Sample Prep - Pandemic Research

Investigate the Immune Response to COVID-19 with Our Products

“… studies suggest that at least a subset of severe COVID-19 infection involves a catastrophic, complement-mediated thrombotic microvascular injury syndrome with sustained activation… of complement.” Translational Research 2020.

Erythrocytes do not have a nucleus, and being in continuous contact with complement proteins in plasma, have a different make-up of complement regulators than nucleated cells. Increased complement activation or decreased complement regulation may result in red cell dysfunction. This may explain some of the clinical symptoms seen in severe COVID-19 patients- low oxygen levels and neurological complications. Therefore, proteomic investigation of erythrocytes is warranted.

The hemoglobin removal products that follow have proven extremely efficient in coverage, detecting post-translational modifications, and quantifying the erythrocyte proteome.


Hemoglobin Depletion For Erythrocyte Proteomics

  • Hemoglobin voids in flow-through, applicable to red cells, heavily hemolyzed serum, whole blood and dried blood spot (DBS) card
  • Low abundance protein and enzyme enrichment
  • Consumable, cost-effective
  • Mild elution maintains native structure with retained enzymatic, functional and bioactivities
  • Compatible with LC-MS, activity-probe profiling and virtually all proteomic analyses
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2DE Comparison

2DE Comparison.
Red circles indicate the Hemoglobin subunits region. The HemoVoid™ eluate (bottom) has been severely depleted of Hemoglobin. The remainder of the red cell proteins are substantially enriched (visualized) and are better resolved in the HemoVoid™ eluate. Many more proteins are detectable after HemoVoid™ treatment with extensive proteome coverage across both dimensions.

Key References

This study aimed to report the post-translational identity, biological activity and concentration of monomethyl and dimethylarginine-modified proteins by using GC-MS and LC-MS/MS approaches. The article states “we included in our method the use of HemoVoid™ … to improve the SDS-PAGE separation of proteins for further processing. HemoVoid™ …allowed removal of erythrocytic hemoglobin to a large extent. … removal of hemoglobin by this technique enabled an effective separation by SDS-PAGE and isolation of bands, presumably by avoiding overloading of the gels by hemoglobin.”.

Bollenbach, Alexander, et al. "GC-MS and LC-MS/MS pilot studies on the guanidine (NG)-dimethylation in native, asymmetrically and symmetrically NG-dimethylated arginine-vasopressin peptides and proteins in human red blood cells." Journal of Chromatography B (2020): 122024.

The article describes the advantage of HemoVoid™ in detection of low abundance proteins when comparing their amounts (in percent) between with four other extraction conditions. Most peptides, following HemoVoid™ extraction, “showed ion abundances ranging between 1.00E+5 and 1.00E+6 (31%). In comparison to this, fewer peptides (10–23%) were within this range following extraction with all other protocols”. With respect to potential biomarkers for Parkinson’s Disease, the article states “For example, PRDX6 accounts for 0.4% of the total ion abundance after DOC (deoxycholate) extraction, whereas following HV (HemoVoid™) extraction, this increases to 8%, a 20-fold enrichment”. The authors conclude that the HemoVoid™ method significantly reduces the concentration of hemoglobin, resulting in an increased signal-to noise of the remaining red cell proteins. The article describes methods to digest the HemoVoid™ bead-bound proteome, greatly simplifying the workflow for LC-MS/MS analysis.

Klatt, Stephan, et al. " Optimizing red blood cell protein extraction for biomarker quantitation with mass spectrometry." Analytical and Bioanalytical Chemistry (2020): 1-14.


Suspension Reagent to remove Hemoglobin to assist the study of lower respiratory tract disease based on testing of bronchoalveolar lavage (BALF) fluid

  • Highly specific for hemoglobin binding
  • depletion from hemolyzed serum, dura, BALF, and whole blood
  • Functional integrity maintained with simple transfer to post-treatment interrogations
  • supports biomarker tests
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Key References

HemogloBind ™ Cited in Comparison Proteomics Study of Covid-19 Patients in Peripheral Blood Derived Mononuclear Cells (PBMCs) – The Barometer of the Immune System

HemogloBind sample preparation technology provides deep and quantitative LC-MS proteome and phosphoproteome analysis. This study provides a comparison of SARS-CoV-2 positive ICU patients with age- and sex-matched SARS-CoV-2 negative ICU patients and healthy individuals, using peripheral blood derived mononuclear cells (PBMCs).

Kaneko, Tomonori, et al. "System-wide hematopoietic and immune signaling aberrations in COVID-19 revealed by deep proteome and phosphoproteome analysis." Research Square preprint (2021).

A research article describes the simplicity and efficiency of BSG's hemoglobin depletion technology for 2X improvement of proteomic information obtained from bronchoalveolar lavage fluid (BALF).

Maneesh Bhargava M. et al."Proteome Profiling in Lung Injury after Hematopoietic Stem Cell Transplantation". Biol Blood Marrow Transplant 22 (2016) 1383-1390.

The cellular thermal shift assay (CETSA) enables proteome-wide target screening for unmodified antimalarial compounds with undetermined mechanisms of action, providing quantitative evidence about direct drug–protein interactions. The article states “The intact-cell CETSA protocol features a HemogloBind- based sample processing step, which provides a relatively fast, reliable and inexpensive method to deplete >90% of hemoglobin from processed intact-cell samples. As a result, it leads to a 40-50% increase in the number of peptide spectrum matches (PSMs) for P. falciparum and non-hemoglobin human proteins.”. The citation is: Dziekan, Jerzy Michal, et al. "Cellular thermal shift assay for the identification of drug–target interactions in the Plasmodium falciparum proteome." Nature Protocols (2020): 1-41.

HemogloBind™ Nucleic Acid

Suspension Reagent to remove Hemoglobin interference for PCR

  • Suitable for infectious disease research or rigorous analysis for whole blood or heavily hemolyzed samples
  • Scaleable suspension reagent
  • Robust and simple, no phenol/chloroform or ammonium sulfate precipitation
  • High Yield – free and soluble DNA or RNA is highly recoverable
  • > 95% Hemoglobin and Protein removal from whole blood lysates & dried blood cards
  • Eliminates inhibitory effects of heme for PCR applications
  • Compatible with silica-type final isolation preps
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RNA/DNS Recoverable from Blood
RNA/DNS Recoverable from Blood


Lipid Removal Reagent and Clarification

  • Effectively replaces chlorinated/fluorinated hydrocarbons (eg. freon)
  • A high binding capacity for lipids with minimal cross-reactivity with proteins and nucleic acids
  • Ideal for clarifying ascites, serum, tissue culture, saliva
  • Exquisite selectivity profile including extracellular vesicle and exosome clearance
  • For downstream processing of monoclonal antibodies

Cleanascite™ is derived through a proprietary formulation of metallic oxide derivatives. Unlike other metallic oxides, Cleanascite™ does not have significant protein binding making its selectivity profile for lipids unique in the bio-research products industry. As a result, it is ideal to clear lipid-associated matrix effects from human sera, bile, ascites, and other high lipid content sample types.

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Cleanascite™ is supplied as a suspension reagent.

Cleanascite™ is supplied as a suspension reagent. Simply add, mix and centrifuge in a 10 minute protocol.

Key References


Farina, Annarita. " Pre-fractionation of Noncirculating Biological Fluids to Improve Discovery of Clinically Relevant Protein Biomarkers." Proteomics for Biomarker Discovery. Humana Press, New York, NY, 2019. 23-37.
For proteomic biomarker discovery, it is necessary to bridge the gap between basic and applied research by complying with clinical requirements. This chapter provides key suggestions for improving the discovery of clinically relevant protein biomarkers from body fluids. The chapter states : ”If the elimination of lipids…is necessary, the sample can by treated with lipid removal (Cleanascite™)…

Plasma/Serum Protein Biomarkers

The authors aimed at simultaneously measuring intact insulin and proinsulin derived C-peptide, to help predict development of diabetes mellitus, as well as in differential diagnosis in cases of hypoglycemia. Cleanascite™ is shown both to improve LC-MS measurements, and validated in accordance with CLIA ’88 guidelines. { doi: 10.1016/j.cca.2016.01.019 }

Vaccine Development

To evaluate immunogenic response to a vaccine candidate, it is necessary to measure the antibodies from sera; a sample with a diverse lipid profile. In this citation, Cleanascite™ was used in a toxin neutralizing assay to evaluate the influence of cholesterol dependency, on a candidate protein pneumococcal vaccine. { doi: 10.1016/j.vaccine.2012.11.005 }

Ascites Monoclonal Antibodies

The researchers determined the role of complement on MAb-mediated protection for four mice Ig subclasses. After centrifugation of ascetic fluid, Cleanascite™ protocol was implemented to remove lipids. { doi: 10.1128/IAI.70.5.2598-2604.2002 }

Cellular Response Applications

The applications and references for the many diverse investigations using Cleanascite™ upstream of cell response measurements are described. { Cleanascite Cell Response Reference Applications }

Tracheal Swab Samples

Li D, Wang J, Wang R, Li Y. A nanobeads amplified QCM immunosensor for the detection of avian influenza virus H5N1, Biosensors and Bioelectronics.2011;26(S10):4146-4154 Fu LM, Shinnick TM. Genome-wide exploration of the drug action of capreomycin on Mycobacterium tuberculosis using Affymetrix oligonucleotide GeneChips Journal of Infection.2007;54(S3):277-284 Fu LM, Shinnick TM. Genome-wide analysis of intergenic regions of mycobacterium tuberculosis H37Rv using affymetrix genechips. EURASIP journal on bioinformatics & systems biology.2007:23054


Lucy E. DesJardin Isolation of M. tuberculosis RNA from Sputum Methods in Molecular Medicine.2001;48:133-139 Beenhouwer DO, Shapiro S, Feldmesser M et al. Both Th1 and Th2 Cytokines Affect the Ability of Monoclonal Antibodies To Protect Mice against Cryptococcus neoformans Infection and immunity.2001;69: 6445-6455 Desjardin LE, Perkins MD, Wolski K et al. Measurement of Sputum Mycobacterium tuberculosis Messenger RNA as a Surrogate for Response to Chemotherapy American journal of respiratory and critical care medicine.1999;160(1):203-10

Viraffinity™ & ViraPrep™ Mammal Kit

Virus Enrichment & Purification

  • Prepares viral samples for subsequent detection and analysis
  • Has pan-virus affinity, unknown for coronavirus
  • Solid-phase polymer separation, protocol does not require ultracentrifugation

Lanes M: Markers
Lane 1: PEG/Phenol-Chloroform
Lane 2: ViraPrep™ Lambda methods
Lane 3: Eco R1 digest of ViraPrep™ Lambda DNA
Note: Insert band apprx. 1 kb

Since the COVID-19 virus can be detected in stool samples, it has been proposed that detection of the virus in wastewaters will help to monitor local or regional outbreaks. For this to succeed, simple and robust measurement of viruses from wastewater is necessary. Conventionally, enteric viruses are first concentrated by a variety of filter methods. A secondary enrichment step is often employed, to reduce to a final volume and improve purity prior to final analysis. This secondary step may be provided by the Viraffinity™ reagent, and does not require ultracentrifugation. As described in these two references: 1) Viraffinity™ can dramatically improve the purification of viruses, and 2) can remove RT-PCR inhibitors in the detection of enteric viruses.

1) Romain Fragnoud R., et al. "Differential proteomic analysis of virus enriched fractions obtained from plasma pools of patients with dengue fever or severe dengue". BMC Infectious Diseases (2015) 15:518.

The article's authors report a method to compare the proteomes of virion-enriched fractions purified from plasma pools of patients with dengue fever or severe dengue. Virions were purified by ultracentrifugation combined with Viraffinity™. “…and became more intense after the Viraffinity™ step...Densitometry indicated that the protein complexity of the purified samples was reduced by roughly 350-fold compared to the unpurified samples.”.

2) Leggitt, Paris R., and Lee-ann Jaykus. "Detection methods for human enteric viruses in representative foods." Journal of Food Protection 63.12 (2000): 1738-1744.

“To optimize viral nucleic acid amplification, secondary PEG precipitates… required a prior adsorption step with an equal volume of Viraffinity™ to further remove RT-PCR inhibitors. In this case, viruses …were adsorbed by the addition of an equal volume of Viraffinity™, … These Viraffinity™ precipitates were used directly in subsequent RNA extractions.”


Prep Size: Application dependent

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ViraPrep™ Mammal

Prep Size: 40 ml

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A research article describes the simplicity and efficiency of this virus enrichment technology to enhance viral proteomic analyses from plasma.

Romain Fragnoud R., et al. "Differential proteomic analysis of virus enriched fractions obtained from plasma pools of patients with dengue fever or severe dengue". BMC Infectious Diseases (2015) 15:518.

The article's authors report a method to compare the proteomes of virion-enriched fractions purified from plasma pools of patients with dengue fever or severe dengue. Virions were purified by ultracentrifugation combined with Viraffinity™. “…and became more intense after the Viraffinity™ step...Densitometry indicated that the protein complexity of the purified samples was reduced by roughly 350-fold compared to the unpurified samples.". The authors conclude that the Viraffinity™ based technique of virion-enrichment allowed them to identify two host proteins that have prognostic value for classifying patients with acute dengue who are more likely to develop a severe dengue.

Our products are for research only
To the best of our knowledge, none of our products has been tested for suitability for any characterization of COVID-19 or its consequences on patients.

Our BSG Advantage


Cost-effective, not derived from biologicals

Cost-effective, not derived from biologicals

  • No specialized instruments or HPLC
  • Economical surface chemistries, not derived from biologicals
  • No regeneration, so no prep to prep variability
  • Simple, fast microfuge bind/wash/elute protocols

On-Bead Digestion

Efficient workflows, quality LC-MS/MS data

Efficient workflows, quality LC-MS/MS data

  • Simple, reproducible workflows
  • Equivalent or better than in-solution digestion
  • Seamless to LC-MS, no desalting or C18 separations
  • Unique proteolytic efficiencies


Diverse strategies, species agnostic

Diverse strategies, species agnostic

  • Products support strategies for both enrichment of low abundance proteomes, or depletion of high abundance proteins
  • Species agnostic not derived from biologicals

Functional Integrity

Maintained throughout all separations

Maintained throughout all separation

  • Mild buffer conditions maintains native structure with retained enzymatic, functional & bio-activities
  • Supports enzyme biomarker assays
  • Functional & Chemical Proteomics
  • Structural & activity-probe Proteomics
  • Top-down & ArrayBridge PEP Proteomics