Skip to Content
Merck
All Photos(2)

Key Documents

View All Documentation

G6532

Sigma-Aldrich

Anti-GroEL antibody produced in rabbit

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

Sign Into View Organizational & Contract Pricing
All Photos(2)

About This Item

UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

Quality Level

200

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

Gene Information

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

Looking for similar products? Visit Product Comparison Guide

General description

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

Specificity

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

Immunogen

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.

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).

Physical form

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

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.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

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
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)
Nina Molin Høyland-Kroghsbo et al.
mBio, 9(6) (2018-11-15)
Clustered regularly interspaced short palindromic repeat (CRISPR)-associated (CRISPR-Cas) systems are adaptive defense systems that protect bacteria and archaea from invading genetic elements. In Pseudomonas aeruginosa, quorum sensing (QS) induces the CRISPR-Cas defense system at high cell density when the risk
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service