Princeton, NJ, April 8, 2016 – Princeton based Biotech Support Group announced today that it has submitted provisional patents disclosing its data on many common proteins dysregulated in cancer. This breakthrough research shows that most of these biomarkers are believed to be dysregulated regardless of the primary tumor, stage of progression or tumor burden. The study which collaborated with the Rutgers Center for Integrative Proteomics shows the most distinguishable pattern of early dysregulation observable as a cancer serum phenotype to date. This forms the basis of a new commercialization plan featuring:
Variant sub-populations (also known as proteoforms) of a common blood protein – Alpha-1-Antitrypsin, with functional reporting features severely distinguishable between cancer patients and normal/healthy individuals
A measurable serum cancer profile that can be modeled with categorical biomarker proteins taken from inflammation, blood coagulation, tissue remodeling, and glycolysis, as well as new markers of unknown function.
The company will present its latest data as a poster report (LB-065) and announce its new commercialization plans at its Exhibit Booth # 658, at the upcoming AACR Annual Meeting 2016, April 16 - 20, 2016 in New Orleans, LA. The AACR meeting is expected to have well over 20,000 research scientists and physicians
Poster presented at US HUPO on March 13-16, 2016:
"The Comparison Of The Serum Proteome In Individuals With Cancers Versus Those Without Cancer, And Its Application To Wellness"
For many diseases, pancreatic cancer for example, long term survival is critically dependent upon early detection. So
various strategies for early detectable markers are being investigated. One such strategy is to identify a singular biomarker,
derived from genomic analysis, and then determine its derivative protein concentration in blood. This has been challenging
as many differentially regulated genes do not generate a differentially regulated protein. An alternative biomarker strategy is
to consider panels of proteins as up and/or down regulated biomarkers, which differ in diseased and normal states. Following
this strategy, many serum proteomic investigations have analyzed one cancer type or another, but our goal was to consider
whether patterns of multiple proteins dysregulated in cancer could be observed regardless of the primary tumor, stage of
progression or tumor burden. In this study we adopt a relatively new method, which combines Albumin depletion and
onbead digestion of the depleted serum in a seamless process, called AlbuVoid™ LC-MS On-Bead. From this method,
able to compare labeled quantification of proteins from normal and disease state sera – for this case, breast, lung and
pancreatic cancer. The methods spectrally quantify over 200 total proteins, in a cost effective and reproducible manner. No
offline peptide level fractionation prior to LC-MS was employed, lowering the LC-MS acquisition time 5-10x compared to
common serum proteomic workflows. We describe these workflow advantages applied towards a “wellness” proteome
strategy whereby knowledge and data surrounding individual normal and healthy proteomes can be annotated, compared
and contrasted to those with a clinically definable disease, in our case the serum cancer phenotype.Read more.
"AlbuSorb™ Product Extension Combines Albumin and Immunoglobulin Depletion in a Consumable Format"
The NuGel™ platform chemistry, a porous polymer coated (ionic, polymeric, aliphatic) silica library of bead architecture allows liquid chromatography mass spectrometry experiments. Albusorb™ from Biotech Support Group depletes albumin.Proteomic enrichment of low abundance proteins from beads and high abundance serum protein depletion may require albumin and immunoglobulin removal. Samples can be human serum or mouse plasma. To obtain LC-MS spectra counts various parameters such as fixed modification (carbamide methylation or cysteine and SDS with Tris) and variable modification (deamidation on Asparagine oxidation) of samples can be set. Some experiments on globin depletion can require protein A combination protocols. A database of serum proteins can be quantified on cancer sera phenotype and normal healthy patients. The sub proteome functional analysis can be applicable to downstream experiments such as antibody arrays, ELISA, LC-MS, 1&2 DE, Western blot etc.