Cartilage Oligomeric Matrix Protein (pseudoachondroplasia epiphyseal dysplasia 1 multiple), MED, THBS5, TSP5, EDM1, PSACH, EPD1, Thrombospondin-5.
COMP is a non-collagenous glycoprotein and is belongs to the thrombospondin family of extracellular proteins. COMP is a calcium-binding protein of high molecular weight (>500kDa) found in the extracellular matrix of articular, nasal and tracheal cartilage. COMP is not only cartilage-derived but is common in other tissues, such as synovium and tendon. Intact COMP is pentameric, with five equal subunits and the carboxy-terminal globular domain of native COMP binds to collagens I, II, and IX. COMP molecules are vital for conserving the properties and integrity of collagen network. Moreover COMP has a storage and delivery function for hydrophobic cellsignaling molecules such as vitamin D. Mutations of the COMP gene cause Pseudoachondroplasia and some forms of multiple epiphyseal dysplasia which implicates that it is vital that COMP develops and functions normally. It is a well-known fact that serum levels of COMP offer essential data about metabolic changes taking place in the cartil
COMP HEK Protein is a 82.4 kDa protein containing 750 aa fused to a 13 aa N-Terminal
COMP HEK Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 20mM TRIS and 50mM NaCl, pH 7.5
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
Store lyophilized COMP HEK Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted COMP HEK can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Amino acid sequence
HVDYKDDDDK PAGQGQSPLG SDLGPQMLRE LQETNAALQD VRELLRQQVR EITFLKNTVM ECDACGMQQS VRTGLPSVRP LLHCAPGFCF PGVACIQTES GARCGPCPAG FTGNGSHCTD VNECNAHPCF PRVRCINTSP GFRCEACPPG YSGPTHQGVG LAFAKANKQV CTDINECETG QHNCVPNSVC INTRGSFQCG PCQPGFVGDQ ASGCQRRAQR FCPDGSPSEC HEHADCVLER DGSRSCVCAV GWAGNGILCG RDTDLDGFPD EKLRCPERQC RKDNCVTVPN SGQEDVDRDG IGDACDPDAD GDGVPNEKDN CPLVRNPDQR NTDEDKWGDA CDNCRSQKND DQKDTDQDGR GDACDDDIDG DRIRNQADNC PRVPNSDQKD SDGDGIGDAC DNCPQKSNPD QADVDHDFVG DACDSDQDQD GDGHQDSRDN CPTVPNSAQE DSDHDGQGDA CDDDDDNDGV PDSRDNCRLV PNPGQEDADR DGVGDVCQDD FDADKVVDKI DVCPENAEVT LTDFRAFQTV VLDPEGDAQI DPNWVVLNQG REIVQTMNSD PGLAVGYTAF NGVDFEGTFH VNTVTDDDYA GFIFGYQDSS SFYVVMWKQM EQTYWQANPF RAVAEPGIQL KAVKSSTGPG EQLRNALWHT GDTESQVRLL WKDPRNVGWK DKKSYRWFLQ HRPQVGYIRV RFYEGPELVA DSNVVLDTTM RGGRLGVFCF SQENIIWANL RYRCNDTIPE DYETHQLRQA
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