GroEL recombinant protein

GroEL (E Coli), (recombinant)

Cat. Num. AAA565950

• Gene Names: groL; ECK4137; groEL; JW4103; mopA
• Applications: ELISA, Western Blot
• Purity: >=90% (SDS-PAGE; Western blot); Purified by multi-step chromatography
• Synonyms: GroEL; GroEL (E Coli); (recombinant); GroEL recombinant protein

• Host: E Coli
• Purity/Purification: >=90% (SDS-PAGE; Western blot); Purified by multi-step chromatography
• Form/Format: Liquid. In 50mM TRIS-HCl, pH7.5, containing 100 mM sodium chloride, 10mM magnesium chloride, 5mM DTT, and 0.05% sodium azide

• Applicable Applications for GroEL recombinant protein: ELISA (EIA), Western Blot (WB), in vitro Assay, Antigen microarray, Activity assay
• Preparation and Storage: For long term storage, store at -80 degree C; Shipping: Shipped on Dry Ice

Related Product Information for GroEL recombinant protein

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 3 7 degree C , increases to about 10% of the total protein content upon shifting the growth temperature to 46 degree C . 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.

Product Categories/Family for GroEL recombinant protein

Proteostasis; Protein Synthesis & Folding

NCBI and Uniprot Product Information

• NCBI GI #: 16131968
• NCBI GeneID: 948665
• NCBI Accession #: NP_418567.1
• NCBI GenBank Nucleotide #: NC_000913.3
• UniProt Accession #: P0A6F5; P06139; Q2M6G1
• Molecular Weight: 57,329 Da
• NCBI Official Full Name: Cpn60 chaperonin GroEL, large subunit of GroESL
• NCBI Official Symbol: groL
• NCBI Official Synonym Symbols: ECK4137; groEL; JW4103; mopA
• NCBI Protein Information: Cpn60 chaperonin GroEL, large subunit of GroESL
• UniProt Protein Name: 60 kDa chaperonin
• UniProt Gene Name: groL
• UniProt Entry Name: CH60_ECOLI

NCBI Description

groL is an essential gene. [More information is available at EcoGene: EG10599]. The Escherichia coli chaperone protein GroEL (Hsp60) and its regulator GroES are necessary for the proper folding of certain proteins , . [More information is available at EcoCyc: EG10599].

Uniprot Description

Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.