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Using HemoVoid to Remove Hemoglobin Before Analysis

Validation of a commercial resin, HemoVoid, to investigate the efficiency of hemoglobin depletion technology before analysis


BSG has developed a chemical library of general non-specific adsorbents, or stated another way - beads with weak affinity or imperfect fit interactions. Without the use of antibodies, progressive displacement allows the beads to bias for or against certain proteins, without compromising protein integrity. Each product is empirically characterized to meet the needs of the application. In particular, HemoVoid™, is designed to remove hemoglobin from erythrocyte lysate samples in a simple and efficient manner.

The Challenge

Used by researchers studying the cytoplasmic protein content of red cells who need to remove hemoglobin, the most abundant protein in red cells, HemoVoid™ is used to enrich the low abundance proteome before analysis.

A recent research article describing the simplicity and efficiency of HemoVoid™, to enrich the soluble cytoplasmic proteins in order to assess the activity of sGC, PDE, and PKG in Hb-free extracts. They aimed to establish a procedure that allowed for fast and reliable preparation of hemoglobin-free cell lysates from as little as 1–2 ml blood.

The Solution

As one of the main advantages of HemoVoid™, the maintenance of functional activity post-separations provided fast, reliable, functional integrity of enriched sub-proteome.

Additional key advantages include:

  • Hemoglobin voids in flow-through >98%, with <30 minute bind/wash/elute protocol
  • Sample types include red blood cells, whole blood, and dried blood cards
  • Species agnostic, validated on human, mouse, sheep, goat, bovine

The Outcome

Without a reliable resin like HemoVoid™, the study would have been compromised by the analytical noise introduced due to the presence of hemoglobin.

This article illustrates the importance of not only removing the influence of hemoglobin in order to perform proteomic analysis of red cells, but that the activities of the soluble RBC enzymes are preserved and can be monitored for differential function in disease.