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Merck

G6532

Sigma-Aldrich

Anti-GroEL antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(e):

Anti-GroEL, GroEL Antibody - Anti-GroEL antibody produced in rabbit - Tested Applications: immunoblotting 1:80,000,indirect ELISA 1:40,000-1:80,000 - Sigma Aldrich G6532, Groel Antibody

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About This Item

UNSPSC-Code:
12352203
NACRES:
NA.46

Biologische Quelle

rabbit

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

IgG fraction of antiserum

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Speziesreaktivität

E. coli

Methode(n)

indirect ELISA: 1:40,000-1:80,000
western blot: 1:80,000

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

Escherichia coli ... groEL(913705) , groEL(913705)
Escherichia coli K12 ... Grol(948665)

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Allgemeine Beschreibung

GroEL protein belongs to the folding chaperonin family. It is a 58.3 kDa protein with apical, intermediate and equatorial functional domains.

Spezifität

The antibody does not cross-react with GroES and bovine HSP 70.

Immunogen

purified recombinant GroEL produced in E. coli.

Anwendung

Anti-GroEL antibody produced in rabbit has been used as positive control in histology and immunohistochemistry of Dirofilaria immitis, nematode worms and in the western blot analysis of the HeLa cells.

Biochem./physiol. Wirkung

GroEL, together with GroES, in the presence of ATP, assists in protein folding. Co-expression of aldehyde dehydrogenase with GroEL/GroES promotes folding and higher production of protein in soluble form. GroES and GroEL bind to the protein substrate, enclosing it in a cage like fold. The target protein after folding gets dissociated from the cage and is accompanied with hydrolysis of adenosine triphosphate (ATP) to adenosine diphosphate (ADP).

Physikalische Form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide

Haftungsausschluss

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Lagerklassenschlüssel

12 - Non Combustible Liquids

WGK

WGK 1

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable

Persönliche Schutzausrüstung

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Analysenzertifikate (COA)

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Die Dokumentenbibliothek aufrufen

Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli.
Lee KH, et al.
Biochemical and Biophysical Research Communications, 298(2), 216-224 (2002)
Rosa Morra et al.
mBio, 9(1) (2018-02-01)
The apparent mislocalization or excretion of cytoplasmic proteins is a commonly observed phenomenon in both bacteria and eukaryotes. However, reports on the mechanistic basis and the cellular function of this so-called "nonclassical protein secretion" are limited. Here we report that
Functional characterization of an archaeal GroEL/GroES chaperonin system Significance of substrate encapsulation.
Figueiredo L, et al.
The Journal of Biological Chemistry, 279(2), 1090-1099 (2004)
Daniela Dimastrogiovanni et al.
eLife, 3 (2015-01-01)
Bacterial small RNAs (sRNAs) are key elements of regulatory networks that modulate gene expression. The sRNA RydC of Salmonella sp. and Escherichia coli is an example of this class of riboregulators. Like many other sRNAs, RydC bears a 'seed' region
The chlamydial periplasmic stress response serine protease cHtrA is secreted into host cell cytosol.
Wu X, et al.
BMC Microbiology, 11(1), 87-87 (2011)

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