RUIMEI
Triple Helix Structure

World's First
Regenerative Human Collagen

Engineered using our patented in vitro tissue regeneration technology — a 100% human-derived collagen matrix that closely mirrors the architecture and function of the body's own tissue. Not recombinant. Not animal-derived. Genuinely human.

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REGENERATED HUMAN COLLAGEN INTACT TRIPLE HELIX STRUCTURE NO IMMUNO- GENICITY BATCH-TO-BATCH STABILITY TYPE I COLLAGEN CHAIN LENGTH PURITY NO CYTO- TOXICITY
Why Human-Derived Matters

ENGINEERED TO OVER-
COME CONVENTION

HOVER OVER EACH ADVANTAGE TO EXPLORE THE STRUCTURAL AND BIOLOGICAL PROPERTIES THAT SET REGENECOLLA™ APART FROM ANIMAL-DERIVED AND RECOMBINANT ALTERNATIVES.

Intact Triple Helix Structure
The hallmark of native collagen — a right-handed triple helix of three polypeptide α-chains — is fully preserved. This intact architecture is the prerequisite for proper cell–receptor binding, mechanical resilience, and bioactive signalling.
No Immunogenicity
Human-homologous design means the immune system recognises this collagen as structurally "self" — dramatically reducing immune reactivity, calcification, and chronic inflammatory response.
Batch-to-Batch Stability
Controlled in vitro cellular expression delivers reproducible structural characteristics across every lot — eliminating variability and ensuring predictable, consistent clinical outcomes.
Type I Collagen Chain Length
Authentic human fibroblasts produce Type I/III collagen with full-sequence active gene sites and precise α-chain lengths — preserving structural integrity lost in conventional extraction or recombinant systems.
Exceptional Molecular Purity
Advanced GMP-aligned purification ensures freedom from residual cellular debris, endotoxins, and non-collagenous protein contaminants — protecting both safety profiles and formulation stability.
No Cytotoxicity
100% human-derived collagen eliminates cytotoxic contamination and zoonotic transmission risks inherent to bovine, porcine, and marine processing. GMP-aligned from seed cell to final lot.

Produced through tissue engineering and in vitro cellular expression techniques, our regenerated human collagen cultivates authentic human cells that produce the exact structural characteristics and biological functions of the body's native collagen — including Type I/III collagen with full-sequence active gene sites and precise chain lengths.

Human Skin Tissue Laboratory

Intact Triple-Helix
Confirmed

CD Spectroscopy SDS-PAGE

Comprehensive analytical characterisation — circular dichroism (CD) spectroscopy and SDS-PAGE — confirms that our regenerated human collagen preserves a native-like triple-helical conformation with full-length polypeptide chains intact.

Circular Dichroism
SDS-PAGE

The CD spectrum displays the signature collagen profile — confirming a perfectly folded native triple-helix structure with characteristic optical activity bands consistent with natural human Type I collagen.

Negative Band 198 nm  −33.71 mdeg
Positive Band 221.5 nm  +3.21 mdeg
Interpretation Native Helix — Confirmed

Distinct α1 and α2 bands matching the molecular weight profile of native human collagen precisely — validating full-length, native-like polypeptide chains and an unparalleled structural fidelity marker.

α1
~138 kDa
α2
~128 kDa

Matches native human collagen molecular weight — precisely.

Four-Level Fibrillar Architecture
Four-Level
Fibrillar
Architecture
i

Under high-resolution electron microscopy, our collagen reveals a hierarchical fibrillar architecture that closely resembles native human Type I collagen — including higher-order supramolecular assembly.

"The world's first tissue-engineered collagen —
structurally indistinguishable from what the body itself makes."

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