Telopeptide is a non-helical structure at both ends of the collagen molecule and is thought to be involved in intermolecular bonding and allergenic reaction due to antigenicity. Removing the telopeptides from collagen by protease treatment produces atelocollagen whose characteristics are superior purity and stability. We have produced atelocollagen-based medical devices for more than 30 years.

The size is approximately 300 nm in length and 1.5 nm in width, and the molecular weight is approximately 300,000.
Collagen is composed of three molecular chains that form a triple helical structure.
The molecular chain is a polypeptide consisting of approximately 1000 amino acids bound together in a unique amino acid sequence of collagen repeating [Gly-X-Y].
Phenylalanine, histidine, proline, glutamic acid, and leucine are primarily in the X position, whereas hydroxyproline and hydroxylysine are typically found in the Y position.

The source of collagen is bovine dermis and therefore both products contain approximately 95% type I collagen and roughly 5% type III and type V collagen.

3D Ready Atelocollagen DMEM-LG (Low Glucose) contains 1,000 mg/ml of glucose, and 3D Ready Atelocollagen DMEM-HG (High Glucose) contains 4,500 mg/ml of glucose.

After the initial thaw, the product can be kept refrigerated for one month. For long-term storage, dispense a small amount at the time of initial thaw and store frozen. Freeze-thawing should be avoided because it affects the gel-forming capacity.

It can be diluted by adding serum-free medium (e.g. DMEM) under ice-cold conditions and then mixing slowly* without whisking.
Note, however, more dilute the product is, the less viscous it becomes and the longer it takes to form a gel, while cells are more likely to accumulate.
*Swirling agitator (rotator) at 4 rpm for 20 min, etc.

Please visit our distributors’ page to download an instruction manual.

Atelocollagen has been used to culture primary mouse small intestinal organoids, primary mouse mammary organoids, and organoids from human brain tumor stem cell lines.

Because each cell is at a different height in the gel, the microscope cannot focus on every cell; however, the morphology of individual cells can be observed.
If you want to culture cells at a certain height, consider sandwich culture in which a collagen gel without cells is formed first, cells are seeded on top of the collagen gel, and then another layer of collagen gel is added.

The graph below shows a representative measurement of compressive strength.
Plastic petri dishes and plates for culture are much stronger compared to tissues.
On the other hand, the strength of the atelocollagen gel is closer to that of native tissue and decreases at lower collagen concentrations.
If you are interested, please also see the video about the collagen gels.

Source of illustration: ©2016 DBCLS TogoTV / CC-BY-4.0

Similar to tissue samples, collagen gel can be fixed and/or embedded in paraffin/OCT compound. Please visit our distributors’ page to download an instruction manual.

The extract obtained by lysing the cells together with the gel using lysis buffer can be analyzed by western blotting as is. If the protein of interest cannot be detected, the collagen gel should be lysed in advance using collagenase*.
*Commercially available collagenase for cell dispersion contains a wide variety of proteases; therefore, ensure that the collagenase you use does not contain an enzyme that degrades the target protein.

We can provide a collagen solution equivalent to that used in manufacturing our atelocollagen-based medical devices as a made-to-order research product. Alternatively, a high concentration collagen solution can be prepared from Atelocollagen powder (Cat No. CLP-01).

Our collagen solution does not contain cell-derived physiologically active compounds, nucleic acids, matrix metalloproteinase (MMP), etc., which could affect the results of your experiment. Unlike soluble basement membrane extracts, we confirm the lot-to-lot consistency of our collagen products.