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AB51307

Recombinant E. coli groEL protein (Tag Free)

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Recombinant E. coli groEL protein (Tag Free) is a Escherichia coli K-12 Full Length protein, in the 1 to 548 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.

View Alternative Names

groL, mopA, b4143, JW4103, groEL, Chaperonin GroEL, 60 kDa chaperonin, Chaperonin-60, GroEL protein, Cpn60

1 Images
SDS-PAGE - Recombinant E. coli groEL protein (Tag Free) (AB51307)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant E. coli groEL protein (Tag Free) (AB51307)

ab51307 in 15% SDS-PAGE

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P0A6F5

Animal free

No

Carrier free

No

Species

Escherichia coli K-12

Storage buffer

pH: 7.5 Constituents: 10% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.395% Tris HCl, 0.077% (R*,R*)-1,4-Dimercaptobutan-2,3-diol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":548,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P0A6F5","tags":[]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The groEL protein often known as 60 kDa chaperonin is a highly conserved molecular chaperone with an approximate mass of 60 kilodaltons. It plays an integral role in assisting the correct folding of nascent or stress-denatured proteins in the cell. Expressed prominently in prokaryotic organisms such as E. coli groEL is an important component of the E. coli expression system due to its ability to maintain protein functionality. By forming a double-ring structure that encapsulates substrates groEL collaborates with its co-chaperonin groES to perform essential protein folding.
Biological function summary

GroEL functions in collaboration with groES as part of a chaperonin complex that stabilizes unfolded proteins and prevents aggregation. It operates by undergoing ATP-dependent conformational changes that create an environment conducive to proper protein folding. E. coli products such as enzymes and structural proteins rely on the folding mechanism orchestrated by groEL to achieve their native conformation. Consequently its role is indispensable for protein homeostasis within E. coli affecting diverse cellular processes.

Pathways

Molecular chaperones including groEL integrate into the protein quality control network which monitors and manages protein integrity and turnover. In particular groEL operates in the folding and stress response pathways. Working closely with other proteins such as DnaK and DnaJ groEL ensures efficient protein folding and repair especially during heat shock conditions. This function maintains cellular viability and is important for cellular adaptation to environmental stressors.

Disruptions in groEL function can lead to protein misfolding-related diseases like Alzheimer's and Parkinson's. Although direct links to groEL are less observed in eukaryotic systems similar chaperone proteins like HSP60 show connections to neurodegenerative disorders. Dysfunctional protein homeostasis due to insufficient chaperone activity highlights the role of molecular chaperones in preventing protein aggregation which is implicated in these diseases.
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Specifications

Form

Liquid

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General info

Function

Together with its co-chaperonin GroES, plays an essential role in assisting protein folding (PubMed : 10532860, PubMed : 16751100, PubMed : 1676490, PubMed : 18418386, PubMed : 18987317, PubMed : 20603018, PubMed : 24816391, PubMed : 2573517, PubMed : 2897629, PubMed : 8104102, PubMed : 9285593). The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding, probably by preventing aggregation and by entropically destabilizing folding intermediates (PubMed : 16751100, PubMed : 18418386, PubMed : 18987317, PubMed : 20603018, PubMed : 24816391). Rapid binding of ATP, followed by slower binding of the non-native substrate protein and GroES to the cis open ring of GroEL initiates productive folding of the non-native protein inside a highly stable GroEL-ATP-GroES complex (PubMed : 19915138, PubMed : 22445172, PubMed : 9285585, PubMed : 9285593). Binding of ATP and GroES induces conformational changes that result in the release of the substrate protein into a nano-cage compartment, within the GroEL central cavity, for folding in isolation (PubMed : 16684774, PubMed : 22445172, PubMed : 8861908, PubMed : 9285585). To discharge GroES and substrate protein, ATP hydrolysis in the cis ring is required to form a GroEL-ADP-GroES complex with decreased stability (PubMed : 9285593). Finally, binding of ATP to the opposite trans ring of GroEL results in disassembly of the cis-ternary complex, which opens the cage and allows release of the folded protein (PubMed : 9285585, PubMed : 9285593). Proteins released in non-native form may be rapidly rebound by another GroEL complex until all of the initially bound polypeptide reaches native form (PubMed : 7867798, PubMed : 7915201). Can rescue kinetically trapped intermediates (PubMed : 20603018). GroEL shows ATPase activity (PubMed : 1676490, PubMed : 379350, PubMed : 9285593). ATP hydrolysis moves the reaction cycle forward but is not required for substrate folding (PubMed : 9285593).. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.. (Microbial infection) Essential for the assembly of several bacteriophages.

Sequence similarities

Belongs to the chaperonin (HSP60) family.

Post-translational modifications

Phosphorylated reversibly during heat shock.

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Product protocols

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Target data

Together with its co-chaperonin GroES, plays an essential role in assisting protein folding (PubMed : 10532860, PubMed : 16751100, PubMed : 1676490, PubMed : 18418386, PubMed : 18987317, PubMed : 20603018, PubMed : 24816391, PubMed : 2573517, PubMed : 2897629, PubMed : 8104102, PubMed : 9285593). The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding, probably by preventing aggregation and by entropically destabilizing folding intermediates (PubMed : 16751100, PubMed : 18418386, PubMed : 18987317, PubMed : 20603018, PubMed : 24816391). Rapid binding of ATP, followed by slower binding of the non-native substrate protein and GroES to the cis open ring of GroEL initiates productive folding of the non-native protein inside a highly stable GroEL-ATP-GroES complex (PubMed : 19915138, PubMed : 22445172, PubMed : 9285585, PubMed : 9285593). Binding of ATP and GroES induces conformational changes that result in the release of the substrate protein into a nano-cage compartment, within the GroEL central cavity, for folding in isolation (PubMed : 16684774, PubMed : 22445172, PubMed : 8861908, PubMed : 9285585). To discharge GroES and substrate protein, ATP hydrolysis in the cis ring is required to form a GroEL-ADP-GroES complex with decreased stability (PubMed : 9285593). Finally, binding of ATP to the opposite trans ring of GroEL results in disassembly of the cis-ternary complex, which opens the cage and allows release of the folded protein (PubMed : 9285585, PubMed : 9285593). Proteins released in non-native form may be rapidly rebound by another GroEL complex until all of the initially bound polypeptide reaches native form (PubMed : 7867798, PubMed : 7915201). Can rescue kinetically trapped intermediates (PubMed : 20603018). GroEL shows ATPase activity (PubMed : 1676490, PubMed : 379350, PubMed : 9285593). ATP hydrolysis moves the reaction cycle forward but is not required for substrate folding (PubMed : 9285593).. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.. (Microbial infection) Essential for the assembly of several bacteriophages.
See full target information groEL
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