A primer on finding the right collagen for your 3D bioprinting workflows.
Being the most abundant protein in mammals has earned collagen a special status in tissue engineering labs. But recent global supply chain disruptions have made finding a reliable supplier to ensure consistent results a truly Herculean race against time. Thankfully, Advanced BioMatrix and CELLINK offer over 30 collagen I products, and our well-oiled pipeline is well poised to minimize disruptions to research that calls for bioengineering with collagen. Here’s a quick cheat sheet on the essentials of bioprinting with this hydrogel and where to find more resources.
The most common collagen types for bioprinting
With 28 collagens having been identified in vertebrates, finding the right collagen for your research might feel as daunting as choosing one bag in the entire grocery aisle dedicated to potato chips. Advanced BioMatrix and CELLINK sell more than 30 collagen I products, making us the world’s largest supplier of collagen I. We also offer types II, III and IV. Here’s a breakdown of the tissue engineering applications for all four.
|Type I Collagen||All tissues and organs||Bovine, rat, human||Solution, powder, sponge, EZ Gel, lyophilized, UV crosslinkable (over 30 products)|
|Type II Collagen||Cartilage, vitreous humor of the eye||Bovine||Sterile solution|
|Type III Collagen||Skin, blood vessels, other organs||Human||Powder, solution|
|Type IV Collagen||Extracellular basement membranes||Human||Powder, lyophilized powder|
What is collagen I?
In short, collagen I is a major structural component of skin, bone, tendon, and other connective tissues. A defining property is that it forms fibrous networks that enhance the structural integrity of the extracellular matrix (ECM) and promote cell adhesion, growth and tissue morphogenesis. Tissue engineers often grow cells inside collagen hydrogels to better replicate the in vivo environment of specific tissues.
What are the different types of collagen extractions?
Collagen extracted with enzymes maintains the triple-helix construction but cleaves the telopeptide regions.
Collagen extracted with acid maintains the triple helix and leaves the telopeptide regions intact.
In the end, telocollagens achieve gelation quicker and produce a stronger hydrogel than atelocollagens of the same concentration.
Does collagen concentration matter in bioprinting?
Collagen formulations with a higher concentration tend to gel quicker and form stronger, stiffer hydrogels. Stiffer hydrogels contribute to the structural integrity of a construct, which is of particular importance when it comes to load-bearing scenarios such as bone tissue engineering. Plus, hydrogel stiffness, like ECM stiffness, impacts a wide variety of cellular pathways, including propagation, differentiation, lineage specification, gene expression, morphology, self-renewal, pluripotency and migration. Using collagen hydrogels with stiffnesses similar to native tissue is critically important, and these can be fine-tuned by controlling the collagen concentration.
Did you know?
Go More In-depth
Download this informative ebrochure on collagen I stiffness.
Over 35 FAQ videos
Explore a trove of informative videos about collagen on Advanced BioMatrix’s YouTube channel.