Protein a agarose

Manufactured by GoldBio

Protein A agarose is a lab equipment product that is used for the purification and isolation of antibodies from biological samples. It consists of agarose beads that have been coupled with Protein A, a bacterial protein that binds to the Fc region of immunoglobulins. The Protein A agarose allows for the selective capture and recovery of antibodies from complex mixtures, such as cell culture supernatants or serum samples.

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Lab products found in correlation

Expi293f cells, by Thermo Fisher Scientific (2 mentions) Protein g agarose, by Thermo Fisher Scientific (1 mentions) Anti igm agarose, by Merck Group (1 mentions)

Spelling variants of this product

Protein A agarose resin (14 citations) Agarose (3 citations) Protein A agarose chromatography (2 citations)

3 protocols using protein a agarose

Cloning and expression of recombinant antibodies

Cited 1 time

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Antibodies were cloned as described previously (46 (link)). Briefly, VH, Vκ, and Vλ genes were amplified by reverse transcription-PCR and nested PCR reactions from singly sorted GC B cells using primer combinations specific for IgG, IgM/A, Igκ, and Igλ from previously described primer sets (47 (link)) and then sequenced. To generate recombinant mAbs, restriction sites were incorporated via PCR with primers to the corresponding heavy and light chain V and J genes. The amplified VH, Vκ, and Vλ genes were cloned into IgG1, Igκ, and Igλ expression vectors, respectively, as described previously (47 (link)–49 ). Heavy and light chain plasmids were co-transfected into Expi293F cells (Gibco) for expression, and mAbs were purified with protein A agarose (GoldBio).

Schmitz A.J., Turner J.S., Liu Z., Aziati I.D., Chen R.E., Joshi A., Bricker T.L., Darling T.L., Adelsberg D.C., Alsoussi W.B., Case J.B., Lei T., Thapa M., Amanat F., O’Halloran J.A., Shi P.Y., Presti R.M., Krammer F., Bajic G., Whelan S.P., Diamond M.S., Boon A.C, & Ellebedy A.H. (2021). A public vaccine-induced human antibody protects against SARS-CoV-2 and emerging variants. bioRxiv.

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Production of Anti-CLEC7A Monoclonal Antibody

Cited 2 times

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Anti-mouse CLEC7A monoclonal antibody (mAb) 2A11 was previously reported (Brown et al., 2002 (link)). A DNA fragment encoding heavy chain variable (VH) and CH1 regions was cloned into the pFUSEmIgG2A-Fc1 vector with L234A, L235A, P329G (LALA-PG) mutation, which blocks Fc binding. A DNA fragment encoding the light chain was cloned into Fc-null pFUSE-mIgG2A-Fc1 vector as previously described (Molgora et al., 2020 (link)). The heavy chain and light chain plasmids were co-transfected into Expi293F cells (Thermo Fisher Scientific) for expression at mass ratio 1:2. When cell viability was below 50% (5–7 days), the supernatant was collected and filtered with 0.22-μm filters. The antibody was purified with protein A agarose (GoldBio). Final preps were concentrated to about 10 mg/mL into PBS and stored in 80°C for future use.

Wang S., Sudan R., Peng V., Zhou Y., Du S., Yuede C.M., Lei T., Hou J., Cai Z., Cella M., Nguyen K., Poliani P.L., Beatty W.L., Chen Y., Cao S., Lin K., Rodrigues C., Ellebedy A.H., Gilfillan S., Brown G.D., Holtzman D.M., Brioschi S, & Colonna M. (2022). TREM2 Drives Microglia Response to Amyloid-β via SYK-dependent and -independent Paths. Cell, 185(22), 4153-4169.e19.

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Antibody Depletion from Plasma

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WP and HIP were mixed with Protein A-agarose (GoldBio), Protein G-agarose (Invitrogen), and anti-IgM-agarose (Sigma, A9935) at an approximate ratio of 1 volume of plasma to 1 volume of packed beads. The mixtures were rotated for 1 hour, pelleted by centrifugation and depleted supernatants removed from the bead pellet.

Wheeler E.A., Lenhart-Pendergrass P.M., Rysavy N.M., Poch K., Caceres S., Calhoun K.M., Serban K., Nick J.A, & Malcolm K.C. (2023). Divergent host innate immune response to the smooth-to-rough M. abscessus adaptation to chronic infection. bioRxiv.

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