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NuGel™ Poly-Amine

NuGel™  Poly-Amine


Base Price: $550.00

Product Code: NPAM

Size (NPAM):


NuGel™ Poly-Amine For Immobilization

  • 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-Amino Technical Data

NuGel™ Poly-Amino is a derivative of NuGel™ polyhydroxy affinity support. This affinity support contains amino groups at the end of hydrophilic spacer arms and is used to couple ligands containing carboxyl, aldehyde, anhydride and epoxy groups.

Technical Data
Spacer Arm Polymerized hydrophilic carbon chain
Porosity 1000Å
Average Particle Size 50um
Substitution Level 100-200 uEq/gm of amine groups

Special Features:

  • Couples ligands containing free carboxyl groups in the presence of a carbodiimide.
  • Couples ligands containing free aldehyde, anhydride and epoxy groups.
  • Couples non-polar ligands in organic solvents.
  • pH stable from 2 to 9.
Click Here To View NuGel™ Poly-Amine Product Protocol

NuGelRelated 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


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Dermot Walls, Robert McGrath and Sinéad T.Loughran A Digest of Protein Purification. Methods Molecular Biology. Volume 681: 3-23 (2011)

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A sensitive and high-throughput assay to detect low-abundance proteins in serum
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Kramer, A., & Schneider-Mergener, J. (2002). Transformation of a L-peptide epitope into a D-peptide analog. In Peptides Frontiers of Peptide Science (pp. 769-770). Springer, Dordrecht

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.