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You are here:Home » Antibodies » Abs to Protein G » Anti -Protein G (Immunoglobulin G Binding Protein G [Precursor], IgG Binding Protein G, spg) (Biotin)

Anti -Protein G (Immunoglobulin G Binding Protein G [Precursor], IgG Binding Protein G,
spg) (Biotin)

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Specifications

Clone Host Grade Applications
Polyclonal Chicken Affinity Purified E B
Protein G is a bacterial protein derived from the cell wall of certain strains of b-hemolytic Streptococcci. It binds with high affinity to the Fc portion of various classes and subclasses of immunoglobulins from a variety of species. Protein G binds to all IgG subclasses from human, mouse and rat species. It also binds to total IgG from guinea pig, rabbit, goat, cow, sheep, and horse. Protein G binds preferentially to the Fc portion of IgG, but unlike Protein A can also bind to the Fab region, making it useful for purification of F(ab') fragments of IgG. Due to it's affinity for the Fc region of many mammalian immunoglobulins, protein G is considered a universal reagent in biochemistry and immunology.
Catalog #P9102-57M
ApplicationsSuitable for use in ELISA and Western Blot. Other applications not tested.
Recommended DilutionsELISA: 1:5000-1:40,000
Western Blot: 1:1000-1:10,000
Optimal dilutions to be determined by the researcher.
Storage and StabilityMay be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Clone TypePolyclonal
IsotypeIgY
HostChicken
Concentration~1mg/ml
FormSupplied as a liquid in PBS, pH 7.2, 0.2% BSA, 0.1% sodium azide. Labeled with Biotin.
PurityPurified by Protein G affinity chromatography.
ImmunogenPurified recombinant Protein G
SpecificityRecognizes Protein G.
Important NoteThis product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.


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