Human cartilage.
Filtered White lyophilized (freeze-dried) powder.
> 95.0%.
Human Collagen-II is a natural protein purified from human cartilage. Collagen- II is purified by proprietary chromatographic techniques.
Collagen, a key structural protein in various tissues, is widely used in diverse industries due to its strength-giving properties. Derived from animals, collagen and its counterpart gelatin are readily available and cost-effective. However, the purity of these materials can vary, potentially leading to inflammatory reactions. Concerns regarding contamination, particularly with prions associated with bovine spongiform encephalopathy (BSE), have emerged. Natural variations in animal collagen due to factors like age and diet contribute to inconsistencies between batches. These inherent limitations can pose challenges in product quality control and safety. Recombinant collagens offer a safer and more consistent alternative, minimizing the risk of immune responses and contamination.
Human Collagen-II, sourced from human cartilage, undergoes a purification process using specialized chromatographic methods.
White, freeze-dried powder that has been filtered.
The lyophilization process of Collagen-I was carried out without the addition of any other substances.
To prepare a stock solution, it is advised to dissolve the lyophilized powder in 0.5 M acetic acid at a pH of 2.5 to achieve a concentration of at least 100 µg/ml. This solution can then be further diluted in other aqueous solutions as needed.
Lyophilized Collagen-II remains stable at room temperature for up to 3 weeks. For extended storage, it should be kept dry and below -18°C. After reconstitution, Collagen-II should be stored at 4°C for a maximum of 2-7 days. For long-term storage, freezing below -18°C is recommended. The addition of a carrier protein (0.1% HSA or BSA) is advised for long-term storage. Repeated freezing and thawing should be avoided.
Greater than 95.0% pure.
Human cartilage.
Introduction Collagen is the most abundant protein in the human body, accounting for approximately 25% of the body’s protein mass . It is a major component of connective tissues such as skin, muscles, tendons, and cartilage. Collagen type II, specifically, is a crucial protein that plays a significant role in maintaining the structural integrity of cartilage.
Structure and Composition Collagen type II is a fibril-forming collagen that is primarily found in cartilage, the vitreous body of the eye, and the nucleus pulposus of intervertebral discs . It is composed of three identical alpha chains that form a triple helix structure, providing high tensile strength and resistance to compression . This structure is essential for the proper functioning of cartilage, as it allows the tissue to withstand mechanical stress and maintain its shape.
Synthesis and Regulation The synthesis of collagen type II involves several steps, starting with the production of precursor molecules called procollagens. These procollagens undergo post-translational modifications, including hydroxylation and glycosylation, before being secreted into the extracellular matrix . Once in the extracellular matrix, the procollagens are cleaved to form mature collagen molecules, which then assemble into fibrils.
Chondrocytes, the cells found in cartilage, play a key role in the synthesis and regulation of collagen type II . These cells produce the necessary enzymes and cofactors required for collagen synthesis, including vitamin C, which is essential for the hydroxylation of proline and lysine residues .
Function and Importance Collagen type II is the main structural component of hyaline cartilage, which covers the ends of bones in joints and provides cushioning and support . This type of cartilage is essential for reducing friction between bones and allowing smooth joint movement. Collagen type II also contributes to the overall stability and strength of cartilage, making it crucial for maintaining joint health.
In addition to its structural role, collagen type II has been shown to play a role in cell adhesion and signaling . It interacts with various cell surface receptors, influencing cell behavior and contributing to the maintenance of normal tissue architecture and function.
Clinical Relevance The degradation of collagen type II is associated with several joint disorders, including osteoarthritis and rheumatoid arthritis . In these conditions, the breakdown of collagen leads to the loss of cartilage integrity, resulting in pain, inflammation, and reduced joint function. Understanding the role of collagen type II in these diseases has led to the development of therapeutic strategies aimed at preserving or restoring cartilage health.