Cartilage Oligomeric Matrix Protein Human CHO
| Type: Recombinant | |||||
| Source: CHO | Species: Human | ||||
| Other names: COMP, Thrombospondin-5, TSP5 | Product of BioVendor | ||||
| Product: | Size: | ||||
|---|---|---|---|---|---|
| RGB002 | 0.1 mg | ||||
Files:
Datasheet PDF
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Product details
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 783 AA. MW: 85.75 kDa (calculated). C-Terminal His-tag+myc-epitope
Amino Acid Sequence
AAQPARRAVR SFCVLLLTLA ALGASGQGQS PLGSDLGPQM LRELQETNAA LQDVRELLRQ QVREITFLKN TVMECDACGM QQSVRTGLPS VRPLLHCAPG FCFPGVACIQ TESGARCGPC PAGFTGNGSH CTDVNECNAH PCFPRVRCIN TSPGFRCEAC PPGYSGPTHQ GVGLAFAKAN KQVCTDINEC ETGQHNCVPN SVCINTRGSF QCGPCQPGFV GDQASGCQRR AQRFCPDGSP SECHEHADCV LERDGSRSCV CAVGWAGNGI LCGRDTDLDG FPDEKLRCPE RQCRKDNCVT VPNSGQEDVD RDGIGDACDP DADGDGVPNE KDNCPLVRNP DQRNTDEDKW GDACDNCRSQ KNDDQKDTDQ DGRGDACDDD IDGDRIRNQA DNCPRVPNSD QKDSDGDGIG DACDNCPQKS NPDQADVDHD FVGDACDSDQ DQDGDGHQDS RDNCPTVPNS AQEDSDHDGQ GDACDDDDDN DGVPDSRDNC RLVPNPGQED ADRDGVGDVC QDDFDADKVV DKIDVCPENA EVTLTDFRAF QTVVLDPEGD AQIDPNWVVL NQGREIVQTM NSDPGLAVGY TAFNGVDFEG TFHVNTVTDD DYAGFIFGYQ DSSSFYVVMW KQMEQTYWQA NPFRAVAEPG IQLKAVKSST GPGEQLRNAL WHTGDTESQV RLLWKDPRNV GWKDKKSYRW FLQHRPQVGY IRVRFYEGPE LVADSNVVLD TTMRGGRLGV FCFSQENIIW ANLRYRCNDT IPEDYETARG GPEQKLISEE DLNSAVDHHH HHH
Source
CHO
Formulation
Frozen in production medium.
Reconstitution
Defrost at ambient temperature.
Storage, Stability/Shelf Life
Store frozen at –20 °C. Stable until expiry date.
Quality Control Test
SDS-PAGE, ELISA test
Applications
Drug discovery, In vitro diagnostic
References
- Bruyere O, Reginster JY, Seidel L, Henrotin YE, Giacovelli G, Rovati LC, Ethgen O, Collette JH. Biochemical markers of bone and cartilage remodeling in prediction of longterm progression of knee osteoarthritis. J Rheumatol. 2003 May;30 (5):1043-50
- Carter SD, Thompson CC, Clegg PD, Vilim V, Misumi K. Measurement of cartilage oligomeric matrix protein (COMP) in normal and diseased equine synovial fluids. Osteoarthritis Cartilage. 2001 Feb;9 (2):119-27
- Dunky A, Bauer K, Kittl EM, Feyertag J, Haberhauer G, Skoumal M. 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
- Jordan JM, Helmick CG, Hochberg MC, Vilim V, Clark A, Luta G, Renner JB, Kraus VB, Dragomir AD. 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
- Jordan JM, Luta G, Stabler T, Renner JB, Dragomir AD, Vilim V, Hochberg MC, Helmick CG, Kraus VB. 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
- Thonar EJ, Kuettner KE, Pavelka K, Masuda K, Vytasek R, Lenz ME, Vilim V. 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
- Vilim V, Olejarova M, Machacek S, Gatterova J, Kraus VB, Pavelka K. Serum levels of cartilage oligomeric matrix protein (COMP) correlate with radiographic progression of knee osteoarthritis. Osteoarthritis Cartilage. 2002 Sep;10 (9):707-13
- Vilim V, Voburka Z, Senolt L, Vytasek R, Tchetverikov I, Kraus VB, Pavelka K. 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
- Vilim V, Vytasek R, Olejarova M, Machacek S, Gatterova J, Prochazka B, Kraus VB, Pavelka K. 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
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