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The protein encoded by COMP is a noncollagenous extracellular matrix (ECM) protein. Additionally we are shipping COMP Antibodies (125) and COMP Kits (57) and many more products for this protein.
Showing 10 out of 22 products:
Human COMP Protein expressed in Human Cells - ABIN2002240
Newton, Weremowicz, Morton, Copeland, Gilbert, Jenkins, Lawler: Characterization of human and mouse cartilage oligomeric matrix protein. in Genomics 1995
Show all 5 references for ABIN2002240
Human COMP Protein expressed in HEK-293 Cells - ABIN2180897
Chen, Thomas, Hecht, Goldring, Lawler: Cartilage oligomeric matrix protein/thrombospondin 5 supports chondrocyte attachment through interaction with integrins. in The Journal of biological chemistry 2005
Show all 2 references for ABIN2180897
Rat (Rattus) COMP Protein expressed in - ABIN1047991
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
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 Proteins) 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 Proteins) 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.
In the absence of ultrasonographic knee cartilage deformation, the response of serum lubricin (show PRG4 Proteins) and COMP following acute vigorous exercise indicates an increase in joint lubrication and cartilage metabolism, respectively, which appears largely independent of exercise modality.
Running appears to decrease knee intra-articular pro-inflammatory cytokine concentration and facilitates the movement of COMP from the joint space to the serum.
Results suggest that serum oligomeric matrix protein and hyaluronic acid (COMP and HA) concentrations can be used to predict early cartilage lesions in the knee.
Serum COMP levels are predictive of subsequent structural changes and incidence of painful knee osteoarthritis.
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 Proteins) 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 Proteins)-induced osteogenic differentiation and promotes BMP-2 (show BMP2 Proteins)-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.
COMP forms a complex with collagens intracellularly that is a prerequisite for collagen secretion.
COMP-Ang1 (show ANGPT1 Proteins) can enhance BMP2 (show BMP2 Proteins)-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 Proteins) null mice, mainly located along the intima-medial border. Plaques in the brachiocephalic artery from ApoE (show APOE Proteins) 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 Proteins) leads to increased deposition of TIMP-3 (show TIMP3 Proteins), which causes partial inactivation of matrix metalloproteinases in bone, including MMP-13 (show MMP13 Proteins).
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
COMP synthesis is differentially regulated by TGFbeta1 (show TGFB1 Proteins) 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