P4689
Protein G′ from proprietary source
recombinant, expressed in E. coli, lyophilized powder
Synonym(s):
G′ protein
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About This Item
NACRES:
NA.46
UNSPSC Code:
12352203
Form:
lyophilized powder
Recombinant:
expressed in E. coli
Product Name
Protein G′ from proprietary source, recombinant, expressed in E. coli, lyophilized powder
recombinant
expressed in E. coli
conjugate
unconjugated
form
lyophilized powder
capacity
~5 mg/mg, solid binding capacity (IgG)
storage temp.
−20°C
Quality Level
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.
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
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.
Physical form
Lyophilized from water.
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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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
Purification and some properties of streptococcal protein G, a novel IgG-binding reagent.
Bjorck L and Kronvall G
Journal of Immunology, 133(2), 969-974 (1984)
P A Jeddi et al.
Immunology, 87(4), 654-659 (1996-04-01)
Reduced galactosylation of immunoglobulin G (IgG) is well documented in rheumatoid arthritis (RA), but the reason for this defect is still unknown. There is some evidence supporting a defect in the biosynthetic pathway, and a reduction in the level of
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
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