{"product_id":"anti-ha-nanobody-magnetic-beads","title":"Anti-HA 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-HA Nanobody Magnetic Beads – Catalog #B2025479\u003c\/h2\u003e\n\u003cp\u003eAnti-HA Nanobody Magnetic Beads (Catalog #B2025479) are laboratory tools for high-affinity isolation of HA-tagged recombinant proteins. The beads are coated with nanobodies—small (~15 kDa), camelid-derived antibody fragments—that recognize the HA epitope with picomolar to nanomolar affinity. Supplied as 0.1 mL in solution, they enable one-step, magnetic bead-based separation of HA fusion proteins from complex protein mixtures, providing superior specificity and binding kinetics compared to conventional monoclonal antibodies.\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;\"\u003eB2025479\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\u003eMolecular Weight or Concentration:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eN\/A\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\u003eTarget epitope:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eHA tag (YPYDVPDYA; hemagglutinin from influenza)\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 type:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eCamelid-derived single-domain antibody fragment\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\u003eBead properties:\u003c\/strong\u003e\u003c\/td\u003e\n\u003ctd style=\"padding:6px 0;\"\u003eMagnetic, used with magnetic separation racks\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;\"\u003eAffinity purification of HA-tagged proteins, co-immunoprecipitation, protein-protein interaction studies, protein complex isolation, mass spectrometry sample preparation\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-HA nanobody, HA-tag nanobody, HA affinity beads, nanobody-based purification, HA epitope tag, nanobody magnetic beads, high-affinity HA purification\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 um.\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 antibodies) are emerging as powerful tools for protein affinity purification and detection. Compared to conventional monoclonal antibodies (~150 kDa), nanobodies are one-tenth the size (~15 kDa), more thermodynamically stable, often exhibit superior specificity, and are frequently found to bind their epitopes with picomolar to nanomolar affinity. These properties make nanobodies especially valuable for sensitive isolation of HA-tagged proteins and for studying transient or weak protein-protein interactions where minimal perturbation is required.\u003c\/p\u003e\n\u003cp\u003eThe HA epitope (YPYDVPDYA) from influenza hemagglutinin is a standard small tag in molecular biology. Anti-HA nanobodies recognize this epitope with extremely high affinity while minimizing non-specific interactions with other cellular or bacterial proteins. When immobilized on magnetic beads, anti-HA nanobodies provide rapid, one-step purification with the added benefits of nanobody-derived affinity and the convenience of magnetic separation.\u003c\/p\u003e\n\u003cp\u003eKey applications include:\u003c\/p\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003eUltra-high-affinity isolation of HA-tagged proteins from complex lysates\u003c\/li\u003e\n\u003cli\u003eCo-immunoprecipitation of transient or weak protein-protein interaction partners\u003c\/li\u003e\n\u003cli\u003eEnrichment of HA-tagged proteins for mass spectrometry\u003c\/li\u003e\n\u003cli\u003eStructural biology workflows requiring minimal sample perturbation\u003c\/li\u003e\n\u003cli\u003ePurification of native protein complexes while preserving interactions\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch3 style=\"margin-top:30px;\"\u003eUsage \u0026amp; Handling Guidance\u003c\/h3\u003e\n\u003cp\u003eThese beads are supplied as a suspension. Gently mix before each use; avoid vortexing. Add the beads directly to your lysate or protein mixture and incubate at 4°C for 15–30 minutes to allow binding (the high affinity of nanobodies often shortens incubation time compared to conventional antibodies). Place the tube in a magnetic rack for 1–2 minutes to pellet the beads, then remove the supernatant and wash 3–5 times with binding buffer or PBS.\u003c\/p\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003e\n\u003cstrong\u003eBinding buffer:\u003c\/strong\u003e PBS, TBS, or your native lysis buffer is suitable. Standard lysis buffers with protease inhibitors work well.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eIncubation:\u003c\/strong\u003e 15–30 minutes at 4°C. Shorter incubation times (compared to monoclonal antibody beads) are often sufficient because of the high affinity of nanobodies.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eWashing:\u003c\/strong\u003e Perform 3–5 washes with 10–15 bead volumes of binding buffer per wash. The high specificity of nanobodies typically results in lower background.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eElution:\u003c\/strong\u003e Elute with low pH buffer (0.1 M glycine, pH 2.8–3.0) or denaturing conditions (6 M urea, 8 M guanidinium chloride).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eMagnetic separation:\u003c\/strong\u003e Use a commercial magnetic rack for 1.5 or 2 mL tubes.\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-HA nanobody magnetic beads in solution\u003c\/li\u003e\n\u003cli\u003eReady-to-use beads for rapid, high-affinity protein purification\u003c\/li\u003e\n\u003cli\u003ePicomolar-to-nanomolar affinity camelid nanobodies\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\u003eNanobodies offer picomolar-to-nanomolar affinity and superior specificity\u003c\/li\u003e\n\u003cli\u003eSmall size (~15 kDa) minimizes steric hindrance and preserves protein interactions\u003c\/li\u003e\n\u003cli\u003eFaster binding kinetics typically shorten purification protocols\u003c\/li\u003e\n\u003cli\u003eExcellent for isolating transient or weak protein complexes\u003c\/li\u003e\n\u003cli\u003eCompatible with downstream mass spectrometry and structural biology methods\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 the affinity of the anti-HA nanobody?\u003c\/strong\u003e\u003cbr\u003eCamelid-derived anti-HA nanobodies typically exhibit Kd values in the picomolar to low-nanomolar range. Request a COA\/TDS for lot-specific affinity data.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eHow do nanobodies compare to conventional monoclonal antibodies?\u003c\/strong\u003e\u003cbr\u003eNanobodies are ~15 kDa versus ~150 kDa for full antibodies, often bind with higher affinity (picomolar to nanomolar), are more stable, and can access epitopes in protein cavities. However, some applications may benefit from the avidity effects of bivalent antibodies.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCan I use shorter incubation times with nanobody beads?\u003c\/strong\u003e\u003cbr\u003eYes. The high affinity and binding kinetics of nanobodies often allow efficient capture in 15–30 minutes, compared to 30–60 minutes for conventional antibody beads.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eAre these beads suitable for structural biology applications?\u003c\/strong\u003e\u003cbr\u003eYes. The small size of nanobodies and their ability to preserve native protein-protein interactions make them well-suited for protein complex purification prior to electron microscopy or crystallography.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eHow do I know if my HA-tagged protein is compatible?\u003c\/strong\u003e\u003cbr\u003eAny protein bearing an N-terminal, C-terminal, or internal HA epitope (YPYDVPDYA) should bind these nanobodies. The accessibility of the epitope in your particular fusion protein may vary; test with a small amount of lysate first.\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;\"\u003eGötzke H, Kilisch M, Martínez-Carranza M, Sograte-Idrissi S, Rajavel A, Schlichthaerle T, Engels N, Jungmann R, Stenmark P, Opazo F, Frey S. The ALFA-tag is a highly versatile tool for nanobody-based bioscience applications. \u003cem\u003eNat Commun.\u003c\/em\u003e 2019;10(1):4403.\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1038\/s41467-019-12301-7\" 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;\"\u003eChen ZS, Huang HC, Wang X, Schön K, Jia Y, Lebens M, Besavilla DF, Murti JR, Ji Y, Sarshad AA, Deng G, Zhu Q, Angeletti D. Influenza A Virus H7 nanobody recognizes a conserved immunodominant epitope on hemagglutinin head and confers heterosubtypic protection. \u003cem\u003eNat Commun.\u003c\/em\u003e 2025;16(1):432.\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1038\/s41467-024-55193-y\" 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":52805760713002,"sku":"BTS-B2025479","price":1205.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/B2025479.png?v=1790801850","url":"https:\/\/bluetigerscientific.com\/products\/anti-ha-nanobody-magnetic-beads","provider":"Blue Tiger Scientific","version":"1.0","type":"link"}