| Cat. No. |
CRP0842 |
| Product overview |
Recombinant Human
Chaperonin 10 produced in E. coli has a molecular mass of
approximately 11 KDa. |
| Description |
Chaperonin 60 (GroEL) and chaperonin 10 (GroES)
belong to the ubiquitous family of heat-shock molecular
chaperones found in prokaryotes and in eukaryotic organelles.
The chaperonins assist the folding of nascent,
organelle-imported or stress-destabilized polypeptides. In
vitro, purified GroEL together with purified GroES in the
presence of Mg-ATP facilitate refolding and reactivation of
denaturedproteins. Chaperonin 10 (GroES) is expressed in E.
coli. |
| Purity |
>95% as
determined by SDS-PAGE. |
| Storage buffer |
Liquid. In
Tris-HCl Buffer (pH 7.4). |
| Gene
Information |
Gene Name |
HSPE1 |
|
Synonyms |
CPN10; GROES;
HSP10; EPF; HSP10; Hsp10; 10 kDa chaperonin; 10 kDa heat shock
protein; mitochondrial; Early-pregnancy factor; chaperonin 10; heat shock 10kD protein 1 |
|
GeneID |
3336 |
|
mRNA Refseq |
NM_002157.1 |
|
Protein Refseq |
NP_002148.1 |
|
MIM |
600141 |
|
Unitprot ID |
P61604 |
|
Chromosome Location |
2q33.1 |
|
Function |
ATP binding, chaperone binding, unfold
protein binding |
|
Process |
caspase
activation, protein folding, response to unfolded protein |
.jpg) |
Download Datasheet
 |
|
A chaperonin
called GroEL-GroES complex (from Escherichia coli) (PDB
code=1aon). Two rings of 7x2GroEL proteins (shown in
blue and green) with a cap (just on one side) of GroES
proteins (red and yellow). Unfolded proteins enter that
cavity (which is protein sized) to be protected during
folding. |
|
