| Cat.
No. |
CRP0843 |
| Product
overview |
Recombinant Human
Chaperonin 60 produced in E. coli has a molecular mass of
approximately 60 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 denatured proteins. Chaperonin 60(GroEL) 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 |
HSPD1 |
|
Synonyms |
CPN60; GROEL;
HSP-60; HSP60; HSP65; Hsp60; HuCHA60; SPG13; chaperonin; 60 kDa
chaperonin; 60 kDa heat shock protein; mitochondrial precursor;
Heat shock protein 60; Mitochondrial matrix protein P1; P60
lymphocyte protein; heat shock 60kD protein 1 (chaperonin); heat
shock protein 65; short heat shock protein 60 Hsp60s1; spastic
paraplegia 13 (autosomal dominant) |
|
GeneID |
3329 |
|
mRNA Refseq |
NM_002156.4 |
|
Protein Refseq |
NP_002147.2 |
|
MIM |
118190 |
|
Uniprot ID |
P10809 |
|
Chromosome Location |
2q33.1 |
|
Pathway |
Prion disease,
Type I diabetes mellitus |
|
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. |
|
