Cartilage Oligomeric Matrix Protein Human HEK293

Cat. No.	Size	Price 1 - 4 pcs / 5 - 9 pcs / 10+ pcs
RD172080100	0.1 mg	$421 / $370 / On request

Technical Data

Type

Recombinant protein

Description

Total 750 AA. MW: 82.4 kDa (calculated). UniProtKB acc.no. P49747. N-Terminal FLAG-tag, 13 extra AA. Protein identity confirmed by MS.

Amino Acid Sequence

HVDYKDDDDKPAGQGQSPLGSDLGPQMLRELQETNAALQDVRELLRQQVREITFLKNTVMECDACGMQQSVRTGLPSVRPLLHCAPGFCFPGVACIQTESGARCGPCPAGFTGNGSHCTDVNECNAHPCFPRVRCINTSPGFRCEACPPGYSGPTHQGVGLAFAKANKQVCTDINECETGQHNCVPNSVCINTRGSFQCGPCQPGFVGDQASGCQRRAQRFCPDGSPSECHEHADCVLERDGSRSCVCAVGWAGNGILCGRDTDLDGFPDEKLRCPERQCRKDNCVTVPNSGQEDVDRDGIGDACDPDADGDGVPNEKDNCPLVRNPDQRNTDEDKWGDACDNCRSQKNDDQKDTDQDGRGDACDDDIDGDRIRNQADNCPRVPNSDQKDSDGDGIGDACDNCPQKSNPDQADVDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQEDSDHDGQGDACDDDDDNDGVPDSRDNCRLVPNPGQEDADRDGVGDVCQDDFDADKVVDKIDVCPENAEVTLTDFRAFQTVVLDPEGDAQIDPNWVVLNQGREIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTVTDDDYAGFIFGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDTESQVRLLWKDPRNVGWKDKKSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTTMRGGRLGVFCFSQENIIWANLRYRCNDTIPEDYETHQLRQA

Source

HEK293

Purity

˃ 90 % by SDS-PAGE

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/µg

Formulation

Filtered (0.4 μm) and lyophilized from 0.5 mg/mL solution in 20 mM Tris buffer, 50 mM 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.

Applications

Western blotting, ELISA

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the lyophilized protein at -80 °C. Lyophilized protein remains stable until the expiry date when stored at -80 °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 week.

Quality Control Test

BCA to determine quantity of the protein.
SDS PAGE to determine purity of the protein. Endotoxin level determination.

Physical Appearance

White lyophilized (freeze-dried) powder.

Note

This product is intended for research use only.

Summary

Research topic

Atherosclerosis, Bone and cartilage metabolism, Cardiovascular disease, Extracellular matrix, Pulmonary diseases

Summary

Cartilage oligomeric matrix protein (COMP), also designated thrombospondin 5 (TSP 5), is a 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 cell-signaling 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 pseudoachondro¬plasia 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 common diseases causing pain and disability in a significant proportion of the adult population and early diagnostics of these diseases is very important for future therapy.

COMP, abundant in cartilage, is now known to be also expressed in tumor tissues from breast, prostate, and colon cancer. Studies have concluded that COMP in breast cancer cells is correlated with poor survival and higher recurrence rates in patients. Elevated levels of COMP in sera can be detected in metastatic breast cancer patients compared with those in early stages of the disease. Additionally, serum COMP could potentially be an independent prognostic marker for metastatic patients. Similarly, studies have shown that COMP expression in prostate cancer correlated with enhanced invasion and with a more progressive disease. Likewise, COMP expression has been correlated with the poor outcome of colon cancer patients. COMP levels in the sera of preoperative patients with colon cancer were much higher than those in healthy donors and were significantly reduced after colectomy. Thus, COMP may be a novel prognostic indicator and biomarker and also a potential therapeutic target for colon cancer.

Increased COMP has been associated with fibrogenesis in systemic sclerosis, skin keloids, vascular atherosclerosis, lung fibrosis, and chronic pancreatitis. Studies have also suggested that COMP contributes to liver fibrosis by regulating collagen-I deposition, with further investigation finding that serum COMP levels could be used as a non-invasive liver fibrosis marker in patients with chronic viral hepatitis (CVH). There is evidence that COMP plays a role in pathogenesis of idiopathic pulmonary fibrosis (IPF) and should be further evaluated as a biomarker for disease activity in IPF.

There is evidence that COMP is essential for maintaining vascular homeostasis, and is an endogenous thrombin inhibitor and negative regulator of hemostasis and thrombosis. Research suggests a pathogenetic role of COMP the development of vascular fibrosis and calcification, and thus COMP may be a novel target in therapy of a number of vascular diseases.

Summary References (23)

References to Cartilage Oligomeric Matrix Protein

Agarwal P, Schulz JN, Blumbach K, Andreasson K, Heinegård D, Paulsson M, Mauch C, Eming SA, Eckes B, Krieg T. Enhanced deposition of cartilage oligomeric matrix protein is a common feature in fibrotic skin pathologies. Matrix Biol. 2013 Aug 8;32(6):325-31. doi: 10.1016/j.matbio.2013.02.010. Epub 2013 Mar 15. PMID: 23507196. See more on PubMed
Bruyere O, Collette JH, Ethgen O, Rovati LC, Giacovelli G, Henrotin YE, SeidelL, Reginster JY. Biochemical markers of bone and cartilage remodeling inprediction of longterm progression of knee osteoarthritis. J Rheumatol. 2003May;30(5):1043-50. PubMed PMID: 12734904. See more on PubMed
Canfield AE, Farrington C, Dziobon MD, Boot-Handford RP, Heagerty AM, Kumar SN, Roberts IS. The involvement of matrix glycoproteins in vascular calcification and fibrosis: an immunohistochemical study. J Pathol. 2002 Feb;196(2):228-34. doi: 10.1002/path.1020. PMID: 11793375. See more on PubMed
Dragomir AD, Kraus VB, Renner JB, Luta G, Clark A, Vilim V, Hochberg MC,Helmick CG, Jordan JM. Serum cartilage oligomeric matrix protein and clinicalsigns and symptoms of potential pre-radiographic hip and knee pathology.Osteoarthritis Cartilage. 2002 Sep;10(9):687-91. PubMed PMID: 12202121. See more on PubMed
Englund E, Bartoschek M, Reitsma B, Jacobsson L, Escudero-Esparza A, Orimo A, Leandersson K, Hagerling C, Aspberg A, Storm P, Okroj M, Mulder H, Jirström K, Pietras K, Blom AM. Cartilage oligomeric matrix protein contributes to the development and metastasis of breast cancer. Oncogene. 2016 Oct 27;35(43):5585-5596. doi: 10.1038/onc.2016.98. Epub 2016 Apr 11. PMID: 27065333. See more on PubMed
Englund E, Canesin G, Papadakos KS, Vishnu N, Persson E, Reitsma B, Anand A, Jacobsson L, Helczynski L, Mulder H, Bjartell A, Blom AM. Cartilage oligomeric matrix protein promotes prostate cancer progression by enhancing invasion and disrupting intracellular calcium homeostasis. Oncotarget. 2017 Sep 21;8(58):98298-98311. doi: 10.18632/oncotarget.21176. PMID: 29228690; PMCID: PMC5716730. See more on PubMed
Farina G, Lemaire R, Korn JH, Widom RL. Cartilage oligomeric matrix protein is overexpressed by scleroderma dermal fibroblasts. Matrix Biol. 2006 May;25(4):213-22. doi: 10.1016/j.matbio.2006.01.007. Epub 2006 Mar 7. PMID: 16520029. See more on PubMed
Inui S, Shono F, Nakajima T, Hosokawa K, Itami S. Identification and characterization of cartilage oligomeric matrix protein as a novel pathogenic factor in keloids. Am J Pathol. 2011 Oct;179(4):1951-60. doi: 10.1016/j.ajpath.2011.06.034. Epub 2011 Aug 26. PMID: 21872564; PMCID: PMC3181360. See more on PubMed
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 cartilageoligomeric matrix protein: the Johnston County Osteoarthritis Project. Arthritis Rheum. 2003 Mar;48(3):675-81. PubMed PMID: 12632420. See more on PubMed
Liang Y, Fu Y, Qi R, Wang M, Yang N, He L, Yu F, Zhang J, Yun CH, Wang X, Liu J, Kong W. Cartilage oligomeric matrix protein is a natural inhibitor of thrombin. Blood. 2015 Aug 13;126(7):905-14. doi: 10.1182/blood-2015-01-621292. Epub 2015 Jun 4. PMID: 26045608. See more on PubMed
Liao Q, Kleeff J, Xiao Y, Di Cesare PE, Korc M, Zimmermann A, Büchler MW, Friess H. COMP is selectively up-regulated in degenerating acinar cells in chronic pancreatitis and in chronic-pancreatitis-like lesions in pancreatic cancer. Scand J Gastroenterol. 2003 Feb;38(2):207-15. doi: 10.1080/00365520310000717. PMID: 12678339. See more on PubMed
Liu TT, Liu XS, Zhang M, Liu XN, Zhu FX, Zhu FM, Ouyang SW, Li SB, Song CL, Sun HM, Lu S, Zhang Y, Lin J, Tang HM, Peng ZH. Cartilage oligomeric matrix protein is a prognostic factor and biomarker of colon cancer and promotes cell proliferation by activating the Akt pathway. J Cancer Res Clin Oncol. 2018 Jun;144(6):1049-1063. doi: 10.1007/s00432-018-2626-4. Epub 2018 Mar 20. PMID: 29560517. See more on PubMed
Magdaleno F, Arriazu E, Ruiz de Galarreta M, Chen Y, Ge X, Conde de la Rosa L, Nieto N. Cartilage oligomeric matrix protein participates in the pathogenesis of liver fibrosis. J Hepatol. 2016 Nov;65(5):963-971. doi: 10.1016/j.jhep.2016.06.003. Epub 2016 Jun 15. PMID: 27318326; PMCID: PMC5831373. See more on PubMed
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. PubMed PMID: 11237659. See more on PubMed
Papadakos KS, Bartoschek M, Rodriguez C, Gialeli C, Jin SB, Lendahl U, Pietras K, Blom AM. Cartilage Oligomeric Matrix Protein initiates cancer stem cells through activation of Jagged1-Notch3 signaling. Matrix Biol. 2019 Aug;81:107-121. doi: 10.1016/j.matbio.2018.11.007. Epub 2018 Nov 28. PMID: 30502484. See more on PubMed
Papadakos KS, Darlix A, Jacot W, Blom AM. High Levels of Cartilage Oligomeric Matrix Protein in the Serum of Breast Cancer Patients Can Serve as an Independent Prognostic Marker. Front Oncol. 2019 Oct 30;9:1141. doi: 10.3389/fonc.2019.01141. PMID: 31737569; PMCID: PMC6831625. See more on PubMed
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 Sjögren's syndrome. Arthritis Res Ther. 2004;6(2):73-4. doi: 10.1186/ar1161. Epub 2004 Mar 8. PMID: 15059267; PMCID: PMC400441. See more on PubMed
Vilim V, Lenz ME, Vytasek R, Masuda K, Pavelka K, Kuettner KE, Thonar EJ.Characterization of monoclonal antibodies recognizing different fragments ofcartilage oligomeric matrix protein in human body fluids. Arch Biochem Biophys.1997 May 1;341(1):8-16. PubMed PMID: 9143347. See more on PubMed
Vilím V, Olejárová M, Machácek S, Gatterová J, Kraus VB, Pavelka K. Serumlevels of cartilage oligomeric matrix protein (COMP) correlate with radiographic progression of knee osteoarthritis. Osteoarthritis Cartilage. 2002Sep;10(9):707-13. PubMed PMID: 12202123. See more on PubMed
Vilím V, Vobůrka Z, Vytásek R, Senolt L, Tchetverikov I, Kraus VB, Pavelka K. Monoclonal antibodies to human cartilage oligomeric matrix protein: epitopemapping and characterization of sandwich ELISA. Clin Chim Acta. 2003Feb;328(1-2):59-69. PubMed PMID: 12559599. See more on PubMed
Vilím V, Vytásek R, Olejárová M, Machácek S, Gatterová J, Procházka B, KrausVB, Pavelka K. Serum cartilage oligomeric matrix protein reflects the presence ofclinically diagnosed synovitis in patients with knee osteoarthritis.Osteoarthritis Cartilage. 2001 Oct;9(7):612-8. PubMed PMID: 11597173. See more on PubMed
Vuga LJ, Milosevic J, Pandit K, Ben-Yehudah A, Chu Y, Richards T, Sciurba J, Myerburg M, Zhang Y, Parwani AV, Gibson KF, Kaminski N. Cartilage oligomeric matrix protein in idiopathic pulmonary fibrosis. PLoS One. 2013 Dec 20;8(12):e83120. doi: 10.1371/journal.pone.0083120. PMID: 24376648; PMCID: PMC3869779. See more on PubMed
Zachou K, Gabeta S, Shums Z, Gatselis NK, Koukoulis GK, Norman GL, Dalekos GN. COMP serum levels: A new non-invasive biomarker of liver fibrosis in patients with chronic viral hepatitis. Eur J Intern Med. 2017 Mar;38:83-88. doi: 10.1016/j.ejim.2017.01.007. Epub 2017 Jan 15. PMID: 28100410. See more on PubMed

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