GroEL (E. coli), (recombinant) | Enzo Life Sciences ADI-SPP-610-D product information

This webpage contains legacy information. The product is either no longer available from the supplier or has been delisted at Labome.

product summary

company name :

Enzo Life Sciences

other brands :

Stressgen, BioMol, Alexis Corporation, Assay Designs, Alexis

product type :

protein

product name :

GroEL (E. coli), (recombinant)

catalog :

ADI-SPP-610-D

quantity :

50 µg

citations: 4

Reference
Quintana F, Farez M, Viglietta V, Iglesias A, Merbl Y, Izquierdo G, et al. Antigen microarrays identify unique serum autoantibody signatures in clinical and pathologic subtypes of multiple sclerosis. Proc Natl Acad Sci U S A. 2008;105:18889-94 pubmed publisher
Kalayoglu M, Galvan C, Mahdi O, Byrne G, Mansour S. Serological association between Chlamydia pneumoniae infection and age-related macular degeneration. Arch Ophthalmol. 2003;121:478-82 pubmed
Habich C, Kempe K, van der Zee R, Burkart V, Kolb H. Different heat shock protein 60 species share pro-inflammatory activity but not binding sites on macrophages. FEBS Lett. 2003;533:105-9 pubmed
Mahdi O, Horne B, Mullen K, Muhlestein J, Byrne G. Serum immunoglobulin G antibodies to chlamydial heat shock protein 60 but not to human and bacterial homologs are associated with coronary artery disease. Circulation. 2002;106:1659-63 pubmed

product information

Product ID :

ADI-SPP-610

Catalog Number :

ADI-SPP-610-D

Product Name :

GroEL (E. coli), (recombinant)

Product Type :

Protein

Size :

50 µg

list of Pubmed id :

19028871, 12695244, 12505167, 12270859

Background :

In its native form, GroEL exists as a 14-mer consisting of two stacked rings each composed of seven identical subunits of Mw ~57,250. Molecular chaperones, such as GroEL and GroES, are thought to function by interacting with transiently exposed interactive peptide surfaces during its nascent synthesis, folding, transport and oligomerization. The net effect of chaperone participation in these processes is a reduction in inappropriate protein-protein interactions that might produce a nonfunctional structure. The GroEL/GroES complex has a high affinity for peptides during ATP hydrolysis when protein substrates would undergo repeated cycles of assisted folding. The GroEL and GroES genes, constituting the GroE operon, are members of the heat shock regulon ofE. coli. Synthesis of the GroE protein, which accounts for approximately 1% of the cellular protein at 37oC, increases to about 10% of the total protein content upon shifting the growth temperature to 46oC. In vivo and in vitro studies have demonstrated that the GroE system participates in facilitating protein folding/ renaturation, for example: 1) Both GroEL and GroES are required for in vivo assembly of the prokaryotic ribulose bisphosphatase carboxylases (RuBisCo’s) inE. coli, 2) Mutations in the groE locus have been shown to interfere with the assembly of heads of bacteriophages lambda and T 2, 3) Chemically denatured citrate synthase refolds to an active, nonaggregated form in the presence of GroEL, GroES, and Mg-ATP, 4) The sigma-subunit of Streptomyces coelicolor RNA polymerase can be renatured in the presence of GroEL after elution from a SDS-polyacrylamide gel, 5) GroEL and GroES facilitated the in vitro refolding of the monomeric mitochondrial enzyme rhodanese, 6) The aggregation of the non-native states(s) of oat phytochrome can be suppressed by interaction with GroEL and a stable binary complex can form between the two proteins.

ALTnames :

Heat shock protein 60, 60kDa Chaperonin, Protein Cpn60 GroEL protein, HSP60

Purity :

≥90% (SDS-PAGE; Western blot)

Buffer :

Liquid. In 50mM TRIS-HCl, pH 7.5, containing 100 mM sodium chloride, 10mM magnesium chloride, 5mM DTT, and 0.05% sodium azide.

Uses :

ATPase activity assay (positive). Western blot control.

Application Summary :

ELISA, WB, in vitro Assay, Antigen microarray, Activity assay

Storage :

-80°C