{"product_id":"anti-vhh-affinity-magnetic-beads","title":"Anti-VHH Affinity 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-VHH Affinity Magnetic Beads – Catalog #B2026670\u003c\/h2\u003e\n\u003cp\u003eAnti-VHH Affinity Magnetic Beads (Catalog #B2026670) combine superparamagnetic particles with high-affinity antibodies targeting VHH (variable domains of heavy-chain-only antibodies). VHHs, also known as nanobodies, are single-domain antibodies (12–15 kDa) derived from camelids. They are powerful tools in research and therapeutic development due to their small size, high thermal stability, and ease of engineering. These magnetic beads facilitate rapid purification of VHH clones from selection campaigns and expression systems.\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;\"\u003eB2026670\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;\"\u003e2 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;\"\u003eSuspension\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;\"\u003eVHH nanobody purification and selection, immunoaffinity isolation of VHH-fusion proteins, extracellular vesicle capture, target-based nanobody enrichment\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;\"\u003eVHH purification, nanobody affinity beads, single-domain antibody capture, anti-VHH antibody, VHH magnetic beads, nanobody isolation, immunomagnetic separation\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\u003eVHH domains are the antigen-binding fragments derived from camelid heavy-chain-only antibodies. Unlike conventional antibodies (four chains), VHHs are single polypeptide chains (~12 kDa), offering distinct advantages: exceptional thermal stability (many VHHs retain binding above 80°C), high solubility, compact size enabling tissue penetration, and direct expression in bacteria or yeast. They are commonly selected from large libraries (\u0026gt;10¹³ clones) by phage or yeast display.\u003c\/p\u003e\n\u003cp\u003eMagnetic bead-based affinity purification is a standard method for VHH selection and enrichment. Anti-VHH antibodies recognize conserved framework regions on all VHHs, providing universal capture. The magnetic format enables rapid, hands-on-free selection: incubate the display library with target-bound to beads, wash away non-binders, and recover VHH-displaying phage or yeast cells.\u003c\/p\u003e\n\u003cp\u003eKey applications include:\u003c\/p\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003eVHH library selection against protein targets and cell-surface antigens\u003c\/li\u003e\n\u003cli\u003eImmunoaffinity purification of recombinant VHH-fusion proteins\u003c\/li\u003e\n\u003cli\u003eCapture of VHH-displaying phage during panning\u003c\/li\u003e\n\u003cli\u003eEnrichment of VHH-functionalized particles (e.g., extracellular vesicles, nanoparticles)\u003c\/li\u003e\n\u003c\/ul\u003e\n\u003ch3 style=\"margin-top:30px;\"\u003eUsage \u0026amp; Handling Guidance\u003c\/h3\u003e\n\u003cp\u003eResuspend beads gently (do not vortex) before use. For phage display selection: coat beads with antigen or target protein, add phage display library, incubate with gentle rotation, wash thoroughly with PBS + 0.05% Tween-20, and recover bound phage by elution (low pH, protease, or dissociation buffer). For protein purification: incubate beads with VHH-containing sample, wash, and elute with imidazole (if His-tagged) or low pH buffer.\u003c\/p\u003e\n\u003cul style=\"padding-left:20px;\"\u003e\n\u003cli\u003e\n\u003cstrong\u003eBinding:\u003c\/strong\u003e Room temperature to 4°C; optimize incubation time based on target concentration (typically 15 min to 2 hours).\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eWashing:\u003c\/strong\u003e Use PBS + 0.05–0.1% Tween-20 or other mild detergents to reduce non-specific binding.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eElution:\u003c\/strong\u003e Low pH (0.1 M HCl or glycine–HCl pH 2.2), 200–500 mM imidazole (for His tags), or protease cleavage depending on VHH format.\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\u003e2 mL of anti-VHH magnetic beads, ready to use\u003c\/li\u003e\n\u003cli\u003eHigh-affinity capture of VHH domains\u003c\/li\u003e\n\u003cli\u003eMagnetic separation eliminates centrifugation\u003c\/li\u003e\n\u003cli\u003eScalable for library selection or recombinant protein purification\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\u003eUniversal capture of all VHH clones from diverse libraries\u003c\/li\u003e\n\u003cli\u003eRapid, equipment-free selection enabling high-throughput campaigns\u003c\/li\u003e\n\u003cli\u003eMinimal sample loss due to magnetic handling\u003c\/li\u003e\n\u003cli\u003eSuitable for both selection and downstream purification workflows\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\u003eDo these beads work for all VHH origins?\u003c\/strong\u003e\u003cbr\u003eYes. Anti-VHH antibodies recognize conserved VHH framework regions, so they capture VHHs from alpacas, llamas, sharks, and other sources used in display libraries.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCan I use these beads for yeast display selection?\u003c\/strong\u003e\u003cbr\u003eYes. Coat the beads with antigen, add yeast-display library, incubate, wash, and recover VHH-displaying yeast cells by plating on selective medium.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eWhat is the beads' binding capacity?\u003c\/strong\u003e\u003cbr\u003eCapacity depends on VHH concentration and size. Typically, 50–100 µL of beads can capture 1–10 µg of VHH protein; optimize for your specific target.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eHow do I prevent non-specific binding?\u003c\/strong\u003e\u003cbr\u003eInclude 0.5–1% BSA or casein in binding buffer, and use 0.05–0.1% Tween-20 in wash buffers.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eCan I re-use the beads?\u003c\/strong\u003e\u003cbr\u003eAfter thorough washing and elution, beads can be regenerated and reused; however, some loss of binding capacity may occur with repeated cycles.\u003c\/li\u003e\n\u003cli\u003e\n\u003cstrong\u003eWhat is the typical recovery of VHHs?\u003c\/strong\u003e\u003cbr\u003eRecovery depends on binding conditions and elution method. Under optimized conditions, 50–90% recovery is typical for affinity-based selection.\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;\"\u003eTerzić J, Filipović L, Mitić N, Stevanović S, Krstić J, de Marco A, Courraud J, Popović M. Application of VHH-Immobilized Cryogel-Based Immunoaffinity Chromatography for Isolation of Extracellular Vesicles. \u003cem\u003eMolecules.\u003c\/em\u003e 2025;30(22).\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.3390\/molecules30224337\" 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;\"\u003eFilipović L, Spasojević M, Prodanović R, Korać A, Matijaševic S, Brajušković G, de Marco A, Popović M. Affinity-based isolation of extracellular vesicles by means of single-domain antibodies bound to macroporous methacrylate-based copolymer. \u003cem\u003eN Biotechnol.\u003c\/em\u003e 2022;69:36-48.\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1016\/j.nbt.2022.03.001\" 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;\"\u003eZhu M, Gong X, Hu Y, Ou W, Wan Y. Streptavidin-biotin-based directional double Nanobody sandwich ELISA for clinical rapid and sensitive detection of influenza H5N1. \u003cem\u003eJ Transl Med.\u003c\/em\u003e 2014;12:352.\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1186\/s12967-014-0352-5\" 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;\"\u003eZanker AA, Stargardt P, Kurzbach SC, Turrina C, Mairhofer J, Schwaminger SP, Berensmeier S. Direct capture and selective elution of a secreted polyglutamate-tagged nanobody using bare magnetic nanoparticles. \u003cem\u003eBiotechnol J.\u003c\/em\u003e 2022;17(5):e2100577.\u003c\/span\u003e\u003ca href=\"https:\/\/doi.org\/10.1002\/biot.202100577\" 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":52809017295146,"sku":"BTS-B2026670","price":1055.0,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0896\/1579\/4474\/files\/B2026670.png?v=1790859400","url":"https:\/\/bluetigerscientific.com\/products\/anti-vhh-affinity-magnetic-beads","provider":"Blue Tiger Scientific","version":"1.0","type":"link"}