Cartilage Oligomeric Matrix Protein Human HEK293

Introduction to the Molecule

Cartilage oligomeric matrix protein (COMP), also designated thrombospondin 5 (TSP 5), is non-collagenous glycoprotein and is a member of the thrombospondin family of extracellular proteins. COMP is a calcium-binding protein of high molecular weight (>500kDa) present in the extracellular matrix of articular, nasal and tracheal cartilage. COMP is not only cartilage-derived but was found widely in other tissues, including synovium and tendon. Intact COMP is pentameric, with five identical subunits and the carboxy-terminal globular domain of native COMP binds to collagens I, II, and IX. It has been proposed that COMP molecules are important for maintaining the properties and integrity of collagen network. In addition COMP may have a storage and delivery function for hydrophobic cellsignaling molecules such as vitamin D. The significance of COMP for normal development and function of cartilage has been underscored by the discovery that mutations of the COMP gene result in pseudoachondro­plasia and some forms of multiple epiphyseal dysplasia. Most published studies have shown that serum levels of COMP provide important information about metabolic changes occurring in the cartilage matrix in joint disease. These studies describe that serum COMP level correlated with cartilage degradation and is a potential prognostic marker in inflammatory joint diseases such as osteoarthritis (OA) and rheumatoid arthritis (RA). Results have demonstrated an association of increasing serum COMP levels with progressive destruction of articular cartilage monitored radiographically. OA and RA are a common disease causing pain and disability in a significant proportion of the adult population and early diagnostics of these diseases is very important for future therapy.

Research topic

Bone and cartilage metabolism

Description

Total 750 AA. MW: 82.4 kDa (calculated). N-Terminal FLAG-tag, 13 extra AA (highlighted). Protein identity confirmed by LC-MS/MS.

Amino Acid Sequence

Source

HEK293

Purity

Purity as determined by densitometric image analysis: >90%

SDS-PAGE gel

10% SDS-PAGE separation of Human COMP 1. M.W. marker – 21, 31, 45, 66, 97 kDa 2. reduced and boiled sample, 5μg / lane 3. non-reduced and non-boiled sample, 5μg / lane

Endotoxin

< 1.0 EU/ug

Formulation

Filtered (0.4 μm) and lyophilized from 0.5 mg/ml in 20mM Tris buffer, 50mM NaCl, pH 7.5

Reconstitution

Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

Storage, Stability/Shelf Life

Store lyophilized protein at –20°C. Lyophilized protein remains stable until the expiry date when stored at –20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80°C for long term storage. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Applications

Cell culture and/or animal studies, ELISA, Western blotting

Note

This product is intended for research use only. The Certificate of Analysis is available on www.biovendor.com

Physical Appearance

Filtered (0.4 μm) white lyophilized (freeze-dried) powder.

References

• Collette JH, Ethgen O, Rovati LC, Giacovelli G, Henrotin YE, Seidel L, Reginster JY, Bruyere O. Biochemical markers of bone and cartilage remodeling in prediction of longterm progression of knee osteoarthritis. J Rheumatol. 2003 May;30 (5):1043-50
• Dragomir AD, Kraus VB, Renner JB, Luta G, Clark A, Vilim V, Hochberg MC, Helmick CG, Jordan JM. Serum cartilage oligomeric matrix protein and clinical signs and symptoms of potential pre-radiographic hip and knee pathology. Osteoarthritis Cartilage. 2002 Sep;10 (9):687-91
• Kraus VB, Helmick CG, Hochberg MC, Vilim V, Dragomir AD, Renner JB, Stabler T, Luta G, Jordan JM. Ethnic and sex differences in serum levels of cartilage oligomeric matrix protein: the Johnston County Osteoarthritis Project. Arthritis Rheum. 2003 Mar;48 (3):675-81
• Misumi K, Vilim V, Clegg PD, Thompson CC, Carter SD. Measurement of cartilage oligomeric matrix protein (COMP) in normal and diseased equine synovial fluids. Osteoarthritis Cartilage. 2001 Feb;9 (2):119-27
• Pavelka K, Kraus VB, Gatterova J, Machacek S, Olejarova M, Vilim V. Serum levels of cartilage oligomeric matrix protein (COMP) correlate with radiographic progression of knee osteoarthritis. Osteoarthritis Cartilage. 2002 Sep;10 (9):707-13
• Pavelka K, Kraus VB, Prochazka B, Gatterova J, Machacek S, Olejarova M, Vytasek R, Vilim V. Serum cartilage oligomeric matrix protein reflects the presence of clinically diagnosed synovitis in patients with knee osteoarthritis. Osteoarthritis Cartilage. 2001 Oct;9 (7):612-8
• Pavelka K, Kraus VB, Tchetverikov I, Vytasek R, Senolt L, Voburka Z, Vilim V. Monoclonal antibodies to human cartilage oligomeric matrix protein: epitope mapping and characterization of sandwich ELISA. Clin Chim Acta. 2003 Feb;328 (1-2):59-69
• Skoumal M, Haberhauer G, Feyertag J, Kittl EM, Bauer K, Dunky A. Serum levels of cartilage oligomeric matrix protein are elevated in rheumatoid arthritis, but not in inflammatory rheumatic diseases such as psoriatic arthritis, reactive arthritis, Raynaud's syndrome, scleroderma, systemic lupus erythematosus, vasculitis and Sjogren's syndrome. Arthritis Res Ther. 2004;6 (2):73-4
• Vilim V, Lenz ME, Vytasek R, Masuda K, Pavelka K, Kuettner KE, Thonar EJ. Characterization of monoclonal antibodies recognizing different fragments of cartilage oligomeric matrix protein in human body fluids. Arch Biochem Biophys. 1997 May 1;341 (1):8-16

By research topic:

• Bone and cartilage metabolism

By molecule:

• Cartilage Oligomeric Matrix Protein