Introducing Biotech Support Group Proteomic Services

With fully developed applications in proteomics, clients can take advantage of our unique enrichment capabilities. From client delivered samples, for example- normal vs. disease, we will deliver proteomic data to serve these applications:

BSG-OMx™ Serum Proteomic LC-MS/MS Identifications
High Abundance Depletion + On-Bead Digestion Efficiency + Simple Workflow
= Better LC-MS Output

*Total protein abundances, label or label-free

*Glycoprotein using ConA glycopeptide fractionation (optional)

Using our proprietary advantaged workflow, we combine albumin depletion with low abundance enrichment on the bead, coupled to on-bead digestion. Normally hard to digest glycoproteins are now efficiently digested producing significant gains in protein identifications from LC-MS/MS. Our methods produce a large number of identifications at a reasonable cost, as only a single 3 hour gradient is required. In addition, an optional glycopeptide enrichment incorporating immobilized ConA, can generate glycoprotein identifications. These can be quantified by both label and label-free spectra, resulting in a variety of specialized outputs to consider:
>Total serum protein abundances
>Glycoprotein abundances
>Ratios of total to glyco, individually or collectively

Typical Performance
Serum Sample Volume
100-200 µl
Albumin Removal
LC-MS unique Protein IDs*
LC-MS unique Peptide IDs*
LC-MS spectral counts*
11,000 - 12,000
ConA Glycoproteins
*from single 3 hour LC gradient

Read this poster report for more information:

BSG-OMx™ Chemical Proteomics


LC-MS identifications of the interacting sub-proteome of any small compound

Compound-centric Displacement Proteomics - An advantaged method to survey small molecule-protein interactions

>Optimize drug compounds, survey promiscuity
>De-convolute drug targets & study MOA
>Identify phenotypic biomarkers
>Any compound, any tissue

The binding interactions of small compounds to proteins within the cell is paramount to understanding a potential therapeutic compound's mechanism of action. It is therefore necessary to have tools and methods to survey the promiscuous behavior of compounds towards multiple proteins and posit such behavior as deterministic of either toxicity or efficacy (poly-pharmacology). We offer a new method for this purpose, called Compound- centric Displacement Proteomics (CCDP). With CCDP, proteins are first non-selectively, and reversibly bound to a novel bead format. A subset of proteins can then be displaced upon introduction of soluble small compounds. Coupled to LC-MS, quantitative metrics of these affinity-eluted sub-proteomes help characterize and identify interacting proteins. These new methods gain efficiencies over prior covalent- based substitution methods and can serve applications in drug target deconvolution, on-target/off-target specificity, poly-pharmacology, and personalized medicine.

Read this poster report for more information:

BSG-OMx™ Functional Proteomics

The unique ArrayBridge PEP platform characterizes function on a proteome scale

Most efforts in proteomics seek to identify and sequence annotate the proteome by LC-MS/MS analyses of peptides derived through proteolytic processing. However, little attention has been paid to functional annotation. Yet functional annotation is crucial as the landscape of protein conformations is highly variable, each conformation contributing to its own functional activity. Sequence annotation alone cannot capture this vital information, so new strategies are necessary. The PEP technology, developed by Array Bridge, uses a modified Two-dimensional Gel Electrophoresis to separate the proteome, without substantially compromising function. The isolated proteins are then electro-eluted from the PEP plate, and enzyme activities are measured systematically.

The PEP technology is an open platform adaptable to any measurable protein function. It serves as an efficient method for high sensitivity proteome pattern profiling, quantitative and systematic top-down analysis of isolated protein function, and purity suitable for Mass Spectrometry protein identification. Furthermore, in different tissues, or under stress or disease conditions, protein sequences that are normally associated with one function, may perform alternative functions - that is what we call the multi-functional proteome. This multi-functional proteome can now be monitored, cataloged and annotated by this PEP-based functional proteomic strategy. Using a top-down approach, we can start with any measurable protein function, resolve functionally active proteins into microwells, and from there, sequence and structurally annotate the subset proteome that presents that function.

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Biotech Support Group pursues strategic alliances that are in keeping with our goal to be a world leader in the development and commercialization of innovative life sciences tools and technology. We specialize in:

  • Hemoglobin Depletion, Low Abundance Enrichment
  • Albumin Depletion, Low Abundance Enrichment
  • Lipid Binding Research
  • Glycoprotein Research
  • Kinase Research
  • Cyclic Nucleotide Phosphodiesterase Research
  • Efficient Protein Removal for Nucleic Acids, Drug Screening & Metabolomics
  • Biomarker discovery
  • High Throughput Formats
  • For more information, please contact: