CAS 58856-73-8 ω-Aminohexyl-Agarose - Analytical Products / Alfa Chemistry

CAT	AP58856738
CAS	58856-73-8
MDL Number	MFCD00801286

Description	saline suspension
Form	saline suspension
Size	10ML, 50ML, 100ML
Storage Conditions	2-8°C

Human Liver Fatty Aldehyde Dehydrogenase: Microsomal Localization, Purification, and Biochemical Characterization

T L Kelson, J R Secor McVoy, W B Rizzo

Biochim Biophys Acta. 1997 Apr 17;1335(1-2):99-110.

PMID: 9133646

New Ligands for Human C-reactive Protein: Calcium-Dependent Binding With Epsilon-Aminocaproic Acid-Agarose and Calcium-Independent Binding With Omega-Aminohexyl-Agarose

S Kuwajima, T Kishida, T Noda, Y Izumi, K Naka, T Matsui, K Okuda

Int J Tissue React. 1990;12(2):71-6.

PMID: 2210970

Purification of Antibodies Against N-homocysteinylated Proteins by Affinity Chromatography on Nomega-homocysteinyl-aminohexyl-Agarose

Joanna Perła, Anetta Undas, Tomasz Twardowski, Hieronim Jakubowski

J Chromatogr B Analyt Technol Biomed Life Sci. 2004 Aug 5;807(2):257-61.

PMID: 15203038

Purification of Human IgG by Negative Chromatography on Omega-Aminohexyl-Agarose

Maria Cristiane Martins de Souza, Igor Tadeu Lazzarotto Bresolin, Sonia Maria Alves Bueno

J Chromatogr B Analyt Technol Biomed Life Sci. 2010 Feb 15;878(5-6):557-66.

PMID: 20079697

Purification, Cloning and Expression of Spinach Leaf Sucrose-Phosphate Synthase in Escherichia Coli

U Sonnewald, W P Quick, E MacRae, K P Krause, M Stitt

Planta. 1993 Feb;189(2):174-81.

PMID: 7763376

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Case Study

ω-Aminohexyl-Agarose: A Versatile Matrix for Fatty Acyl-Conjugation and Protein Pull-Down Applications

Li, Tie-Mei, et al. Scientific reports 9.1 (2019): 14226.

ω-Aminohexyl-Agarose is widely utilized as a functional matrix for conjugation with fatty acids, enabling affinity-based protein interaction studies. In a recent study, fatty acids ranging from C2 to C20 were covalently linked to ω-Aminohexyl-Agarose beads via an optimized modification of a previously established protocol. The conjugation process involved the reaction of fatty acid anhydrides with the agarose-bound amine groups in the presence of N,N-Diisopropylethylamine (DIEA) in dimethylformamide at 65°C. Successful conjugation was verified through a ninhydrin assay, ensuring complete amine blocking.
The resultant fatty acyl-conjugated agarose beads were employed in protein pull-down experiments to investigate protein-lipid interactions. Recombinant proteins, following GST tag cleavage, were incubated with the modified agarose beads in an optimized buffer system. After incubation, the bound proteins were eluted, analyzed by SDS-PAGE, and detected using silver staining, with quantitative assessments performed using ImageJ. Additionally, stable isotope-labeled Hela cell lysates were subjected to the same pull-down procedure, followed by LC-MS/MS analysis to identify lipid-binding proteins.
This study highlights ω-Aminohexyl-Agarose as a critical tool for biochemical and proteomic research, facilitating the study of protein-lipid interactions through a robust and reproducible immobilization approach. Its application in affinity-based assays underscores its importance in advancing lipidomics and structural biology.

ω-Aminohexyl-Agarose for Selective IgG Purification from Human Serum

De Souza, M. C. M., Bresolin, I. T. L., & Bueno, S. M. A. (2010). Journal of Chromatography B, 878(5-6), 557-566.

ω-Aminohexyl-Agarose, a CNBr-activated gel, has demonstrated significant utility in the selective purification of immunoglobulin G (IgG) from human serum using negative chromatography. In a recent study, ω-Aminohexyl-Agarose was packed into columns and equilibrated with various Good's buffers (Mes, Mops, and Hepes) to evaluate their influence on serum protein adsorption and IgG recovery.
Serum samples, diluted in equilibration buffer, were loaded onto the ω-Aminohexyl-Agarose column, followed by washing and elution with NaCl-containing buffer. Protein retention was monitored via UV absorption at 280 nm, and IgG purity was assessed using nephelometry and the Bradford method. Results indicated that buffer pH played a crucial role in IgG purification. Among the tested conditions, Hepes buffer at pH 6.8 provided the optimal balance, yielding 35.1% nonretained IgG with a purity of 95.6%.
Further experiments compared ω-Aminohexyl-Agarose (spacer arm of one atom) with ω-Aminohexyl-Bisoxirane-Agarose (spacer arm of 12 atoms). The longer spacer arm in the bisoxirane-activated gel reduced steric hindrance, enhancing IgG selectivity and yield.
These findings establish ω-Aminohexyl-Agarose as a valuable tool for serum protein separation, particularly in applications requiring high-purity IgG. Its effective performance in negative chromatography highlights its potential in antibody purification and biomedical research.