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P4689

Sigma-Aldrich

Protein G′ from proprietary source

recombinant, expressed in E. coli, lyophilized powder

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NACRES:
NA.46

recombinant

expressed in E. coli

Quality Level

conjugate

unconjugated

form

lyophilized powder

capacity

~5 mg/mg, solid binding capacity (IgG)

storage temp.

−20°C

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vibrant-m

G4386

γ-Globulins from human blood

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

300

conjugate

unconjugated

conjugate

peroxidase conjugate

conjugate

unconjugated

conjugate

-

storage temp.

−20°C

storage temp.

−20°C

storage temp.

2-8°C

storage temp.

2-8°C

form

lyophilized powder

form

lyophilized powder

form

essentially salt-free, lyophilized powder

form

powder

capacity

~5 mg/mg, solid binding capacity (IgG)

capacity

-

capacity

-

capacity

-

General description

Genetically engineered truncated protein G; retains affinity for IgG, but lacks albumin- and Fab- binding sites and membrane-binding regions.
Protein G is a group G Streptococcus protein and is a large multi-domain cell wall protein. It interacts with the Fc region of IgG (immunolglobulin) through its repeating 55-amino acid domain. Strain GX7809 and GX7805 contain two and three such protein repeats respectively.

Application

Protein G has been used for the analysis of mAb (monoclonal antibody) synergy towards hCG (human chorionic gonadotropin) using surface plasmon resonance (SPR), and for serum IgG galactosylation obtained from RA (rheumatoid arthrtitis) patients and MRL-lpr mice.

Biochem/physiol Actions

Protein G is implicated in the evasion of host defence response by Streptococcus, via its protein binding properties. It is interacts with α2-micorglobulin which is a predominant inhibitor of human plasma.

Physical form

Lyophilized from water.

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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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25G
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Arie Ryvkin et al.
PloS one, 7(8), e41469-e41469 (2012-08-08)
Polyclonal serum consists of vast collections of antibodies, products of differentiated B-cells. The spectrum of antibody specificities is dynamic and varies with age, physiology, and exposure to pathological insults. The complete repertoire of antibody specificities in blood, the IgOme, is
C R Goward et al.
The Biochemical journal, 267(1), 171-177 (1990-04-01)
The gene for Protein G from Streptococcus strain G148 was cloned and expressed in Escherichia coli. The regions on the gene corresponding to the albumin-binding domains and the Fab-binding region were then deleted by site-directed mutagenesis. The translation of regions
Oleksiy Krupin et al.
Sensors (Basel, Switzerland), 19(3) (2019-02-06)
Straight long-range surface plasmon-polariton (LRSPP) waveguides as biosensors for label-free detection are discussed. The sensors consist of 5-μm-wide 35-nm-thick gold stripes embedded in a low-index optical-grade fluoropolymer (CYTOPTM) with fluidic channels etched to the Au surface of the stripes. This
Thomas Pausch et al.
Pancreas, 47(5), 561-567 (2018-04-24)
Defensins are antimicrobial peptides playing a role in innate immunity, in epithelial cell regeneration, and in carcinogenesis of inflammation-triggered malignancies. We analyzed this role in pancreatic ductal adenocarcinoma (PDAC) in the context of its association with chronic pancreatitis (CP). Human
A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G.
Gronenborn AM et al
Science, 253(5020), 657-661 (1991)

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