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539207 Protein G-Agarose

539207
  
Purchase on Sigma-Aldrich

Áttekintés

Replacement Information
Description
Overview

This product has been discontinued.





Protein G binds to the Fc portion of immnuoglobulins (Igs) from various species; useful for binding to Igs that do not react well with protein A. Can be used for antibody immunoprecipitation procedure and to purify immunoglobulins and IgG fractions. Binding capacity: approximately 17-27 mg human IgG/ml gel. Contains approximately 2.5 mg recombinant protein G/ml gel.
Catalogue Number539207
Brand Family Calbiochem®
References
ReferencesKelley, C.A., et al. 1992. J. Biol. Chem. 267, 2127.
Sano, T., et al. 1992. Science 258, 120.
Schwartz, A.L. and Ciechanover, A. 1999. Annu. Rev. Med. 50, 57.
Voges, D., et al. 1999. Annu. Rev. Biochem. 68, 1015.
Product Information
FormLiquid slurry
Formulation50% suspension in PBS, 20% ethanol, pH 7.0.
Preservative0.05% sodium azide
Applications
Adatbeállítási hiba. A pagelet <collection_feature_application_id-AB PUR> nem található.
Immunoprecipitation
Application NotesImmunoblotting (1:1000)
Biological Information
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Standard Handling
Storage +2°C to +8°C
Do not freeze Yes
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Katalógusszám GTIN
539207 0

Documentation

Protein G-Agarose Certificates of Analysis

TitleLot Number
539207

References

Hivatkozások áttekintése
Kelley, C.A., et al. 1992. J. Biol. Chem. 267, 2127.
Sano, T., et al. 1992. Science 258, 120.
Schwartz, A.L. and Ciechanover, A. 1999. Annu. Rev. Med. 50, 57.
Voges, D., et al. 1999. Annu. Rev. Biochem. 68, 1015.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision04-September-2008 RFH
ApplicationImmunoblotting (1:1000)
DescriptionProtein G binds to the Fc portion of immnuoglobulins (Igs) from various species; useful for binding to Igs that do not react well with protein A. Can be used for antibody immunoprecipitation procedure and to purify immunoglobulins and IgG fractions. Binding capacity: approximately 17-27 mg human IgG/ml gel. Contains ~2.5 mg recombinant protein G/ml gel. The particle size ranges from 45-165 µm with an average size of ~90 µm.
FormLiquid slurry
Formulation50% suspension in PBS, 20% ethanol, pH 7.0.
Recommended reaction conditions
Purification of IgG from Serum or Ascites using Protein G Agarose Preparation of Solutions: Loading buffer: 10 mM sodium phosphate, pH 7.0, 150 mM NaCl, 0.05% NaN3 Elution buffer: 500 mM acetic acid (adjust the pH to 3.0 with 0.005% NH4OH) Stripping buffer: 1 M acetic acid, pH 2.4 Column Preparation: Pack the column with protein G-agarose (3 ml of agarose per 1 ml of serum or ascites is generally sufficient). Wash with 5 volumes of loading buffer or until the pH of the eluate is 7.0. Sample Loading: Dilute the sample (serum or ascites) with 2 volumes of loading buffer or alternatively dialyze the sample against the loading buffer. Load the sample on the column at a flow rate of 0.5 ml/min. Wash with loading buffer until the absorbance of the eluate at 280 nm approaches background levels. Elution: Elute the IgG by adding the elution buffer. Immediately neutralize the pH of the eluted IgG. Regeneration and Storage: Wash the column with 5 volumes of stripping buffer. Wash with loading buffer until the pH of the eluate is 7.0. Seal the column outlet and store in the refrigerator (4°C). Note: This protocol is meant to serve as a guideline and may need to be modified for specific applications.
Preservative0.05% sodium azide
Storage +2°C to +8°C
Do Not Freeze Yes
Toxicity Standard Handling
ReferencesKelley, C.A., et al. 1992. J. Biol. Chem. 267, 2127.
Sano, T., et al. 1992. Science 258, 120.
Schwartz, A.L. and Ciechanover, A. 1999. Annu. Rev. Med. 50, 57.
Voges, D., et al. 1999. Annu. Rev. Biochem. 68, 1015.