Sepharose a g beads

Manufactured by Thermo Fisher Scientific

Sourced in United States

Sepharose A/G beads are a type of agarose-based resin used for protein purification. They are designed to selectively bind immunoglobulins (Ig) and other proteins that interact with protein A or protein G. The beads provide a versatile platform for affinity-based separation and enrichment of target proteins from complex biological samples.

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Lab products found in correlation

R960 25, by Thermo Fisher Scientific (1 mentions) Amicon spin column, by Merck Group (1 mentions) Silverquest kit, by Thermo Fisher Scientific (1 mentions) Anti flag m2 antibody, by Merck Group (1 mentions)

Spelling variants of this product

Sepharose beads (8 citations) Sepharose G beads (6 citations)

2 protocols using sepharose a g beads

Identification of MERS-CoV S1-Interacting Host Proteins

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Membrane proteins from
pcDNA–MERS-CoV–S1–V5–transfected BEAS2B cells were
immunoprecipitated with mAb against V5 (ThermoFisher Scientific, R96025) and
Sepharose A/G beads (ThermoFisher Scientific). In parallel, the membrane
proteins from the BEAS2B cells were immunoprecipitated with purified
MERS-CoV–S1–FLAG protein, anti-FLAG M2 antibody (Sigma, F1804),
and Sepharose A/G beads (ThermoFisher Scientific). Pulled down proteins reactive
to anti-V5 beads were washed and incubated with 0.1 m glycine, pH 3.5,
and those reactive to anti-FLAG M2 beads were eluted in 3× FLAG peptide
solution (Sigma, 150 ng/μl final concentration). Eluted samples were
spin-dialyzed in Amicon spin column with 10-kDa cutoff (Millipore) and separated
by SDS-PAGE, stained with SilverQuest kit (ThermoFisher Scientific). The gel
fragment was excised for LC-MS/MS analysis carried out in the Center for Genomic
Sciences, University of Hong Kong. MS/MS data were searched against all
mammalian protein databases in NCBI and Swiss-Prot. The protein was identified
as GRP78 with significant hits over different domains of the sequence.

Chu H., Chan C.M., Zhang X., Wang Y., Yuan S., Zhou J., Au-Yeung R.K., Sze K.H., Yang D., Shuai H., Hou Y., Li C., Zhao X., Poon V.K., Leung S.P., Yeung M.L., Yan J., Lu G., Jin D.Y., Gao G.F., Chan J.F, & Yuen K.Y. (2018). Middle East respiratory syndrome coronavirus and bat coronavirus HKU9 both can utilize GRP78 for attachment onto host cells. The Journal of Biological Chemistry, 293(30), 11709-11726.

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Characterization of FADD Protein Interactions

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To characterize the binding of purified and/or TAT-conjugated FADD to partner proteins, recombinant His-tagged FADD (1 μg) was initially immunoprecipitated with anti-His (3 μg) and Sepharose A/G beads (Thermofisher Scientific, Waltham, MA, USA) in NP-40 buffer (20 mM Tris-HCl, pH 7.4, containing 150 mM NaCl, 0.2% (vol/vol) NP-40, 10% (wt/vol) glycerol, and complete protease-inhibitor ‘cocktail’). The protein-beads complexes were washed with binding buffer, followed by incubation with total cell lysates from HCT 116 (1 μg) overnight at 4 °C. The protein complex was eluted in SDS-PAGE sample buffer (62.5 mM Tris-HCl, pH 6.8, 10% (wt/vol) glycerol, 2% (wt/vol) SDS, 0.7 M β-mercaptoethanol, and 0.001% (wt/vol) bromophenol blue) and analyzed by Western blot.

Ranjan K., Waghela B.N., Vaidya F.U, & Pathak C. (2020). Cell-Penetrable Peptide-Conjugated FADD Induces Apoptosis and Regulates Inflammatory Signaling in Cancer Cells. International Journal of Molecular Sciences, 21(18), 6890.

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