Collagen-I Mouse
Mouse tail tendon.
Filtered White lyophilized (freeze-dried) powder.
> 90.0%.
Description
Mouse Collagen-I is a natural protein purified from Mouse tail tendon. Collagen-I is purified by proprietary chromatographic techniques.
Product Specs
Collagen is a fibrous protein that forms a major part of the extracellular matrix, providing structural support and tensile strength to tissues. Collagen and its derivative, gelatin, have a long history of use in various fields, including medicine, pharmaceuticals, and consumer products, dating back over a century. Derived from animal sources, these materials are readily available and cost-effective. However, conventional formulations often lack high purity levels and may trigger inflammatory responses in certain individuals. Concerns have also been raised regarding potential contamination of bovine-derived products with infectious agents, such as the prion responsible for mad cow disease and its human counterpart, Creutzfeldt-Jakob Disease. Animal-derived collagens undergo extensive modifications throughout their lifespan in the extracellular matrix, impacting their extractability and biophysical properties. Consequently, collagens extracted from tissues exhibit significant batch-to-batch variability and can be challenging to analyze comprehensively. Products containing animal-derived collagen carry the risk of eliciting adverse inflammatory or immune reactions in humans and may harbor viruses or prions, which are potentially life-threatening pathogens. In contrast, recombinant collagens closely resemble native collagen proteins, minimizing the likelihood of inflammation, immune responses, and disease transmission compared to animal-sourced collagen.
Mouse Collagen-I is a naturally occurring protein extracted from the tail tendon of mice. The purification process involves specialized chromatographic methods.
This product appears as a white, lyophilized (freeze-dried) powder that has been filtered.
The lyophilization process of Collagen-I does not include any additional substances.
To create a working stock solution, it is advisable to dissolve the lyophilized powder in 0.5 M acetic acid at a pH of 3, maintaining a temperature of 4°C. The resulting solution should have a concentration of at least 100 µg/ml. This stock solution can be further diluted with other aqueous solutions as needed.
While lyophilized Collagen-I remains stable at room temperature for up to three weeks, it is recommended to store it in a dry environment below -18°C. Once reconstituted, Collagen-I should be stored at 4°C for a period of 2 to 7 days. For long-term storage, it is advisable to store it below -18°C. To enhance stability during extended storage, the addition of a carrier protein such as 0.1% HSA or BSA is suggested. It is crucial to avoid repeated freeze-thaw cycles to maintain product integrity.
The purity of this product exceeds 90.0%.
Mouse tail tendon.
Product Science Overview
Collagen Type I is a fibrillar collagen composed of two α1(I) chains and one α2(I) chain, forming a triple helix structure. This unique structure provides high tensile strength, making it essential for the mechanical stability of tissues . The triple helix is approximately 300 nm long and 1.5 nm in diameter .
Mouse Collagen-I serves several critical biological functions:
- Structural Support: It provides mechanical strength to tissues, enabling them to withstand stretching and pressure.
- Cell Adhesion: It facilitates cell attachment, migration, and differentiation, which are vital for tissue repair and regeneration .
- Wound Healing: Collagen Type I is a major component of the extracellular matrix (ECM) and plays a significant role in wound healing by promoting the formation of new tissue .
The synthesis and degradation of Collagen Type I are tightly regulated processes involving several enzymes and signaling pathways:
- Procollagen Processing: Collagen Type I is initially synthesized as procollagen, which undergoes cleavage of its propeptides to form mature collagen .
- Cross-Linking: Enzymes such as lysyl oxidase facilitate the formation of covalent cross-links between collagen molecules, enhancing the stability and strength of the collagen fibers .
Mouse Collagen-I is widely used in various research and medical applications:
- Cell Culture: It is used as a substrate to promote cell attachment, proliferation, and differentiation in vitro .
- Tissue Engineering: Collagen scaffolds are employed in tissue engineering to support the growth and development of new tissues .
- Disease Models: Mouse models with altered Collagen Type I expression are used to study diseases such as osteogenesis imperfecta and Ehlers-Danlos syndrome .
