Certificate of Analysis and Data Sheet

Source:
E.Coli

Catalog No.
HSP-005

Description :

GroES protein is the co-chaperonin of GroES in E.coli and assists protein folding. GroEL mediated folding requires the co-chaperonin GroES which is essential for viability. GroES is composed of a single heptameric ring of 10kDa subunits that binds to the ends of the GroEL cylinder. GroES gene was amplified by PCR from E.coli and cloned into an expression vector. This protein was overexpressed in E.coli and was purified by using conventional chromatography techniques.
Recombinant GroES produced in E.Coli is a single,non-glycosylated polypeptide chain conjtaining 97 amino acids and having a molecular mass of 10.4 kDa.

Physical Appearance:

Sterile filtered clorless solution.

Formulation:

The protein (1mg/ml) contains 25mM Tris-HCl buffer (pH 7.5), 100mM NaCl, 1mM DTT and 10% Glycerol.

Stability:

Store at 4蚓 if entire vial will be used within 2-4 weeks.
Store, frozen at -20蚓 for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.

Purity:

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by reducing and non-reducing SDS-PAGE Coomassie.

Sequence:

MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE NGEVKPLDVKVGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA.

Usage:

This material is offered by ProSpec-TechnoGene for research, laboratory or further evaluation purposes.

Latest Publications:

1. Allosteric signaling of ATP hydrolysis in GroEL-GroES complexes.
Nat Struct Mol Biol 2006 Jan 22;
2. Modulation of costimulatory molecules CD80/CD86 on B cells and macrophages by stress proteins GroEL, GroES and DnaK.
Int J Immunopathol Pharmacol 2005 Oct-Dec;18(4):637-44
3. Improvement in the expression of CYP2B6 by co-expression with molecular chaperones GroES/EL in Escherichia coli.
Protein Expr Purif 2005 Nov 9;
4. Amyloid-like fibril formation of co-chaperonin GroES: nucleation and extension prefer different degrees of molecular compactness.
J Mol Biol 2005 Sep 2;351(5):1057-69
5. Multiple equilibria of the Escherichia coli chaperonin GroES revealed by m ass spectrometry.
Protein Sci 2005 May;14(5):1375-9
6. No evidence for a forced-unfolding mechanism during ATP/GroES binding to substrate-bound GroEL: no observable protection of metastable Rubisco intermediate or GroEL-bound Rubisco from tritium exchange.
FEBS Lett 2005 Feb 14;579(5):1183-6