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The protein encoded by COMP is a noncollagenous extracellular matrix (ECM) protein. Additionally we are shipping COMP Kits (63) and COMP Proteins (21) and many more products for this protein.
Showing 10 out of 123 products:
Human Monoclonal COMP Primary Antibody for EIA, IHC (fro) - ABIN118963
Milz, Sicking, Sprecher, Putz, Benjamin: An immunohistochemical study of the triangular fibrocartilage complex of the wrist: regional variations in cartilage phenotype. in Journal of anatomy 2007
Show all 4 references for ABIN118963
Rat (Rattus) Monoclonal COMP Primary Antibody for EIA, IP - ABIN187632
Newton, Weremowicz, Morton, Copeland, Gilbert, Jenkins, Lawler: Characterization of human and mouse cartilage oligomeric matrix protein. in Genomics 1995
Show all 2 references for ABIN187632
Human Monoclonal COMP Primary Antibody for EIA, IHC (fro) - ABIN187634
Oldberg, Antonsson, Lindblom, Heinegård: COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins. in The Journal of biological chemistry 1992
Show all 2 references for ABIN187634
Human Polyclonal COMP Primary Antibody for WB - ABIN191480
Spitznagel, Nitsche, Paulsson, Maurer, Zaucke: Characterization of a pseudoachondroplasia-associated mutation (His587-->Arg) in the C-terminal, collagen-binding domain of cartilage oligomeric matrix protein (COMP). in The Biochemical journal 2004
Human Polyclonal COMP Primary Antibody for WB - ABIN947722
Clement, Aphkhazava, Nieves, Callaway, Olszewski, Rotzschke, Santambrogio: Protein expression profiles of human lymph and plasma mapped by 2D-DIGE and 1D SDS-PAGE coupled with nanoLC-ESI-MS/MS bottom-up proteomics. in Journal of proteomics 2013
Human Polyclonal COMP Primary Antibody for EIA, WB - ABIN452859
Kim, Lee, Kim: Changes in serum cartilage oligomeric matrix protein (COMP), plasma CPK and plasma hs-CRP in relation to running distance in a marathon (42.195 km) and an ultra-marathon (200 km) race. in European journal of applied physiology 2009
The aims of this study were to investigate the proteomic composition of injured tendons during early and late disease stages to identify disease-specific cleavage patterns of the extracellular matrix protein cartilage oligomeric matrix protein (COMP).
The present results suggest that not only type III collagen (show COL3A1 Antibodies) but also cartilage oligomeric matrix protein is involved in the repair and remodeling processes of the digital flexor tendon.
Within the limitations of the study design, production of COMP during healing of skin wounds does not appear to be influenced by wound type or anatomic site, nor does it appear to be correlated with TGF-beta1 (show TGFB1 Antibodies) concentrations.
COMP concentrations in digital flexor tendon sheath synovial fluid were significantly greater than those in normal horses with noninfected tenosynovitis caused by intrathecal tendon/ligament tearing, but not by other lesions.
The present study indicates that dynamic in vivo compression at high load and frequency lowers matrix content of COMP in the articular cartilage of the third carpal bone.
The expression of COMP in circulation reflects the severity of rheumatoid arthritis.
findings suggest that Cartilage oligomeric matrix protein (COMP) is associated with the stage of liver fibrosis in chronic hepatitis C
The GG genotype of Med23 (show MED23 Antibodies) gene associate with Cognitive Decline and Dementia.
COMP does not directly modify the expression of genes involved in cartilage homeostasis in contrast to several other cartilage matrix proteins.
Overexpression of COMP inhibits BMP-2 (show BMP2 Antibodies)-induced osteogenic differentiation and promotes BMP-2 (show BMP2 Antibodies)-induced chondrogenic differentiation.
Real-time polymerase chain reaction (RT-PCR) assay presented significantly higher (p<0.01) COMP expression of mesenchymal stem cells cultured with HA/COMP multilayered films.
Mutations in specific residues and/or regions of the type III repeats of COMP are significantly associated with either Pseudoachondroplasia or multiple epiphyseal dysplasia.
Serum COMP was not acutely influenced by experimental anterior knee pain during running.
Novel cartilage oligomeric matrix protein (COMP) neoepitopes identified in synovial fluids from patients with joint diseases using affinity chromatography and mass spectrometry.
Variants within the cartilage oligomeric matrix protein (COMP) gene are not associated with Achilles tendinopathy
COMP-Ang1 (show ANGPT1 Antibodies) can enhance BMP2 (show BMP2 Antibodies)-induced cranial bone regeneration with increased pericyte recruitment. Combined delivery of the proteins might be a therapeutic strategy to repair cranial bone damage.
COMP deficiency shortened tail-bleeding and clotting time and accelerated ferric-chloride-induced thrombosis. COMP specifically inhibited thrombin-induced platelet aggregation, activation, and retraction and the thrombin-mediated cleavage of fibrinogen.
COMP immunoreactivity was observed in about half of the investigated plaques from the ApoE (show APOE Antibodies) null mice, mainly located along the intima-medial border. Plaques in the brachiocephalic artery from ApoE (show APOE Antibodies) mice lacking COMP were increased in size with 54%.
study will facilitate better awareness of the differential diagnoses that might be associated with the PSACH/MED spectrum and subsequent care of PSACH/MED patients
The lack of arthritis, together with high levels of COMP-specific antibodies, in COMP-deficient mice indicates that susceptibility to arthritis is COMP specific and that endogenous expression of COMP in wild-type mice tolerizes B cells in vivo.
results imply that COMP is not a key upstream mediator of the anabolic effects of ML on the skeleton.
Lack of COMP and matrilin 3 (show MATN3 Antibodies) leads to increased deposition of TIMP-3 (show TIMP3 Antibodies), which causes partial inactivation of matrix metalloproteinases in bone, including MMP-13 (show MMP13 Antibodies).
A novel form of chondrocyte stress triggered by the expression of a human-like mutation in COMP is central to the pathogenesis of pseudoachondroplasia.
reducing steady state levels of COMP mRNA alleviates intracellular retention of other extracellular matrix proteins associated with the pseudoachondroplasia cellular pathology
Data show that cartilage oligomeric matrix protein (COMP) promotes cell attachment via independent mechanisms involving cell surface CD47 (show CD47 Antibodies) and alphaVbeta3 integrin and that cell attachment to COMP induces formation of fascin (show FSCN1 Antibodies)-stabilized actin microspikes.
COMP synthesis is differentially regulated by TGFbeta1 (show TGFB1 Antibodies) in the surface and middle zones of bovine articular cartilage.
role for proteinases other than MMPs in the degradation of COMP in cartilage
COMP mutant expression in tendon fibroblasts leads to increased apoptotic cell death irrespective of the secretory characteristics of mutant COMP
COMP mRNA expression level was markedly increased by ball oscillation.
COMP acts as a catalyst in collagen fibrillogenesis.
The protein encoded by this gene is a noncollagenous extracellular matrix (ECM) protein. It consists of five identical glycoprotein subunits, each with EGF-like and calcium-binding (thrombospondin-like) domains. Oligomerization results from formation of a five-stranded coiled coil and disulfides. Binding to other ECM proteins such as collagen appears to depend on divalent cations. Mutations can cause the osteochondrodysplasias pseudochondroplasia (PSACH) and multiple epiphyseal dysplasia (MED).
cartilage oligomeric matrix protein
, cartilage oligomeric matrix protein (pseudoachondroplasia, epiphyseal dysplasia 1, multiple)
, cartilage oligomeric matrix protein(pseudoachondroplasia, epiphyseal dysplasia 1, multiple)
, pseudoachondroplasia (epiphyseal dysplasia 1, multiple)
, putative cartilage oligomeric matrix protein