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Protein G Agarose

>98% (HPLC and SDS-PAGE), suspension

protein g, agarose


>98% (HPLC and SDS-PAGE)




pkg of 15 mL (05015952001 [settled resin volume])
pkg of 2 mL (11719416001 [settled resin volume])
pkg of 5 mL (11243233001 [settled resin volume])



shipped in

wet ice

storage temp.


General description

Protein G was initially isolated from G148, a human group G Streptococcal strain. It is a cell wall protein and shows high affinity to IgG (immunoglobulin G). It has a putative molecular weight of 30,000Da. It interacts with all subclasses of human IgG and also binds to mouse, rabbit and goat IgG.


Protein G is a cell wall protein, isolated from a specific bacterial strain, which has specific binding sites for certain classes of immunoglobulins from different species. Protein G binds nearly all subclasses of IgG, but no other classes of immunoglobulins.
Binding capacity: 20mg human IgG (polyclonal)/ml (the IgG is loaded at pH 7.0, and eluted with 200mM glycine, pH 2.8)
Structure: recombinant Protein G (E. coli, Mr = 22,000) is covalently coupled to crosslinked 4% agarose beads: 2.5mg Protein G (>98% pure)/1ml gel.


Affinity chromatography using Protein G Agarose, like Protein A Agarose, is the method of choice for purification of IgG from many species. It has been used as a pre-clearing agent during-
  • Ubiquitination assay
  • Immunoprecipitation

Features and Benefits

Preswollen gel, ready-to-use, 2ml or 5ml gel (settled gel volume) in buffer that contains 14-19% ethanol as a preservative, nonsterile.
Protein G content: 2.5mg/ml preswollen gel


Purity: >98% (HPLC, SDS-PAGE); entirely free from staphylococcal enterotoxins.

Other Notes

For life science research only. Not for use in diagnostic procedures.


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Hazard Statements

Hazard Classifications

Eye Irrit. 2 - Flam. Liq. 3

Storage Class Code

3 - Flammable liquids



Flash Point(F)

102.2 °F

Flash Point(C)

39 °C

Certificate of Analysis

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Certificate of Origin

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Product Information Sheet

Quotes and Ordering

T-H Kim et al.
Cell death & disease, 5, e1527-e1527 (2014-11-21)
Understanding the molecular networks that regulate adipogenesis is crucial for combating obesity. However, the identity and molecular actions of negative regulators that regulate the early development of adipocytes remain poorly understood. In this study, we investigated the role of CREB3L4
Jakob Triebel et al.
European journal of endocrinology, 161(2), 345-353 (2009-05-30)
In vitro experiments and in vivo studies on rodents demonstrate that N-terminal 14, 15, 16, 17, and 18 kDa fragments prolactin-related vasoinhibin (PRL-V) of human PRL are natural inhibitors of neovascularization in the retina and elsewhere. These N-terminal PRL fragments
R Travis Taylor et al.
Methods (San Diego, Calif.), 55(2), 166-171 (2011-08-23)
Ubiquitin (Ub) conjugation to a substrate protein is a widely used cellular mechanism for control of protein stability and function, modulation of signal transduction pathways and antiviral responses. Identification and characterization of ubiquitinated viral proteins is an important step in
L Björck et al.
Journal of immunology (Baltimore, Md. : 1950), 133(2), 969-974 (1984-08-01)
Protein G, a bacterial cell wall protein with affinity for immunoglobulin G (IgG), has been isolated from a human group G streptococcal strain (G148). Bacterial surface proteins were solubilized by enzymatic digestion with papain. Protein G was isolated by sequential

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