G6532

Anti-GroEL antibody produced in rabbit

Name: Anti-GroEL antibody produced in rabbit
Brand: SIGMA

IgG fraction of antiserum, buffered aqueous solution

Synonym(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

NACRES:

NA.46

UNSPSC Code:

12352203

Product Name

Anti-GroEL antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

E. coli

technique(s)

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

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

200

Gene Information

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

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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.

Biochem/physiol Actions

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).

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

Disclaimer

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.

General description

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

Immunogen

purified recombinant GroEL produced in E. coli.

Physical form

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

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Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

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Certificates of Analysis (COA)

Lot/Batch Number

0000447549

0000342519

0000213581

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Translation Stress Positively Regulates MscL-Dependent Excretion of Cytoplasmic Proteins.

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

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)

Recognition of the small regulatory RNA RydC by the bacterial Hfq protein.

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

Immunohistochemical/immunogold detection and distribution of the endosymbiont Wolbachia of Dirofilaria immitis and Brugia pahangi using a polyclonal antiserum raised against WSP (Wolbachia surface protein).

Kramer L, et al.

Parasitology Research, 89(5), 381-386 (2003)

TraN: A novel repressor of an Enterococcus conjugative type IV secretion system.

Verena Kohler et al.

Nucleic acids research, 46(17), 9201-9219 (2018-07-31)

The dissemination of multi-resistant bacteria represents an enormous burden on modern healthcare. Plasmid-borne conjugative transfer is the most prevalent mechanism, requiring a type IV secretion system that enables bacteria to spread beneficial traits, such as resistance to last-line antibiotics, among

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