Keratin Protein Technology

Keratin Is a Class of Protein That Helps Heal Wounds

Long known to be a critical structural component of the skin, keratins are a family of fibrous proteins that are plentiful in both the epidermis (first) and dermis (second) layers of the skin. Ubiquitous in nature, these proteins exist in hair, nails, horn, hoofs, wool, feathers, and epithelial cells. In addition to its vital role as a physical structure, research into keratin function at some of the world’s leading medical universities has identified the crucial biological role that keratin proteins play in the wound- healing process.

Keratin Proteins Regulate Key Cellular Activities

Keratins are the major proteins in keratinocytes and are essential for cell migration and upregulation of keratin expression in response to wounding.1 Keratin proteins serve important structural and protective functions, particularly in the epithelium, where they act to stabilize the cell against mechanical stress as well as hydrate the skin and provide a waterproof barrier.2

In laboratory tests, Keratin proteins have been shown to regulate key cellular activities. They are able to signal to cells in the skin (keratinocytes and fibroblasts) in a way that effects their migration and proliferation. This is a critical component necessary for wound healing.3,4

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Innovation Unfolds—Our Proprietary Replicine™ Bioactive Keratin® Technology

At Molecular Biologicals, we have developed a unique, proprietary, evidence-based technology called Replicine™ Bioactive Keratin—a manufacturing process whereby keratin is carefully extracted from sheep’s wool while keeping the form and the function of the keratin protein intact, thereby maintaining its bioactivity. In essence, we have discovered the scientific attributes of an intact bioactive molecule, which is the essential factor for healing wounds.

1. It Starts at the Source—Pure New Zealand Wool

Keratin is extracted from a sustainable, renewable natural resource—pure New Zealand sheep’s wool, a 100% natural material harvested by shearing during the spring months. No animals are harmed at any stage of the wool harvesting process.


2. Maintaining Form and Function—The Effect of Replicine™ Bioactive Keratin

With our unique proprietary Replicine™ Bioactive Keratin process, we have isolated the intermediate filament protein and extracted it from the structure intact without breaking important bonds within the protein. When extracted in its intact form, keratin has extremely high levels of bioactivity.


The amino acids in keratins are linked in a particular sequence, coiling together to build strong protein networks.



Our Replicine™ Bioactive Keratin process allows us to maintain the form and function of the protein as well as its bioactivity, the main factor needed for healing.



This has the effect of increasing the rates of proliferation and migration of keratinocyte cells present in the wound, stimulating them to quickly enter a hyperproliferative phase.


This accelerates epithelialization, essential for wound healing.2

It also has the effect of increasing levels of collagen IV and VII, critical for basal membrane integrity.2,5


3. The Art of Transformation—Creating a Versatile Biopolymer

Our Replicine™ Bioactive Keratin technology allows us to control the molecule, creating a versatile biopolymer material that can be formed into a liquid, gel, or solid.



1.Sussman G. Advances in wound dressing technology. Wounds Int. 2013;4(4):12-14. 2. Jina NH, Marsh C, Than M, et al. Keratin gel improves poor scarring following median sternotomy. ANZ J Surg. 2015;85(5):378-380. 3. Pechter PM, Gil J, Valdes J, et al. Keratin dressings speed epithelialization of deep partial-thickness wounds. Wound Rep Reg. 2012;20:236-242. 4. Batzer AT, Marsh C, Kirsner RS. The use of keratin-based wound products on refractory wounds. Int Wound J. 2016;13(1):110-115. 5. Loan F, Cassidy S, Marsh C, et al. Keratin-based products for effective wound care management in superficial and partial thickness burns injuries. Science Direct.2016;42:541-547.