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G6532

Sigma-Aldrich

Anti-GroEL antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonyme(s) :

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

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.46

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Espèces réactives

E. coli

Technique(s)

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

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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

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Description générale

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

Spécificité

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

Immunogène

purified recombinant GroEL produced in E. coli.

Application

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.

Actions biochimiques/physiologiques

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).

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

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

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

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
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)
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
Tetracycline treatment and sex-ratio distortion: a role for Wolbachia in the moulting of filarial nematodes?
Casiraghi M, et al.
International Journal For Parasitology, 32(12), 1457-1468 (2002)
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)
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