ChromoTek Halo-Trap Magnetic Agarose

The ChromoTek Halo-Trap Magnetic Agarose consists of an anti-Halo-tag Nanobody (VHH), which is covalently bound to magnetic agarose beads. Halo-Trap Magnetic Agarose is used to immunoprecipitate Halo-tag proteins from cell extracts of various organisms like mammals, plants, bacteria, yeast, insects etc. in the presence or absence of a covalently bound ligand. The interaction between Halo-Trap and the Halo-tag protein is reversible.

Specificity

Halo-Tag

Applications

IP, CoIP, ChIP, RIP

Type

Nanobody

Conjugate

Magnetic agarose

Publications

2

Cat no : otma

Synonyms

Halo-Trap, Halo, Halo tag

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Validation Data Gallery

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  Halo-Trap Magnetic Agarose for immunoprecipitation of Halo-tag proteins. HEK293T cell lysate with Halo-tag protein. Coomassie and Western blot. Halo-tag antibody [28A8], monoclonal mouse IgG1and anti-mouse secondary antibody. I: Input, FT: Flow-Through, B: Bound

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  Halo-trap Magnetic Agarose for immunoprecipitation of Halo-tag proteins. HEK293T cell lysate with Halo-tag protein. I: Input, FT: Flow-Through, B: Bound

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  Chromatin Immunoprecipitation (ChIP) utilizing Halo-Trap Magnetic Agarose (otma) was performed on cross-linked chromatin isolated from the liver of a transgenic mouse line expressing a Halo-tagged version of clock factor REVERBα (HaloReverbα). Samples were isolated at timepoints of non-peak (ZT20) or peak (ZT8) binding of the REVERBα protein to the Bmal1 promoter region of the genome. The enriched DNA was then quantified by ddPCR utilizing primers directed at a gene desert (negative control region) or the Bmal1 promoter. Fold enrichment of each sample DNA is relative to that of the negative control region of each sample.

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Product Information

The ChromoTek Halo-Trap Magnetic Agarose consists of an anti-Halo-tag Nanobody (VHH), which is covalently bound to magnetic agarose beads. Halo-Trap Magnetic Agarose is used to immunoprecipitate Halo-tag proteins from cell extracts of various organisms like mammals, plants, bacteria, yeast, insects etc. in the presence or absence of a covalently bound ligand. The interaction between Halo-Trap and the Halo-tag protein is reversible.

• Description: Immunoprecipitation of Halo-tagged proteins and their interacting factors with anti-Halo Nanobody conjugated to magnetic agarose beads.

  • Halo Trap recognizes Halo fusion proteins that are already bound to chloralkane-based ligands of the Halo-tag, e.g. dyes, biotin, etc.

  • Halo-Trap can be used for affinity purification

  • Bound Halo-fusion protein can be eluted without protease

  • Structure and function are characterized

• Applications: IP, CoIP, ChIP, RIP
• Specificity/Target: Halo-tag (modified variant of the bacterial haloalkane dehalogenase enzyme from Rhodococcus rhodochrous) in the absence or presence of covalently bound chloralkane-based ligands.
• Binding capacity: 12.5 μg of recombinant Halo-tag per 25 μL bead slurry
• Conjugate: Magnetic agarose beads; bead size: ~40 µm (cross-linked 6 % magnetic agarose beads)
• Elution buffer: SDS sample buffer; 0.2 M glycine pH 2.5
• Wash buffer compatibility: 2 M urea, 2 M NaCl, 10 mM DTT, 2 % Nonidet P40 Substitute, 2 % Triton X-100
• Type: Nanobody
• Class: Recombinant
• Host: Alpaca
• Affinity (KD): Dissociation constant K_D of 2 nM
• Compatibility with mass spectrometry: The Halo-Trap is optimized for on-bead digestion. For the application note, please click here: On-bead digest protocol for mass spectrometry
• RRID: AB_2892995
• Storage Buffer: 20% ethanol
• Storage Condition: Upon receipt store at +4°C. Do not freeze!

Other Formats

Halo-Trap Agarose kit

Halo-Trap Agarose

Halo-Trap Magnetic Agarose Kit

Halo-Trap Magnetic Particles M-270 Kit

Halo-Trap Magnetic Particles M-270

Publications

Application	Title
IP	Cell Rep; Increased degradation of FMRP contributes to neuronal hyperexcitability in tuberous sclerosis complex; Authors - Kellen D Winden
IP	Sci Adv; ER-export and ARFRP1/AP-1-dependent delivery of SARS-CoV-2 Envelope to lysosomes controls late stages of viral replication; Authors - Guy J Pearson