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Affinity Binding & Capture Oligonucleotides

Robust pull‑down, surface immobilization, and immuno‑detection using affinity‑tagged oligonucleotides: biotin↔streptavidin, DIG/DNP/FITC↔antibody, His‑mimic↔Ni‑NTA, and more. Custom design, synthesis, purification/QC, and documentation.

Biotin ↔ Streptavidin DIG / DNP / FITC Ni‑NTA ↔ His Thiol • Amino • Click Antibody / Protein A/G RUO → GMP‑like
Overview Products Get Started Workflow FAQ Speak to a Scientist References

Overview

Bio‑Synthesis delivers end‑to‑end Affinity Binding & Capture solutions — from application‑led design (tag choice, linker/spacer, surface geometry) to custom synthesis, purification (desalt/HPLC/PAGE), and QC (UPLC/HPLC, LC‑MS, optional endotoxin/bioburden) with ISO‑aligned documentation. We support biotin/avidin, DIG/DNP/FITC hapten–antibody, His‑tag/Ni‑NTA, thiol/maleimide–gold, amino/NHS coupling, aldehyde/hydrazide/click, thioctic/lipoic SAMs, antibody & Protein A/G, aptamer handles, and metal‑chelator tags at RUO → GMP‑like scales in Lewisville, TX.

Formats
Tubes • Beads • Plates
Scale
µmol → multi‑gram
QC
UPLC/HPLC • LC‑MS •
Binding
Supply
RUO → GMP‑like
What we manufacture
  • Biotin systems: 5′/3′‑Biotin, Biotin‑TEG, internal Biotin‑dT, desthiobiotin, PEG/C18 spacers.
  • Hapten tags: DIG, DNP, FITC/FAM with antibody partners.
  • Ni‑NTA/His: His₆ peptides, NTA modifiers for reversible capture.
  • Reactive chemistries: Thiol/maleimide, amino/NHS, aldehyde/hydrazide, azide/alkyne click.
  • Surface handles: Thioctic/lipoic/dithiolane for SAMs; gold/electrode attachment.
  • Protein & aptamer conjugates: Antibody/Protein A/G; sequence‑selected aptamers.
  • Metal chelators & peptides: NTA/DTPA/DOTA/NOTA; RGD, Strep‑Tag II, Twin‑Strep, FLAG, HA.
Services you can expect
  • Application‑led design: tag choice, linker length, surface geometry.
  • Process & purification: desalt/HPLC/PAGE, controlled drying/storage.
  • Documentation: ISO‑aligned CoA, sequence map, capture/elution guidance.
  • Scale‑up & transfer: RUO → GMP‑like with phased tech transfer.
Biotin–Streptavidin complex illustration
Biotin–Streptavidin Binding Complex (illustrative)

Products

System Function Common Modifications Applications
Biotin–Streptavidin / Avidin Strongest non‑covalent pair (Kd ≈ 10⁻¹⁵ M). 5′/3′‑Biotin; Biotin‑TEG; internal Biotin‑dT; Desthiobiotin; Biotin‑PEG/C18 spacers. ELISA, affinity purification, SPR, streptavidin beads/chips.
Digoxigenin (DIG) Hapten recognized by anti‑DIG antibodies. 5′/3′‑DIG; internal DIG‑dT. ISH, blot detection, antibody capture.
DNP / FITC Hapten–antibody affinity with optional fluorescence. 5′/3′‑DNP; 5′‑FITC; internal FAM‑dT. Immuno‑capture, surface tagging, dual readout.
His‑Tag / Polyhistidine Ni²⁺ chelation via NTA/Ni‑NTA for reversible immobilization. Oligo–His₆ peptide; Ni‑NTA‑functionalized oligos. Ni‑NTA beads/chips, IMAC‑style workflows.
Thiol / Maleimide / Gold Sulfhydryl coupling for surfaces and particles. 5′/3′‑Thiol‑C6; Thiol‑Modifier C3 S‑S; maleimide linkers. Gold electrodes, nanoparticles, sensor attachment.
Amino / NHS‑Reactive Amine coupling to carboxyl‑activated surfaces. 5′‑Amino‑C6; 3′‑Amino‑C7; internal amino‑dT; amine‑PEG. Slides, beads, sensor chips.
Aldehyde / Hydrazide / Click Bio‑orthogonal handles for oriented immobilization. 5′‑Aldehyde‑TEG; hydrazide; azide/alkyne for click. Site‑specific conjugation, enzyme‑free ligation.
Thioctic / Lipoic / Dithiolane Self‑assembled monolayers (SAMs) on gold/metal. 5′‑Thioctic; 3′‑Lipoic; internal dithiolane. Biosensors, electrochemical chips.
Streptavidin / NeutrAvidin Direct Protein–oligo conjugates for high‑affinity capture without biotin. Oligo–Streptavidin; Oligo–NeutrAvidin. Direct immobilization, bead‑based capture.
Antibody / Protein G / Protein A Fc‑region binding or antigen‑specific capture. Oligo–antibody (SMCC/sulfo‑SMCC); Protein A/G–oligo. Diagnostics, barcoding, PLA.
Aptamer‑Based Handles Sequence‑specific capture; tunable/reversible. Custom aptamers (e.g., streptavidin‑aptamer, thrombin‑aptamer). Proteins, small molecules, ions.
Metal Chelator Tags Metal‑ion coordination for specific capture. NTA/DTPA/DOTA/NOTA; EDTA‑TEG; metal‑binding amidites. Ni²⁺/Co²⁺/Fe³⁺ capture, purification, MRI agents.
Avidin‑Tagged Nanoparticles / Beads High‑capacity capture interface. Gold–biotin; magnetic bead–streptavidin; agarose–avidin. Magnetic separation, nucleic acid purification, kits.
Peptide‑ / Ligand‑Conjugated Tags Peptide/ligand affinity for specific receptors. RGD, Strep‑Tag II, Twin‑Strep, FLAG, HA‑tag oligos. Integrin assays, engineered streptavidin binding, protein capture.
Technical Notes
Placement & Spacers
  • 5′/3′ ends first: best accessibility; internal tags via dT‑linkers when geometry demands.
  • Spacer length: start with C6; move to C12/PEG if surfaces are crowded or signal is low.
  • Dual‑tagging: combine orthogonal tags (e.g., biotin + DIG) for multiplex or QC.
Surfaces, Buffers & Blocking
  • Beads/plates/chips: confirm capacity (pmol/mg) and avoid overloading.
  • Blocking: casein/BSA or commercial blockers reduce non‑specific binding.
  • Stringency: tune salt/surfactant; keep temperature consistent across runs.
Elution & Reversible Release
  • Ni‑NTA: elute with 200–500 mM imidazole or chelate with EDTA.
  • Biotin systems: use cleavable linkers (disulfide) or photocleavable tethers when harsh elution is undesirable.
  • Hapten tags: mild pH or competitive hapten may displace; validate recovery and integrity.
QC & Documentation
  • Purification: HPLC/PAGE; identity by LC‑MS when applicable.
  • Provide CoA, sequence map, capture/elution notes; optional endotoxin/bioburden.
Quick Recipes (Starting Points)
  1. Streptavidin pull‑down: 5′‑biotin‑TEG oligo → bind (RT, 10–30 min) → wash (high‑salt + 0.01–0.05% surfactant) → analyze or SS‑release (10–50 mM DTT, 5–15 min).
  2. Ni‑NTA reversible capture: His‑mimic oligo → bind → wash → elute with 250–300 mM imidazole; desalt/dialyze before enzymes.
  3. Immuno‑detection: DIG/DNP or FITC tags → hybridize → anti‑hapten detection or bead capture; block with casein/BSA.

Workflow — Numbered Swim-Lanes

1

Biotin / Streptavidin
Tag & Prepare

5′/3′‑Biotin; start with C6 spacer, extend to C12/PEG if needed. Block surfaces.

Biotin-TEG Biotin-dT Desthiobiotin
Bind

Capture on streptavidin beads/plates (RT, 10–30 min). Avoid overloading capacity.

Mag beads SPR chips
Wash

High‑salt + 0.01–0.05% surfactant; keep temperature consistent.

Casein/BSA Orthogonal tags
Analyze / Release

On‑surface readout or release via DTT (disulfide) or use desthiobiotin for reversibility.

SS-linker Desthiobiotin

2

Ni‑NTA / His
Tag & Prepare

His₆ peptide or NTA‑oligos; confirm Ni²⁺ charge state; chelator‑free buffers.

His₆ NTA‑oligo
Bind

Bind to Ni‑NTA surfaces; maintain pH 7–8; keep imidazole low during binding.

Imidazole ≤10 mM Avoid EDTA
Wash

Wash with 10–20 mM imidazole to reduce non‑specific binders.

Low surfactant
Elute / Recover

Elute with 250–300 mM imidazole or EDTA; desalt/dialyze before enzymes.

Desalt Dialysis

3

Hapten–Antibody
Label

Tag with DIG, DNP, or FITC at ends (or internal via dT) per geometry.

DIG‑dT FAM‑dT
Hybridize / Bind

Hybridize probe, then capture/detect with the matched antibody or surface.

Anti‑DIG Anti‑DNP
Wash

Optimize stringency with salt/surfactant; include blockers to cut background.

Casein BSA
Readout / Release

Perform colorimetric/fluorescent readout or elute for downstream analysis.

ELISA FISH

Get Started — Affinity Binding & Capture

Speak with a Bio‑Synthesis scientist about biotin/DIG/FITC, His‑tag/Ni‑NTA, thiol/gold, amino/NHS, or click‑chemistry capture designs.

Speak to a Scientist Browse Tags

FAQ

Is “Affinity Binding & Capture” a function or property?

Function/Application. The enabling type is an affinity tag (e.g., biotin, DIG, DNP, FITC, His‑mimic).

5′ vs 3′ vs internal tagging — what should I choose?

Default to 5′/3′ for accessibility; use internal dT‑linkers when mid‑strand placement is required. Add C6–C12/PEG spacers to reduce steric hindrance.

How do I achieve reversible capture?

For Ni‑NTA, elute with imidazole or EDTA. For biotin systems, insert disulfide or photocleavable linkers between tag and oligo for gentle release.

What QC documents do I receive?

CoA, UPLC/HPLC, LC‑MS (as applicable); optional endotoxin/bioburden for sensitive applications.

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References — Affinity Tags, Capture & Immobilization

  1. Wilchek M, Bayer EA. The avidin–biotin complex in bioanalytical applications. Methods Enzymol. 1990. PubMed.
  2. Höltke HJ, Ankenbauer W, et al. The digoxigenin (DIG) system for non‑radioactive labelling and detection. Mol Cell Probes. 1995. PubMed.
  3. Knecht S, et al. Oligohis‑tags: mechanisms of binding to Ni2+–NTA surfaces. J Mol Recognit. 2009. PubMed.
  4. Hermanson GT. Bioconjugate Techniques, 3rd ed. Academic Press. Elsevier.
  5. Glen Research — Labels & Modifiers. Catalog.
  6. Bio‑Synthesis, Inc. (Lewisville, TX). Custom Oligonucleotide Services.

Why Choose Bio-Synthesis

Trusted by biotech leaders worldwide for over 40+ years of delivering high quality, fast and scalable synthetic biology solutions.

Greetings Researchers,

Please be advised that any information, guidelines, writeups, and oral/video/graphic content on our website are intended solely as general guidelines.
It is the researcher's sole responsibility to conduct thorough research on the designs of the products intended for their experiments before submitting
their designs to Biosynthesis for review of production feasibility.
Thank you for your understanding.

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