POLYCLONAL ANTIBODY For research use only, Not for diagnostic use. Catalog No. PRPG-CPF-M02 Anti COMP Fragment (2127F5) [Cartilage Oligomeric Matrix Protein ]

BACKGROUND COMP - Cartilage oligomeric matrix protein - belongs to the thrombospondin family of ECM components and is a prominent multidomain glycoprotein of cartilage, accounting for up to 1% of the wet weight of articular tissues and having an approximate Mr of 97 kDa [1-4]. COMP may also be found in tendon, bone (i.e. ), ligament, certain smooth muscles and synovium and more recently has been discovered to be a primary constituents of the dermal ECM [5]. In the ECM COMP is present in a pentameric, disulfide-bonded complex of an Mr of about 550 kDa, often seen associated with the cell surface [3, 5]..＊

Product type Primary antibodies Immunogen Recombinant EGF domain of human COMP Host Species Mouse Fusion Partner - Clone Designation 2127F5 Isotype IgG1 Host - Source Hybridoma cell culture Purification - Form Liquid

Formulation Buffer Supernatant supplemented with 0.05% NaN3 Concentration ND Volume 2 mL Label Unlabeled Specificity COMP (Cartilage Oligomeric Matrix Protein) Cross species reactivity Human, Other species have not been tested. Storage Conditions Store at 4°C for short-term storage and -20°C for prolonged storage Aliquot to avoid cycles of freeze / thaw. Other Data Link : UniProtKB/Swiss-Prot P49747 (COMP_HUMAN)

Application notes ・ Western blotting, 1/20 - 1/40* Recommended dilutions ・ Immunohistochemistry, 1/20 - 1/30 (Paraffin sections)

Optimal dilutions/concentrations should be determined by the end user.

References 1) Oldberg A, et all., J Biol Chem. 1992 Nov 5;267(31):22346-50. PMID: 1429587 2) Hedbom E, et all., J Biol Chem. 1992 Mar 25;267(9):6132-6.. PMID: 1556121 3) Morgelin M, et all., J Biol Chem. 1992 Mar 25;267(9):6137-41.PMID: 1556122 4) Cesare PE, et all., J Orthop Res. 1995 May;13(3):422-8.. PMID: 7602403 5) Agarwal P, et all., J Biol Chem. 2012 Jun 29;287(27):22549-59. PMID: 22573329

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Anti- COMP Fragment (2117B2) Ab Cat#:PRPG-CPF-M01 1/3 Version#: 1-130821

ANTIBODY CHARACTERIZATION

19 ‐

11 ‐ 9 ‐

5 ‐

Left panel: Western blotting on recombinant COMP produced in HEK293 cells after SDS-PAGE under reducing conditions on 8% gels. Lanes 1 and 2 from left show secreted and cell-bound COMP, whereas the two adjacent lanes show the controls. Right panels: immunohistochemical stainings of human articular cartilage at lower (left) and higher magnification (right).

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Anti- COMP Fragment (2117B2) Ab Cat#:PRPG-CPF-M01 2/3 Version#: 1-130821 ＊< BACKGROUND : COMP Fragment > COMP - Cartilage oligomeric matrix protein - belongs to the thrombospondin family of ECM components and is a prominent multidomain glycoprotein of cartilage, accounting for up to 1% of the wet weight of articular tissues and having an approximate Mr of 97 kDa [1-4]. COMP may also be found in tendon, bone (i.e. osteoblasts), ligament, certain smooth muscles and synovium and more recently has been discovered to be a primary constituents of the dermal ECM [5]. In the ECM COMP is present in a pentameric, disulfide-bonded complex of an Mr of about 550 kDa, often seen associated with the chondrocyte cell surface [3, 5]. Although the function of COMP is not completely elucidated, it appears to mediate chondrocyte attachment via integrins and to stabilize the articular cartilage ECM via specific Ca2+/Zn2+-dependent interactions with collagen types II and IX, aggrecan, fibronectin, matrilins and ECM protein 1. In addition, mutations in the human COMP gene have been linked to the development of pseudoachondroplasia and multiple epiphyseal dysplasia [8-14], which are autosomal-dominant forms of short-limb . In of these patients, COMP remains frequently entrapped in intracellular vescicles. COMP is a substrate for a variety of ECM degrading enzymes, including MMP-1, MMP-13, MMP-19, MMP20 and ADAMTS-4, -7 and -12. Fragments of COMP have been detected in the diseased cartilage, synovial fluid, and serum of patients with knee injuries, post-traumatic and primary osteoarthritis and rheumatoid arthritis and have proposed to be diagnostic/prognostic of degenerative cartilage diseases [15-18]. This has led the development of serological/body fluid assays for the quantitative monitoring of circulating levels of COMP and its degradation products [19].

1.Oldberg A, Antonsson P, Lindblom K, Heinegård D. 1992. COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins. J Biol Chem 267, 22346-22350. 2.Hedbom E, Antonsson P, Hjerpe A, Aeschlimann D, Paulsson M, Rosa-Pimentel E, Sommarin Y, Wendel M, Oldberg A, Heinegård D. 1992. Cartilage matrix proteins. An acidic oligomeric protein (COMP) detected only in cartilage. J Biol Chem 267, 6132-6136. 3.Mörgelin M, Heinegård D, Engel J, Paulsson M. 1992. Electron microscopy of native cartilage oligomeric matrix protein purified from the Swarm rat chondrosarcoma reveals a five-armed structure. J Biol Chem 267, 6137-6141. 4.Di Cesare PE, Mörgelin M, Carlson CS, Pasumarti S, Paulsson M. 1995. Cartilage oligomeric matrix protein: isolation and characterization from human articular cartilage. J Orthop Res 13, 422-428. 5.Agarwal P, Zwolanek D, Keene DR, Schulz JN, Blumbach K, Heinegård D, Zaucke F, Paulsson M, Krieg T, Koch M, Eckes B. 2012. Collagen XII and XIV, new partners of cartilage oligomeric matrix protein in the skin suprastructure. J Biol Chem 287, 22549-22559. 6.Agarwal P, Schulz JN, Blumbach K, Andreasson K, Heinegård D, Paulsson M, Mauch C, Eming SA, Eckes B, Krieg T. 2013. Enhanced deposition of cartilage oligomeric matrix protein is a common feature in fibrotic skin pathologies. Matrix Biol. [Epub ahead of print]. 7.Fife RS, Kluve-Beckerman B, Houser DS, Proctor C, Liepnieks J, Masuda I, McCarty DJ, Ryan LM. 1993. Evidence that a 550,000-dalton cartilage matrix glycoprotein is a chondrocyte membrane-associated protein closely related to ceruloplasmin. J Biol Chem 268, 4407-4411. 8.Stanescu V, Do TP, Chaminade F, Maroteaux P, Stanescu R. 1994. Non-collagenous protein screening in the human chondrodysplasias: link proteins, cartilage oligomeric matrix protein (COMP), and fibromodulin. Am J Med Genet 51, 22-28. 9.Hecht JT, Nelson LD, Crowder E, Wang Y, Elder FF, Harrison WR, Francomano CA, Prange CK, Lennon GG, Deere M, et al. 1995. Mutations in exon 17B of cartilage oligomeric matrix protein (COMP) cause pseudoachondroplasia. Nat Genet 10, 325-329. 10.Briggs MD, Hoffman SM, King LM, Olsen AS, Mohrenweiser H, Leroy JG, Mortier GR, Rimoin DL, Lachman RS, Gaines ES, et al. 1995. Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene. Nat Genet. 10, 330-336. 11.Mabuchi A, Haga N, Ikeda T, Manabe N, Ohashi H, Takatori Y, Nakamura K, Ikegawa S. 2001. Novel mutation in exon 18 of the cartilage oligomeric matrix protein gene causes a severe pseudoachondroplasia. Am J Med Genet 104, 135-139. 12.Thur J, Rosenberg K, Nitsche DP, Pihlajamaa T, Ala-Kokko L, Heinegård D, Paulsson M, Maurer P. 2001. Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX. J Biol Chem 276, 6083-6092. 13.Cao LH, Wang LB, Wang SS, Ma HW, Ji CY, Luo Y. 2011. Identification of novel and recurrent mutations in the calcium binding type III repeats of cartilage oligomeric matrix protein in patients with pseudoachondroplasia. Genet Mol Res 10, 955-963. 14.Posey KL, Veerisetty AC, Liu P, Wang HR, Poindexter BJ, Bick R, Alcorn JL, Hecht JT. 2009. An inducible cartilage oligomeric matrix protein mouse model recapitulates human pseudoachondroplasia phenotype. Am J Pathol 175, 1555-1563. 15.Vilím V, Olejárová M, Machácek S, Gatterová J, Kraus VB, Pavelka K. 2002. Serum levels of cartilage oligomeric matrix protein (COMP) correlate with radiographic progression of knee osteoarthritis. Osteoarthritis Cartilage 10, 707-713. 16.Tseng S, Reddi AH, Di Cesare PE. 2009. Cartilage Oligomeric Matrix Protein (COMP): A Biomarker of Arthritis. Biomark Insights 4:33-44. 17…Hoch JM, Mattacola CG, Medina McKeon JM, Howard JS, Lattermann C. 2011. Serum cartilage oligomeric matrix protein (sCOMP) is elevated in patients with knee osteoarthritis: a systematic review and meta-analysis. Osteoarthritis Cartilage 19, 1396-1404. 18.Verma P, Dalal K. 2013. Serum cartilage oligomeric matrix protein (COMP) in knee osteoarthritis: a novel diagnostic and prognostic biomarker. J Orthop Res 31, 999-1006. 19.Lai Y, Yu XP, Zhang Y, Tian Q, Song H, Mucignat MT, Perris R, Samuels J, Krasnokutsky S, Attur M, Greenberg JD, Abramson SB, Di Cesare PE, Liu CJ. 2012. Enhanced COMP catabolism detected in serum of patients with arthritis and animal disease models through a novel capture ELISA. Osteoarthritis Cartilage 20, 854-862

*References relative to this antibody are underlined.

For research use only, Not for diagnostic use.

TOYO 2CHOME, KOTO-KU, TOKYO, 135-0016, JAPAN URL: http://www.cosmobio.co.jp e-mail: [email protected] [Outside Japan] Phone : +81-3-5632-9617 [国内連絡先] Phone : +81-3-5632-9610 FAX : +81-3-5632-9613 FAX : +81-3-5632-9619

Anti- COMP Fragment (2117B2) Ab Cat#:PRPG-CPF-M01 3/3 Version#: 1-130821