P4689
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
Productos recomendados
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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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
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