AlbuVoid™ for studying the albumin fraction for drug and protein interactions & analyzing the unbound fraction for albuminome subproteome biomarker discovery.
AlbuVoid™ is an albumin depletion plus low abundance serum protein enrichment reagent from Biotech Support Group that allows researchers to explore how albumin binds to proteins or drug complexes. To do biomarker and proteomic studies, AlbuVoid™ uses mild buffers thus preserving functional properties of the sample.
Serum albumin is the most abundant protein in serum, typically present at approximately 30-40 mg/ml. Albumin binds to protein, lipid, and small molecules in the intracellular space and has been found to form associations with peptide hormones, serum amyloid A, interferons, glucagons, bradykinin, insulin, and Streptococcal Protein G. Furthermore, albumin has been reported to bind to a small number of specific proteins such as paraoxonase 1 , alpha-1-acid glycoprotein , and clusterin (indirect interaction through paraoxonase 1) and apolipoprotein E 12 in serum. Albumin has been found to change with disease which alters its binding to metals and currently functions as a biomarker for ischemia. Albumin is found in a variety of biological samples, including plasma, amniotic fluid, seminal fluid, and cerebral spinal fluids, among others.
A modification of albumin that has previously been identified as a biomarker for myocardial ischemia is the N-terminus N-acetylation of albumin, which decreases the binding affinity of albumin to cobalt and nickel. The fatty acid transport function of albumin is modified in atherosclerosis and diabetes . In patients with diabetes, the binding capacity of albumin for fatty acids is increased, and in patients with atherosclerosis the capacity is decreased. In conclusion, the evidence the albumin is changing with disease is clear.
The AlbuVoid™ protocol uses mild buffers; the protocol conditions are so gentle that the functional activity is retained in flow through(albumin fraction) & elution fraction(albumin depleted serum/plasma proteins). Researchers now have a choice to study albumin for biomarker and proteomic studies focusing on how albumin-protein complexes and albumin-drug complexes interact. Such studies could also be focused on potential disease and non-disease research work to analyze how affinity binding sites and ligands interact under changing physiological conditions.
For more information, visit Biotech Support Group http://www.biotechsupportgroup.com/product_info.php?products_id=42
References
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