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Custom VHHs

VHHs

Your own set of custom VHHs.

Contact us to obtain information on how to proceed. It is very straightforward. Briefly, we obtain your single domain antibodies from an immunized animal. Turnaround time is approximately 3 weeks. The VHHs are ready for prokaryotic expression and you can use them straight away in your experiments. Once you obtained single domain antibodies/VHHs against your target of interest, many new research opportunities arise. Below is a non-exhaustive list showcasing what you can do.

Generate VHHs against your target(s) of interest and magnify your research potential

Now you can generate VHHs that matter most to you and to your research. Include this technology into your next grant application or better even, contact us today. You can either provide us with the purified antigen, or we can generate this in collaboration with you. We guide you through the process, keep you up to date and help you further once you obtain your VHHs of interest. Our researchers have more than two decades of experience in applying them in research.

1520212958405 1

Recombinant expression, intrabody, immunomodulation

  • Express and purify recombinant nanobodies in large amounts (10-100 mg, ormore) at relatively low cost in bacteria or yeast. You routinely obtain milligram quantities per liter bacterial culture. Now you have your pet antibodies for the next decade, and longer.
  • Add any tag you like. Remember, you have the nanobody cDNA! Depending on the epitope they recognize, they can be useful for Western blotting, pull-down/immunoprecipitation experiments. No need to repeatedly purchase antibodies. Let bacteria do the work for you.
  • Use nanobodies like any other cDNA: clone it into an expression vector and transform, transfect, transduce, nucleofect, electroporate… your nanobody into a prokaryotic host or into eukaryotic cells and modulate properties of the antigen.
  • Alternatively, you can use protein transduction to introduce a recombinant nanobody directly into cells.
  • Learn the affinity of the nanobody-antigen interaction via SPR, isothermal titration calorimettry, Octet platform….
  • Epitope mapping becomes easy: using antigen deletion fragments, NMR, X-ray crystallography,..
shutterstock_263643107 1

Stuff you can do in cells

  • You can tune expression of the nanobody to the expression level of the antigen, avoiding unnecessary overexpression. You know exactly how much nanobody is expressed (generally, you don’t know how much of a pharmacological inhibitor enters cells).
  • Generate stable cell lines that express your nanobody of interest in an inducible manner through i.e. lentiviral transduction.
  • You no longer require to overexpress your protein (antigen) of interest as a GFP fusion protein, which may cause artefacts.
  • Trace your protein of interest in living cells by coupling a nanobody to a fluorescent protein through simple cDNA cloning.
  • Delocalize your antigen to other compartments in a cell (nucleus, mitochondria, peroxisomes, endoplasmic reticulum…)
shutterstock_187253015 1

And more...

  • Trigger protein loss of function by tagging your nanobody with a subcellular targeting sequence
  • Eradicate your target protein of interest from cells (protein knock-out) through degradation via the proteasome. As revolutionary as RNAi in 2001.
  • Use your nanobody as a chaperone for co-crystallization studies, to obtain detailed insight into its epitope.
  • Nanobodies are conducive to protein crystallization. This can be a stepping stone to development of a small compound inhibitor via medicinal chemistry.
shutterstock_110934590 1

High end imaging at cellular, organismal level

  • Label your nanobody with a fluorophore for use in (super-resolution) fluorescence microscopy.
  • Link them to quantum dots or nano-gold particles, without jeopardizing nanobody function.
  • Turn it into a diagnostic or a tracer by labeling with 99mTc or other radionuclide
  • Use your nanobody in combination with proteomics, screen for interaction partners, or loss of interaction partners (nanobody footprinting). Due to their small size (15 kDa) they yield much less contaminating peptides in mass spectrometry as a conventional antibody.
  • Share your nanobody with other researchers and formulate new projects and ideas.
  • Insert unnatural amino acids at any pre-chosen site in their primary structure and endow them with unique chemical reactivities.
image 1116x784 1
VHHs

Your own set of custom VHHs.

Contact us to obtain information on how to proceed. It is very straightforward. Briefly, we obtain your single domain antibodies from an immunized animal. Turnaround time is approximately 3 weeks. The VHHs are ready for prokaryotic expression and you can use them straight away in your experiments. Once you obtained single domain antibodies/VHHs against your target of interest, many new research opportunities arise. Below is a non-exhaustive list showcasing what you can do.

Generate VHHs against your target(s) of interest and magnify your research potential

Now you can generate VHHs that matter most to you and to your research. Include this technology into your next grant application or better even, contact us today. You can either provide us with the purified antigen, or we can generate this in collaboration with you. We guide you through the process, keep you up to date and help you further once you obtain your VHHs of interest. Our researchers have more than two decades of experience in applying them in research.

shutterstock_339120512 e1501333583826

Recombinant expression, intrabody, immunomodulation

  • Express and purify recombinant nanobodies in large amounts (10-100 mg, ormore) at relatively low cost in bacteria or yeast. You routinely obtain milligram quantities per liter bacterial culture. Now you have your pet antibodies for the next decade, and longer.
  • Add any tag you like. Remember, you have the nanobody cDNA! Depending on the epitope they recognize, they can be useful for Western blotting, pull-down/immunoprecipitation experiments. No need to repeatedly purchase antibodies. Let bacteria do the work for you.
  • Use nanobodies like any other cDNA: clone it into an expression vector and transform, transfect, transduce, nucleofect, electroporate… your nanobody into a prokaryotic host or into eukaryotic cells and modulate properties of the antigen.
  • Alternatively, you can use protein transduction to introduce a recombinant nanobody directly into cells.
  • Learn the affinity of the nanobody-antigen interaction via SPR, isothermal titration calorimettry, Octet platform….
  • Epitope mapping becomes easy: using antigen deletion fragments, NMR, X-ray crystallography,..
shutterstock_263643107

Stuff you can do in cells

  • You can tune expression of the nanobody to the expression level of the antigen, avoiding unnecessary overexpression. You know exactly how much nanobody is expressed (generally, you don’t know how much of a pharmacological inhibitor enters cells).
  • Generate stable cell lines that express your nanobody of interest in an inducible manner through i.e. lentiviral transduction.
  • You no longer require to overexpress your protein (antigen) of interest as a GFP fusion protein, which may cause artefacts.
  • Trace your protein of interest in living cells by coupling a nanobody to a fluorescent protein through simple cDNA cloning.
  • Delocalize your antigen to other compartments in a cell (nucleus, mitochondria, peroxisomes, endoplasmic reticulum…)
shutterstock_187253015 1

And more

  • Trigger protein loss of function by tagging your nanobody with a subcellular targeting sequence
  • Eradicate your target protein of interest from cells (protein knock-out) through degradation via the proteasome. As revolutionary as RNAi in 2001.
  • Use your nanobody as a chaperone for co-crystallization studies, to obtain detailed insight into its epitope.
  • Nanobodies are conducive to protein crystallization. This can be a stepping stone to development of a small compound inhibitor via medicinal chemistry.
shutterstock_110934590

High end imaging at cellular, organismal level

  • Label your nanobody with a fluorophore for use in (super-resolution) fluorescence microscopy.
  • Link them to quantum dots or nano-gold particles, without jeopardizing nanobody function.
  • Turn it into a diagnostic or a tracer by labeling with 99mTc or other radionuclide
  • Use your nanobody in combination with proteomics, screen for interaction partners, or loss of interaction partners (nanobody footprinting). Due to their small size (15 kDa) they yield much less contaminating peptides in mass spectrometry as a conventional antibody.
  • Share your nanobody with other researchers and formulate new projects and ideas.
  • Insert unnatural amino acids at any pre-chosen site in their primary structure and endow them with unique chemical reactivities.
image 1116x784 1
immunomodulation

Recombinant expression, intrabody

  • Express and purify recombinant nanobodies in large amounts (10-100 mg, ormore) at relatively low cost in bacteria or yeast. You routinely obtain milligram quantities per liter bacterial culture. Now you have your pet antibodies for the next decade, and longer.
  • Add any tag you like. Remember, you have the nanobody cDNA! Depending on the epitope they recognize, they can be useful for Western blotting, pull-down/immunoprecipitation experiments. No need to repeatedly purchase antibodies. Let bacteria do the work for you.
  • Use nanobodies like any other cDNA: clone it into an expression vector and transform, transfect, transduce, nucleofect, electroporate… your nanobody into a prokaryotic host or into eukaryotic cells and modulate properties of the antigen.
  • Alternatively, you can use protein transduction to introduce a recombinant nanobody directly into cells.
  • Learn the affinity of the nanobody-antigen interaction via SPR, isothermal titration calorimettry, Octet platform….
  • Epitope mapping becomes easy: using antigen deletion fragments, NMR, X-ray crystallography,..
Cell Lines

Stuff you can do in cells

  • You can tune expression of the nanobody to the expression level of the antigen, avoiding unnecessary overexpression. You know exactly how much nanobody is expressed (generally, you don’t know how much of a pharmacological inhibitor enters cells).
  • Generate stable cell lines that express your nanobody of interest in an inducible manner through i.e. lentiviral transduction.
  • You no longer require to overexpress your protein (antigen) of interest as a GFP fusion protein, which may cause artefacts.
  • Trace your protein of interest in living cells by coupling a nanobody to a fluorescent protein through simple cDNA cloning.
  • Delocalize your antigen to other compartments in a cell (nucleus, mitochondria, peroxisomes, endoplasmic reticulum…)
loss of function

And more...

  • Trigger protein loss of function by tagging your nanobody with a subcellular targeting sequence
  • Eradicate your target protein of interest from cells (protein knock-out) through degradation via the proteasome. As revolutionary as RNAi in 2001.
  • Use your nanobody as a chaperone for co-crystallization studies, to obtain detailed insight into its epitope.
  • Nanobodies are conducive to protein crystallization. This can be a stepping stone to development of a small compound inhibitor via medicinal chemistry.
super-resolution

High end imaging at cellular, organismal level

  • Label your nanobody with a fluorophore for use in (super-resolution) fluorescence microscopy.
  • Link them to quantum dots or nano-gold particles, without jeopardizing nanobody function.
  • Turn it into a diagnostic or a tracer by labeling with 99mTc or other radionuclide
  • Use your nanobody in combination with proteomics, screen for interaction partners, or loss of interaction partners (nanobody footprinting). Due to their small size (15 kDa) they yield much less contaminating peptides in mass spectrometry as a conventional antibody.
  • Share your nanobody with other researchers and formulate new projects and ideas.
  • Insert unnatural amino acids at any pre-chosen site in their primary structure and endow them with unique chemical reactivities.