{"product_id":"anti-flag-nanobody-magnetic-beads","title":"Anti-Flag Nanobody Magnetic Beads","description":"\u003cdiv style=\"max-width:1400px; margin:0 auto; padding:40px 20px; font-family:'Open Sans',sans-serif; font-weight:300; background:#fff; color:#333; font-size:0.95rem; box-sizing:border-box;\"\u003e\n  \u003cdiv style=\"display:flex; flex-direction:column; gap:20px;\"\u003e\n\u003ch2 style=\"margin:0; font-weight:600;\"\u003eAnti-Flag Nanobody Magnetic Beads – Catalog #B2025502\u003c\/h2\u003e\n\u003cp\u003eAnti-Flag nanobody magnetic beads (Catalog #B2025502) are superparamagnetic particles covalently conjugated with nanobodies (VHH single-domain antibodies) derived from camelids (llama or alpaca) that recognize the FLAG epitope with high affinity and specificity. Supplied as 0.1 mL of suspension, these beads enable rapid, one-step capture and purification of FLAG-tagged proteins with minimal steric hindrance and excellent performance in structural and biochemical studies. The small size of nanobodies (~15 kDa) compared to conventional antibodies (~150 kDa) reduces the bead coating density while maintaining high binding capacity, allowing improved access to the FLAG epitope even when proteins are part of large complexes.\u003c\/p\u003e\n\u003cdiv style=\"overflow-x:auto; max-width:100%; margin-bottom:20px;\"\u003e\n\u003ctable style=\"width:100%; max-width:640px; border-collapse:collapse;\"\u003e\n\u003ctbody\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eCatalog number:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eB2025502\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eLot number:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eBatch dependent\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eExpiration Date:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eBatch dependent\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eAmount:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003e0.1 mL\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eSupplied as:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eSolution\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eNanobody source:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eCamelid-derived VHH (single-domain antibody)\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eTarget epitope:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eFLAG tag\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eApplications:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eFLAG-tagged protein purification, co-immunoprecipitation, immunopull-down from native complexes, cryo-EM sample preparation, structural biology, functional binding assays\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eStorage:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003e2–8°C\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eKeywords:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eAnti-FLAG nanobody, VHH antibody beads, camelid antibody, single-domain antibody, FLAG-tag nanobody, magnetic nanobody beads, immunoprecipitation with nanobody\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003ctr style=\"border-bottom:1px solid #ddd;\"\u003e\n\u003ctd style=\"width:150px; padding:6px 10px 6px 0; vertical-align:top;\"\u003e\u003cstrong\u003eGrade:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eBiotechnology grade. All products are highly pure. All solutions are made with Type I ultrapure water (resistivity \u0026gt;18 MΩ-cm) and are filtered through 0.22 µm.\u003c\/td\u003e\n\u003c\/tr\u003e\n\u003c\/tbody\u003e\n\u003c\/table\u003e\n\u003c\/div\u003e\n\u003ch3 style=\"margin-top:30px;\"\u003eScientific Overview\u003c\/h3\u003e\n\u003cp\u003eNanobodies (variable domains of camelid heavy-chain-only antibodies, also called VHH) are single-domain antibodies approximately 15 kDa in size. They offer distinct advantages over conventional antibodies in many applications: small size improves tissue penetration and allows conjugation at higher density on solid supports; high thermostability enables use under harsh conditions; and flexibility in binding cleft accommodates larger epitopes with high affinity. These properties have made nanobodies the antibodies of choice for cryo-electron microscopy, intracellular immunofluorescence, and functional studies where steric interference must be minimized.\u003c\/p\u003e\n\u003cp\u003eWhen coated onto magnetic beads, anti-FLAG nanobodies provide selective, high-affinity capture of FLAG-epitope-containing proteins. Because nanobodies are significantly smaller than conventional antibodies, the same bead surface can be functionalized at higher density, potentially increasing overall binding capacity. Additionally, the smaller size means less spatial interference: when isolating protein complexes or capturing proteins in native conformations, the minimal antibody footprint preserves protein–protein interactions and structural integrity.\u003c\/p\u003e\n\u003cp\u003eKey applications include:\u003c\/p\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003eRapid, high-efficiency isolation of FLAG-tagged proteins from cell lysates\u003c\/li\u003e\n\u003cli\u003eImmunopull-down of native macromolecular complexes\u003c\/li\u003e\n\u003cli\u003eCo-immunoprecipitation with minimal steric hindrance\u003c\/li\u003e\n\u003cli\u003eSample preparation for cryo-EM and structural biology studies\u003c\/li\u003e\n\u003cli\u003eFunctional assays requiring native protein conformation\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch3 style=\"margin-top:30px;\"\u003eUsage \u0026amp; Handling Guidance\u003c\/h3\u003e\n\u003cp\u003eStore at 2–8°C. Mix gently before use (do not vortex). Incubate beads with sample (typically 5–20 µL of bead suspension per mL of lysate) at 4°C for 30 minutes to 1 hour with gentle rotation, or at room temperature for 10–20 minutes with mixing. Use a magnetic rack to immobilize beads, then carefully remove the supernatant. Wash beads 2–3 times in appropriate buffer (PBS, Tris-HCl, or HEPES, pH 7.0–8.0). Elute with acidic buffer (0.1 M glycine–HCl, pH 2.8), neutral salt buffer (1 M NaCl), or FLAG peptide competitor (10–100 µg\/mL DYKDDDDK in PBS). Neutralize acidic eluates immediately.\u003c\/p\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003e\n\u003cstrong\u003eIncubation optimization:\u003c\/strong\u003e Shorter incubation times (10–20 min) with nanobodies can sometimes achieve similar binding to longer incubations with conventional antibodies due to high nanobody affinity.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eNative complex preservation:\u003c\/strong\u003e For co-IP of native complexes, use gentler buffers (0.2–0.5% Triton X-100 or 0.1% NP-40) and minimize washing stringency.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eElution method:\u003c\/strong\u003e Competitive elution with FLAG peptide is gentlest for downstream functional assays; acidic elution is faster and more efficient for structural studies.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eReusability:\u003c\/strong\u003e Regenerate beads by washing thoroughly with neutral then acidic buffer if reuse is necessary, but test efficiency with a new sample first.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch3 style=\"margin-top:30px;\"\u003eWhat You Get\u003c\/h3\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003e0.1 mL of anti-FLAG nanobody magnetic bead suspension\u003c\/li\u003e\n\u003cli\u003eHighly specific, high-affinity single-domain antibody reagent\u003c\/li\u003e\n\u003cli\u003eReady-to-use for immunoprecipitation and protein isolation\u003c\/li\u003e\n\u003cli\u003eMinimal steric hindrance for native complex studies\u003c\/li\u003e\n\u003cli\u003eFor research use only (RUO)\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch3 style=\"margin-top:30px;\"\u003eWhy Researchers Choose It\u003c\/h3\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003eNanobody-based design provides exceptional affinity and specificity with minimal steric effects\u003c\/li\u003e\n\u003cli\u003eSmall size enables access to FLAG epitopes in large protein complexes\u003c\/li\u003e\n\u003cli\u003eHigh thermostability supports use under challenging buffer conditions\u003c\/li\u003e\n\u003cli\u003eMagnetic separation is faster and gentler than conventional methods\u003c\/li\u003e\n\u003cli\u003eIdeal for cryo-EM, structural biology, and functional studies requiring native conformations\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch3 style=\"margin-top:30px;\"\u003eFrequently Asked Questions (FAQ)\u003c\/h3\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003e\n\u003cstrong\u003eWhat is a nanobody?\u003c\/strong\u003e\u003cbr\u003eA nanobody is a single-domain antibody (~15 kDa) derived from camelids (llama, alpaca) that can bind antigens with high affinity and specificity. Nanobodies are significantly smaller than conventional antibodies (~150 kDa), making them ideal for applications where small size is beneficial.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eHow do these beads differ from conventional anti-FLAG beads?\u003c\/strong\u003e\u003cbr\u003eNanobody-coated beads have lower steric hindrance due to the small size of VHH domains. This is especially advantageous for co-immunoprecipitation of native complexes and cryo-EM sample preparation, where antibody size can interfere with protein–protein interactions or sample preparation.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eWhat elution method should I use?\u003c\/strong\u003e\u003cbr\u003eAcid elution (glycine–HCl, pH 2.8) is fastest and most efficient. For applications requiring native proteins, use competitive elution with FLAG peptide or neutral high-salt buffer (1 M NaCl). Test your target protein's stability under each condition.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCan nanobodies handle harsh pH or temperature?\u003c\/strong\u003e\u003cbr\u003eNanobodies are more thermostable than conventional antibodies. They can typically tolerate pH 2–10 and temperatures up to 70°C, but we recommend confirmatory testing with your specific sample.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eIs the small package size (0.1 mL) sufficient for my experiments?\u003c\/strong\u003e\u003cbr\u003e0.1 mL of magnetic bead suspension is typically sufficient for 5–10 typical immunoprecipitation experiments. Contact us for larger quantities if needed.\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003cdiv style=\"margin-top:20px; font-weight:bold; color:#c8102e;\"\u003eThis product is for Research Use Only (RUO). It is not intended for diagnostic or therapeutic use in humans or animals.\u003c\/div\u003e\n\u003chr\u003e\n\u003ch4\u003eReferences\u003c\/h4\u003e\n\u003cul style=\"padding-left:0; margin:0; list-style:none;\"\u003e\n\u003cli style=\"display:flex; justify-content:space-between; align-items:flex-start; gap:12px; padding:8px 0; border-bottom:1px solid #eee;\"\u003e\n\u003cspan style=\"flex:1;\"\u003eMuyldermans S. Nanobodies: natural single-domain antibodies. \u003cem\u003eAnnu Rev Biochem.\u003c\/em\u003e 2013;82:775-97.\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1146\/annurev-biochem-063011-092449\" target=\"_blank\" rel=\"noopener\" style=\"flex-shrink:0; margin-top:2px;\"\u003e\u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height:28px; width:auto;\"\u003e\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli style=\"display:flex; justify-content:space-between; align-items:flex-start; gap:12px; padding:8px 0; border-bottom:1px solid #eee;\"\u003e\n\u003cspan style=\"flex:1;\"\u003eFridy PC, Li Y, Keegan S, Thompson MK, Nudelman I, Scheid JF, Oeffinger M, Nussenzweig MC, Fenyö D, Chait BT, Rout MP. A robust pipeline for rapid production of versatile nanobody repertoires. \u003cem\u003eNat Methods.\u003c\/em\u003e 2014;11(12):1253-60.\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1038\/nmeth.3170\" target=\"_blank\" rel=\"noopener\" style=\"flex-shrink:0; margin-top:2px;\"\u003e\u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height:28px; width:auto;\"\u003e\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli style=\"display:flex; justify-content:space-between; align-items:flex-start; gap:12px; padding:8px 0; border-bottom:1px solid #eee;\"\u003e\n\u003cspan style=\"flex:1;\"\u003eMcMahon C, Baier AS, Pascolutti R, Wegrecki M, Zheng S, Ong JX, Erlandson SC, Hilger D, Rasmussen SGF, Ring AM, Manglik A, Kruse AC. Yeast surface display platform for rapid discovery of conformationally selective nanobodies. \u003cem\u003eNat Struct Mol Biol.\u003c\/em\u003e 2018;25(3):289-296.\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1038\/s41594-018-0028-6\" target=\"_blank\" rel=\"noopener\" style=\"flex-shrink:0; margin-top:2px;\"\u003e\u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height:28px; width:auto;\"\u003e\u003c\/a\u003e\n\u003c\/li\u003e\n\u003cli style=\"display:flex; justify-content:space-between; align-items:flex-start; gap:12px; padding:8px 0; border-bottom:1px solid #eee;\"\u003e\n\u003cspan style=\"flex:1;\"\u003eSchotte L, Rombaut B, Thys B. A liquid phase affinity capture assay using magnetic beads to study protein-protein interaction: the poliovirus-nanobody example. \u003cem\u003eJ Vis Exp.\u003c\/em\u003e 2012;(63).\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.3791\/3937\" target=\"_blank\" rel=\"noopener\" style=\"flex-shrink:0; margin-top:2px;\"\u003e\u003cimg src=\"https:\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/Reference.png?v=1775409336\" alt=\"Reference\" style=\"height:28px; width:auto;\"\u003e\u003c\/a\u003e\n\u003c\/li\u003e\n\u003c\/ul\u003e\n  \u003c\/div\u003e\n\u003c\/div\u003e","brand":"Molecular Depot","offers":[{"title":"Default Title","offer_id":52805763039530,"sku":"BTS-B2025502","price":1235.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/B2025502.png?v=1790801873","url":"https:\/\/bluetigerscientific.com\/products\/anti-flag-nanobody-magnetic-beads","provider":"Blue Tiger Scientific","version":"1.0","type":"link"}