COMP Human
HEK293 Cells.
Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1, Thrombospondin-5
Sterile filtered colorless solution.
Greater than 85.0% as determined by SDS-PAGE.
Description
COMP Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 749 amino acids (21-757a.a) and having a molecular mass of 82.4kDa.
COMP is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
COMP, a large glycoprotein, plays a crucial role in cartilage health. As a member of the thrombospondin family, this non-collagenous protein is found abundantly in the extracellular matrix of various cartilaginous tissues like articular, nasal, and tracheal cartilage. Its presence extends to other tissues such as synovium and tendon. COMP forms a pentameric structure, with each subunit contributing to its high molecular weight exceeding 500kDa. This protein exhibits calcium-binding properties. The carboxy-terminal globular domain of COMP interacts with collagen types I, II, and IX, highlighting its importance in maintaining the structural integrity and characteristics of the collagen network. Additionally, COMP serves as a reservoir and transporter for signaling molecules like vitamin D. Genetic mutations affecting COMP are linked to skeletal disorders like Pseudoachondroplasia and certain types of multiple epiphyseal dysplasia, emphasizing its crucial role in skeletal development and function.
Recombinant human COMP, produced in HEK293 cells, is a single polypeptide chain that has been glycosylated. This protein consists of 749 amino acids (specifically, residues 21 to 757), resulting in a molecular weight of 82.4kDa. To facilitate purification, a 6-amino acid His tag is attached to the C-terminus. The purification process utilizes proprietary chromatographic methods to ensure high purity.
The appearance of the solution is a clear and colorless liquid that has been sterilized by filtration.
The COMP solution is provided at a concentration of 0.5mg/ml and is prepared in a phosphate buffered saline solution (pH 7.4) containing 10% glycerol.
For short-term storage (up to 2-4 weeks), the COMP solution should be stored at a refrigerated temperature of 4°C. For extended storage, it is recommended to store the solution in a frozen state at -20°C. To further enhance stability during long-term storage, the addition of a carrier protein like HSA or BSA (at a concentration of 0.1%) is advisable. To maintain the quality of the protein, it is crucial to minimize the number of freeze-thaw cycles.
The purity of this product is determined using SDS-PAGE analysis and is guaranteed to be greater than 85.0%.
Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1, Thrombospondin-5
HEK293 Cells.
ADPDAHSLWY NFTIIHLPRH GQQWCEVQSQ VDQKNFLSYD CGSDKVLSMG HLEEQLYATD AWGKQLEMLR EVGQRLRLEL ADTELEDFTP SGPLTLQVRM SCECEADGYI RGSWQFSFDG RKFLLFDSNN RKWTVVHAGA RRMKEKWEKD SGLTTFFKMV SMRDCKSWLR DFLMHRKKRL EPTAPPTMAP GLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH
Product Science Overview
COMP is a large, pentameric glycoprotein with a molecular weight of approximately 550 kDa. It belongs to the thrombospondin gene family and is characterized by its disulfide-linked structure. The protein contains several domains, including epidermal growth factor-like repeats and calcium-binding repeats, which are essential for its function .
COMP is primarily involved in the assembly and stabilization of the extracellular matrix in cartilage. It binds to various matrix components, including collagen types I, II, and IX, and matrilins . This binding capability is crucial for maintaining the structural integrity of cartilage and facilitating chondrogenesis, the process by which cartilage is formed .
COMP is present during the early stages of human limb development and continues to play a role in maintaining healthy cartilage throughout life . However, its expression is significantly upregulated in conditions such as osteoarthritis (OA) and rheumatoid arthritis (RA) . In OA, COMP is secreted by chondrocytes and is often associated with collagen fibers in the cartilage matrix . Elevated levels of COMP have been detected in the serum and synovial fluid of patients with OA, making it a potential biomarker for the disease .
The human recombinant form of COMP is produced using recombinant DNA technology, which involves inserting the COMP gene into a host cell to produce the protein. This recombinant protein is used in various research applications to study its structure, function, and role in diseases. It is also utilized in developing therapeutic strategies for cartilage-related disorders .
Due to its involvement in cartilage integrity and disease, COMP has garnered significant interest as a potential therapeutic target. Research has shown that COMP can induce arthritis in animal models, providing insights into the pathogenesis of RA . Additionally, its role as a biomarker for musculoskeletal diseases like knee OA highlights its diagnostic potential .
