Recombinant Human COL2A1, N-His

Reference: YHB97501
Product nameRecombinant Human COL2A1, N-His
Uniprot IDP02458
Origin speciesHomo sapiens (Human)
Expression systemProcaryotic expression
Protein delivered with Tag?N-Terminal His Tag
Buffer0.01M PBS, pH 7.4.
Delivery conditionDry Ice
Storage condition4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Host speciesEscherichia coli (E.coli)
Aliases /SynonymsCOL2A1, Collagen alpha-1(II) chain, Alpha-1 type II collagen
NoteFor research use only

Description of Recombinant Human COL2A1, N-His


Recombinant human col2a1, also known as collagen type II alpha 1, is a protein that plays a crucial role in the structure and function of cartilage and other connective tissues in the body. This protein has been extensively studied for its potential therapeutic applications in various diseases, making it a promising drug target.

Structure of Recombinant Human Col2a1

Recombinant human col2a1 is a homotrimeric protein, meaning it is made up of three identical subunits. Each subunit consists of approximately 1,400 amino acids and has a molecular weight of around 150 kDa. The primary structure of col2a1 is characterized by the presence of repeating triple-helical domains, with a characteristic Gly-X-Y sequence. These domains are responsible for the protein’s unique triple-helical structure, which gives it its strength and stability.

The secondary structure of col2a1 is predominantly helical, with a small amount of beta-sheet structure. The tertiary structure is a tightly coiled triple-helix, with three polypeptide chains intertwined. This structure provides the protein with its tensile strength and resistance to mechanical stress.

Activity of Recombinant Human Col2a1

The main function of col2a1 is to provide structural support to connective tissues, particularly in cartilage. It is the most abundant protein in cartilage, making up approximately 75% of its dry weight. Col2a1 is responsible for the tensile strength and elasticity of cartilage, allowing it to withstand mechanical stress and maintain its shape.

In addition to its structural role, col2a1 also plays a crucial role in the maintenance and repair of cartilage. It is involved in the synthesis and deposition of new cartilage matrix, as well as the regulation of chondrocyte function. Chondrocytes are the cells responsible for producing and maintaining cartilage, and col2a1 is essential for their proper functioning.

Application as a Drug Target

Given its crucial role in cartilage structure and function, recombinant human col2a1 has been identified as a potential drug target for various diseases. One of the most significant applications of col2a1 is in the treatment of osteoarthritis, a degenerative joint disease characterized by the breakdown of cartilage. By targeting col2a1, it is possible to slow down the progression of osteoarthritis and potentially even repair damaged cartilage.

Col2a1 has also been studied as a potential target for the treatment of other joint disorders, such as rheumatoid arthritis and juvenile idiopathic arthritis. In these conditions, the immune system attacks the cartilage, leading to inflammation and joint damage. By targeting col2a1, it may be possible to prevent or slow down the destruction of cartilage and improve joint function.

Furthermore, recombinant human col2a1 has shown potential in the treatment of intervertebral disc degeneration, a common cause of back pain. By promoting the synthesis and deposition of new cartilage matrix, col2a1 may help to repair damaged discs and alleviate symptoms.


In conclusion, recombinant human col2a1 is a crucial protein involved in the structure and function of cartilage and other connective tissues. Its unique triple-helical structure and activity make it a promising drug target for various diseases, particularly those affecting the joints. Further research and development of col2a1-based therapies could potentially lead to more effective treatments for these conditions.


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