NuGel™ Poly-NHS
NuGel™ Poly-NHS
- Non-specific sites are virtually eliminated by a polymer coating
- Stable across a wide pH range 2 – 10
- 1000Å, 50µm Silica suitable for LC and batch processes
- Applications include: Enzyme immobilization, separation and purification of biopolymers, immobilization of proteins & ligands – monoclonal antibodies, hormones, peptides, haptens, drugs, etc
Silica has been an industry standard as an advantageous matrix suitable for high performance liquid chromatography. With NuGel™, non-specific sites have been virtually eliminated making it an ideal support for affinity purification. Through a proprietary polymer coating, Silica is crosslinked forming a reactive Poly-Epoxy functionality stable across a wide pH range (pH 2 to 10). From this foundational chemistry, all of the NuGel™ affinity products are derived.
NuGel™ Poly-NHS Technical Data
NuGel™ Poly-NHS is a derivative of NuGel™ polyamino affinity support. This affinity support contains NHS groups at the end of hydrophilic spacer arms and is used to couple ligands containing amino groups.
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Technical Data |
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Spacer Arm |
Polymerized hydrophilic carbon chain |
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Porosity |
1000Å |
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Average Particle Size |
50um |
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Substitution Level |
100-200 uEq/gm of NHS groups |
Special Features:
- Couples ligands containing free amino groups.
- pH stable from 2 to 9.
Click here to view NuGel™ Poly-NHS Product Sheet
NuGel Related References
Patents
Monoclonal antibodies directed to the cytotoxic lymphocyte maturation factor European Patent EP0790255
Purification of immunoglobulins using affinity chromatography and peptide US 2006/0153834 A1
Affinity
Dermot Walls, Robert McGrath and Sinéad T.Loughran A Digest of Protein Purification. Methods Molecular Biology. Volume 681: 3-23 (2011)
Ehrlich, G. K., Michel, H., Chokshi, H. P. and Malick, A. W. Affinity purification and characterization of an anti-PEG IgM. Journal of Molecular Recognition, 22: 99–103 (2009).
Development of hepatitis B virus capsids into a whole-chain protein antigen display platform: New particulate Lyme disease vaccines. International Journal of Medical Microbiology Volume 298, Issues 1-2, 3 January 2008, Pages 135-142
A sensitive and high-throughput assay to detect low-abundance proteins in serum Hongtao Zhang, Xin Cheng, Mark Richter & Mark I Greene. Nature Medicine 12, 473 - 477 (2006)
Transformation of a L-peptide epitope into a D-peptide analog. Peptides Frontiers of Peptide Science American Peptide Symposia, 2002, Volume 5, Session XI, 769-770
Expression and folding of an antibody fragment selected in vivo for high expression levels in Escherichia coli cytoplasm. Research in Microbiology Volume 153, Issue 7, September 2002, Pages 469-474
Identification of model peptides as affinity ligands for the purification of humanized monoclonal antibodies by means of phage display Journal of Biochemical and Biophysical Methods Volume 49, Issues 1-3.2001
George K. Ehrlich, Pascal Bailon, Wolfgang Berthold. Phage Display Technology - Identification of Peptides as Model Ligands for Affinity Chromatography Affinity Chromatography Methods in Molecular Biology, 2000, Volume 147, 209-220
A Digest of Protein Purification and partial amino acid sequence of a 28 kDa cyclophilin-like component of the rat liver sigma receptor. Life Sciences , Volume 55, Issue 8, 1994.
Nachman, M., Azad, A. R. M. and Bailon, P. (1992), Efficient recovery of recombinant proteins using membrane-based immunoaffinity chromatography (MIC). Biotechnology and Bioengineering, 40: 564–571.
Kinetic aspects of membrane-based immunoaffinity chromatography. Journal of Chromatography A Volume 597, Issues 1-2, 24 April 1992, Pages 167-172
Identification of model peptides as affinity ligands for the purification of humanized monoclonal antibodies by means of phage display. Methods in Molecular Biology, 2000, Volume 147, 209-220
Membrane-based receptor affinity chromatography. Journal of Chromatography A Volume 597, Issues 1-2, 24 April 1992, Pages 155-166 9th International Symposium on Affinity Chromatography and Biological Recognition
Ion Exchange
Levin W Protein Purification of recombinant human secretory phospholipase A2 (group II) produced in long-term immobilized cell culture. Expr Purif 1992 Feb;3(1):27-35.