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Protein G Immunoprecipitation Kit

sufficient for 50 assays


Quality Level


sufficient for 50 assays

storage temp.



The kit is designed to allow maximal recovery of immunoprecipitates. It provides all the necessary reagents to perform immunoprecipitation from cell extracts of any protein to which a suitable antibody is available. Based on protein G, the kit binds to most commonly used antibodies. In addition, spin columns are provided to enable quick washes without the loss of protein G resin and thus protein yield is maximized.

Features and Benefits

  • Minimal loss of antigen-antibody bound beads during washing.
  • Minimal or no non-specific signals by increasing the stringency of the washing step.

Preparation Note

When preparing reagents, use ultrapure water (17M -cm)

Kit Components Also Available Separately

Product No.

  • S65465 M Sodium chloride solution 15 mL

  • P3296Protein G Agarose 2 mL

  • 7173610% Sodium dodecyl sulfate solution 1 mL



Signal Word


Hazard Statements

Precautionary Statements

Hazard Classifications

Eye Dam. 1 - Flam. Liq. 3 - Skin Irrit. 2

Storage Class Code

3 - Flammable liquids

Certificate of Analysis

Certificate of Origin

Patricia Workman et al.
Journal of bacteriology, 194(13), 3512-3521 (2012-05-01)
The BamA protein of Escherichia coli plays a central role in the assembly of β-barrel outer membrane proteins (OMPs). The C-terminal domain of BamA folds into an integral outer membrane β-barrel, and the N terminus forms a periplasmic polypeptide transport-associated...
Signal Transduction Protein Array Analysis Links LRRK2 to Ste20 Kinases and PKC Zeta That Modulate Neuronal Plasticity
Zach,S et al.
PLoS ONE, 5(10) (2010)
Attenuated PGI2 synthesis in obese Zucker rats
Hodnett,B et al.
American Journal of Physiology. Regulatory, Integrative and Comparative Physiology, 296(3), R715-R721 (2010)
G-protein alpha-s and -12 subunits are involved in androgen-stimulated PI3K activation and androgen receptor transactivation in prostate cancer cells
Liu,J et al.
Prostate (2011)
Drew Bennion et al.
Molecular microbiology, 77(5), 1153-1171 (2010-07-06)
BamA of Escherichia coli is an essential component of the hetero-oligomeric machinery that mediates β-barrel outer membrane protein (OMP) assembly. The C- and N-termini of BamA fold into trans-membrane β-barrel and five soluble POTRA domains respectively. Detailed characterization of BamA...

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