Triple Helix Structure

Human Collagen
Engineered for Structural Fidelity

Developed through a proprietary in-vitro tissue-regeneration platform, RégénéColla™ is a human-cell-derived collagen matrix characterised from chain profile to triple-helix conformation and fibrillar organisation. A rigorous approach to structural biomaterials.

RÉGÉNÉCOLLA™ HUMAN COLLAGEN INTACT TRIPLE HELIX PROFILE BIOLOGICAL COMPATIBILITY LOT-TO-LOT CONSISTENCY DEFINED TYPE I CHAIN PROFILE CONTROLLED PURITY CYTOCOMPAT- IBILITY
Intact Triple-Helix Profile
The triple helix is a defining feature of collagen. RégénéColla™ is assessed for a right-handed triple-helical profile using structural methods that should be interpreted together with the approved analytical report.
Biological Compatibility
A human-cell-derived source avoids the cross-species origin of bovine, porcine and marine collagen. Biological compatibility still depends on the final product, route of use and product-specific evaluation.
Lot-to-Lot Consistency
Controlled in-vitro production and defined downstream processing are designed to support reproducible material attributes. Lot consistency is evaluated against the approved specification.
Defined Type I Chain Profile
The reported SDS-PAGE profile shows distinct α1 and α2 bands at approximately 116 kDa and 97 kDa, supporting the stated Type I collagen chain profile.
Controlled Purification
Downstream purification is designed to control cellular residues, endotoxin and non-collagenous process impurities. Release limits should be read from the specification for the relevant material grade.
Cytocompatibility Assessed
Cytocompatibility is assessed within the quality and preclinical programme for the relevant product. Test method, sample identity and acceptance criteria are necessary for interpreting the result.

RégénéColla™ is produced through tissue engineering and controlled in-vitro human-cell culture, followed by downstream purification and structural characterisation. This page explains how the material is made and assessed; performance and clinical claims remain specific to the final product and approved use.

Human Skin Tissue Laboratory

Structural Identity
Assessed

CD Spectroscopy SDS-PAGE
Circular Dichroism
SDS-PAGE

The reported CD profile shows a negative band at 198 nm and a positive band at 221.5 nm, a pattern presented as consistent with triple-helical collagen conformation.

Negative Band 198 nm  −33.71 mdeg
Positive Band 221.5 nm  +3.21 mdeg
Interpretation Triple-Helix Profile — Consistent

The reported SDS-PAGE profile shows distinct α1 and α2 bands at approximately 116 kDa and 97 kDa, supporting the stated Type I collagen chain profile.

α1
~116 kDa
α2
~97 kDa

Chain profile consistent with the reported Type I collagen reference.

Four-Level Collagen Architecture

AMINO ACID SEQUENCE

Collagen’s primary structure is defined by Gly-X-Y repeats. Product-specific sequence identity and coverage should be read together with the approved analytical report.

Amino Acid Sequence Triple-Helix Conformation Fibril Formation Extracellular Matrix Network