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Introducing ezGEL

The ULTIMATE blood concentrate just got even better!

EZGEL is a 100% autologous and natural gel material, obtained through centrifugation of a whole blood sample to isolate beneficial cells, then subjected to a cooling and heating process, without any chemical addition nor modification, for rejuvenating and volumizing purposes.

By heating up Plasma, particularly HSA, we're modifying its rheological properties. Temperature variation is the most natural way to create an intermolecular bond, without using any additives such as BDDE for cross linking.

EZGEL is created by combining this heated plasma gel and EZPRF concentrate at a 2:1 ratio.

Wait, what's ezPRF again?

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Low Speed
Centrifugation

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More Cells

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100% Natural
No additive

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Fibrin Scaffold

What's new with ezPRF ?

Meet human serum albumin (HSA)

Shaped very much like a heart, serum albumins are the most abundant proteins in blood, constituting nearly 60% of blood plasma proteins.

This is the star protein of our new protocol. We'll illustrate denaturation and take a deep look at this protein's reaction to temperature (Unfolding).

But first, let's refresh our memory on some of the key definitions.

Denaturation

When a protein starts to lose it's biomolecular structure. Denaturation of proteins is a process of transition from the folded to the unfolded state.

Unfolding / refolding

Denaturation is reversible under a certain temperature / stress. We prefer "unfolding" and "refolding" up until it's irreversible because it's a very visual term. (see next section)

Aggregation

Forming a cluster of things that have come together.

Self-assembly

Self-assembly is a process in which a disordered system of pre-existing components forms an organized structure or pattern.

Melting point

The protein melting point (TM) is defined as the temperature at which the protein denatures.

Understanding protein unfolding (Denaturation)

Folded molecular structure

A folded protein is just like a folded paper clip! In their folded state, they can be moved around and won't get tangled.

Our folded proteins flow freely in their fluid vehicle / environment (The plasma).

Unfolded & self-assembled

Once unfolded, paper clips start aggregating and assemble in an organized structure

This is also called self-assembly of proteins.

Why 75°C*?

The temperature behavior of Albumin has been studied for over 50 years. Many articles can be found online, here's a quick recap:

  • The thermal denaturation of HSA takes place in a sequential manner - domain II starts to denature at 56°C followed by domain I at 62°C – these are also called melting points.
  • After 65°C, more β-sheet structures are formed that correlate with the generation of aggregation of protein.
  • At 70°C, HSA undergoes self-assembly to form fibrillar structures.
  • Below 74°C, the rate of the irreversible process is very slow.
  • The hydrodynamic radius of HSA increases four times at around 75°C. This means more volume.

Conclusion: at 75°C, our proteins' self-assembly is irreversible, but we haven't overcooked them.

* 75°C = 167°F

Before and After Pictures

Published Literature

We're working longevity studies, but for now here are several studies on the unfolding of HSA:


» Temperature Behavior of HSA - 1979

Rolf WETZEL, Manfred BECKER, Joachim BEHLKE, Heidi BILLWITZ, Siegfried BOHM, Bernd EBERT, Harald HAMANN, Johannes KRUMBIEGEL, and Giinter LASSMANN

» Reversible Denaturation of HSA - 1972

KNUT WALLEVIK - From the Department of Chemistry, University of Oregon, Eugene, Oregon 97403, and The Finsen Laboratory, The Finsen Institute, Copenhagen, Denmark

» Transition from native to unfolded aggregated state of HSA - 2014

Nirmal Kumar Das, Narayani Ghosh, Ajit Prabhakar Kale, Ramakanta Mondal, Uttam Anand, Subhadip Ghosh, Virendra Kumar Tiwari, Manmohan Kapur, and Saptarshi Mukherjee

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