Mouse Cartilage oligomeric matrix protein(COMP) ELISA kit

Instructions
Code CSB-EL005778MO
Size 96T,5×96T,10×96T
See More Details 24T ELISA kits trial application
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Product Details

Target Name cartilage oligomeric matrix protein
Alternative Names CompCartilage oligomeric matrix protein ELISA kit; COMP ELISA kit
Abbreviation COMP
Uniprot No. Q9R0G6
Species Mus musculus (Mouse)
Sample Types serum, plasma, tissue homogenates
Detection Range 6.25 ng/mL-400 ng/mL
Sensitivity 1.56 ng/mL
Assay Time 1-5h
Sample Volume 50-100ul
Detection Wavelength 450 nm
Research Area Cell Biology
Assay Principle quantitative
Measurement Sandwich
Precision
Intra-assay Precision (Precision within an assay): CV%<8%
Three samples of known concentration were tested twenty times on one plate to assess.
Inter-assay Precision (Precision between assays): CV%<10%
Three samples of known concentration were tested in twenty assays to assess.
Linearity
To assess the linearity of the assay, samples were spiked with high concentrations of mouse COMP in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay.
SampleSerum(n=4)
1:1Average %91
Range %86-95
1:2Average %102
Range %97-107
1:4Average %91
Range %85-97
1:8Average %97
Range %91-103
Recovery
The recovery of mouse COMP spiked to levels throughout the range of the assay in various matrices was evaluated. Samples were diluted prior to assay as directed in the Sample Preparation section.
Sample TypeAverage % RecoveryRange
Serum (n=5) 9589-98
EDTA plasma (n=4)9790-100
Typical Data
These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.
ng/mlOD1OD2AverageCorrected
4002.512 2.600 2.556 2.370
2001.680 1.571 1.626 1.440
1000.955 0.962 0.959 0.773
500.576 0.561 0.569 0.383
250.394 0.384 0.389 0.203
12.50.313 0.324 0.319 0.133
6.250.259 0.264 0.262 0.076
00.187 0.185 0.186
Troubleshooting
and FAQs
ELISA kit FAQs
Storage Store at 2-8°C. Please refer to protocol.
Lead Time 5-7 working days

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Target Data

Function May play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP). Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 (By similarity).
Gene References into Functions
  1. COMP could normally have a protective role against PASMC phenotype switching PMID: 28860005
  2. these findings revealed the essential role of COMP in retarding the development of vascular aging and vascular smooth muscle cell senescence. PMID: 27498005
  3. COMP deficiency drove macrophages toward the atherogenic phenotype and thereby aggravated atherosclerotic calcification. PMID: 27151399
  4. COMP forms a complex with collagens intracellularly that is a prerequisite for collagen secretion. PMID: 26746240
  5. The accumulation and thereby the functionality of thrombospondin in extracellular matrix is controlled by concentration-dependent, intermolecular "matrix trapping" mechanism. PMID: 25995382
  6. 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. PMID: 26045608
  7. COMP immunoreactivity was observed in about half of the investigated plaques from the ApoE null mice, mainly located along the intima-medial border. Plaques in the brachiocephalic artery from ApoE mice lacking COMP were increased in size with 54%. PMID: 25133350
  8. 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 PMID: 24312420
  9. 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. PMID: 23754310
  10. results imply that COMP is not a key upstream mediator of the anabolic effects of ML on the skeleton. PMID: 23098652
  11. Lack of COMP and matrilin 3 leads to increased deposition of TIMP-3, which causes partial inactivation of matrix metalloproteinases in bone, including MMP-13. PMID: 22378539
  12. A novel form of chondrocyte stress triggered by the expression of a human-like mutation in COMP is central to the pathogenesis of pseudoachondroplasia. PMID: 22006726
  13. reducing steady state levels of COMP mRNA alleviates intracellular retention of other extracellular matrix proteins associated with the pseudoachondroplasia cellular pathology PMID: 20421976
  14. Data show that cartilage oligomeric matrix protein (COMP) promotes cell attachment via independent mechanisms involving cell surface CD47 and alphaVbeta3 integrin and that cell attachment to COMP induces formation of fascin-stabilized actin microspikes. PMID: 20033473
  15. Cartilage oligomeric matrix protein-deficient mice have normal skeletal development. PMID: 12024046
  16. Comp was expressed in tendon clone cells. PMID: 12837285
  17. Negative regulation of transcription is an important mechanism for chondrocyte-specific expression of the COMP gene PMID: 15183430
  18. ADAMTS-7 is the first metalloproteinase found to bind directly to and degrade COMP PMID: 16585064
  19. COMP appears to be required for granulin PC cell-derived growth factor-mediated chondrocyte proliferation PMID: 17307734
  20. a mutation in the C-terminal domain of COMP exerts a dominant-negative effect on both intra- and extracellular processes. PMID: 17588960
  21. contribution of COMP to the phenotype of mice deficient in both collagen IX and COMP appears minor, even though clear differences in the deposition of matrilin-3 were detected PMID: 18191556
  22. COMP-deficient mice develop an early onset collagen-induced arthritis and more severe arthritis during the chronic phase. PMID: 19014566

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Subcellular Location Secreted, extracellular space, extracellular matrix
Protein Families Thrombospondin family
Tissue Specificity Expressed only in cartilage, including nasal, knee epiphyseal and rib tissues.
Database Links

KEGG: mmu:12845

STRING: 10090.ENSMUSP00000003659

UniGene: Mm.45071

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