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Key Documents

P4689

Sigma-Aldrich

Protein G′ from proprietary source

recombinant, expressed in E. coli, lyophilized powder

Sinónimos:

G′ protein

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About This Item

UNSPSC Code:
12352203
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

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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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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
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
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
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
T Klonisch et al.
Immunology, 89(2), 165-171 (1996-10-01)
The effects of orientating pairs of synergistic monoclonal antibodies (mAb) on binding of human chorionic gonadotropin (hCG) was studied by radioimmunoassay (RIA), enzyme-linked immunosorbent assay (ELISA) and surface plasmon resonance (SPR). Antibody synergy towards hCG required two functionally intact antibodies

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