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Recombinant Escherichia coli 10 kDa chaperonin (groS)

Recombinant Escherichia coli 10 kDa chaperonin (groS)

Code	CSB-YP363855ENV
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP363855ENV
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP363855ENV-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code	CSB-BP363855ENV
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP363855ENV
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Product Details
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Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

groS

Uniprot No.

P0A6F9

Alternative Names

groS; groES; mopB; b4142; JW410210 kDa chaperonin; GroES protein; Protein Cpn10

Species

Escherichia coli (strain K12)

Expression Region

1-97

Target Protein Sequence

MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE NGEVKPLDVK VGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA

Protein Length

full length protein

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function

Together with the chaperonin GroEL, plays an essential role in assisting protein folding. 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. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel. Regulates the ATPase activity of GroEL.; (Microbial infection) Essential for the assembly of several bacteriophages.

Gene References into Functions

Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes PMID: 23048033
Studies indicate that the amount of GroEL and GroES in an E. coli cell under normal conditions is sufficient to assist in the folding of no more than 5% of the proteins within the cell. PMID: 22177460
substrate folding activity of a single ring GroEL variant is stimulated by modulating the cochaperonin GroES PMID: 21757689
unfolded GroES has covalent structural changes that lead to amyloid fibril formation detected by NMR PMID: 21507961
The association of ATP and GroES to a polypeptide-bound ring of GroEL encapsulates the folding proteins in the central cavity of that ring (cis ring) and allows it to fold in a protected environment where the risk of aggregation is reduced. PMID: 20006619
structural analysis of GroEL and its binding to GroES PMID: 15475965
the two stages of GroES fibril formation prefer different molecular states of the same protein PMID: 16054644
a shift in orientation of GroEL apical domains between the apo-protein and stable GroEL.GroES complexes is highly ordered, and transient conformational intermediates permit the association of GroES before the displacement of bound polypeptide PMID: 16684774
GroEL holds the nascent chain on the ribosome in a polypeptide length-dependent manner and post-translationally encapsulates the polypeptide using the GroES cap to accomplish the chaperonin-mediated folding process. PMID: 16754671
Coexpression of GroEL and GroES enhanced the growth rate of aconitase producing cells by 30%. PMID: 16822698
F170L su substitution has a decreased requirement for the chaperones GroEL and GroES as a result of restoring the temperature-sensitive-folding coat proteins to a wild type-like state. PMID: 17441504
Data show that structure-forming characteristics of GroES appear to be conserved through the backbone reversal process, although the differential conformational behavior upon heating also indicates differences. PMID: 18359305
The GroEL/GroES compartment is essential for protein folding in vivo. PMID: 18418386
there is an an intermediate GroEL/substrate/GroES complex in which the substrate and GroES bind to GroEL by sharing seven common binding sites PMID: 18430731

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Subcellular Location

Cytoplasm. Note=Exclusively localized in foci, usually near 1 cell pole in mid-to-late exponential phase; polar localization depends on the minCDE operon. Foci form near midcell.

Protein Families

GroES chaperonin family

Database Links

KEGG: ecj:JW4102

STRING: 316385.ECDH10B_4335

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