract
Heat shock (stress) proteins (HSP) are produced by prokaryotic and eukaryotic cells, and are among the most conserved molecules in phylogeny. HSP-60 is a member of HSP family with a uniquely high level of sequence conservation.
Monoclonal Anti-Heat Shock Protein 60 (mouse IgG1 isotype) is derived from the LK1 hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with recombinant human heat diseases.
Specificity
The antibody recognizes an epitope located between amino acid residues 383-447 of the human HSP 60. It is not cross-reactive with the bacterial counterpart (E. coli), or with helminth and spinach HSP60. The antibody reacts with constitutive and inducible HSP60. It demonstrates a raised level of staining in immunohistochemistry of synovial membranes taken from patients with juvenile chronic arthritis.
Immunogen
recombinant human heat shock protein 60 (HSP60)
Application
Monoclonal Anti-Heat Shock Protein 60 has been used in the following techniques:
Enzyme linked immunosorbent assay (ELISA)
Immunoblotting
Immunocytochemistry
Immunohistochemistry
Immunoelectron microscopy
Double immunofluorescence
Biochem/physiol Actions
A wide variety of environmental perturbations, such as a sudden increase in temperature, induce cells to rapidly synthesize a group of polypeptides known as the heat shock (stress) proteins. HSP-60 is considered to be a potential antigen in a number of autoimmune diseases. Abnormal immune reactivity involving shock protein 60 (HSP60) has also been implicated in the pathogenesis of schizophrenia. This monoclonal antibody enables the differentiation between the HSP60 of mammalian and bacterial origin.
Abnormal immune reactivity involving HSP60 has also been implicated in the pathogenesis of schizophrenia.
Physical form
Monoclonal Anti-Heat Shock Protein 60 is provided as ascites fluid with 0.1% sodium azide as a preservative.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Mitochondrial membrane permeabilization is a rate-limiting step of cell death. This process is, at least in part, mediated by opening of the permeability transition pore complex (PTPC) Several soluble proteins from the mitochondrial intermembrane space and matrix are involved in
Identification of antibodies to heat shock proteins 90 kDa and 70 kDa in patients with schizophrenia
Kim JJ, et al.
Schizophrenia Research, 52(1-2), 127-135 (2001)
Heat shock protein 60 levels in tissue and circulating exosomes in human large bowel cancer before and after ablative surgery
Campanella C, et al.
Cancer, 121(18), 3230-3239 (2015)
Elevated blood Hsp60, its structural similarities and cross-reactivity with thyroid molecules, and its presence on the plasma membrane of oncocytes point to the chaperonin as an immunopathogenic factor in Hashimoto's thyroiditis
The Journal of experimental medicine, 192(8), 1081-1092 (2000-10-18)
Syncytia arising from the fusion of cells expressing a lymphotropic HIV type 1-encoded envelope glycoprotein complex (Env) with cells expressing the CD4/CXC chemokine receptor 4 complex spontaneously undergo cell death. Here we show that this process is accompanied by caspase
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