- 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.
Polymerized hydrophilic carbon chain
Average Particle Size
100-200 uEq/gm of NHS groups
- Couples ligands containing free amino groups.
- pH stable from 2 to 9.
Click here to view NuGel™ Poly-NHS Product Sheet
NuGel Related References
Monoclonal antibodies directed to the cytotoxic lymphocyte maturation factor European Patent EP0790255
Purification of immunoglobulins using affinity chromatography and peptide US 2006/0153834 A1
Chaumet, Alexandre, Sandrine Castella, Laïla Gasmi, Aurélie Fradin, Gilles Clodic, Gérard Bolbach, Robert Poulhe, Philippe Denoulet, and Jean-Christophe Larcher. "Proteomic analysis of Interleukin enhancer binding factor 3 (Ilf3) and Nuclear Factor 90 (NF90) interactome." Biochimie (2013).
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
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.